# Patent

## Title
Nucleic acid and amino acid sequences relating to Streptococcus pneumoniae for diagnostics and therapeutics

## Abstract

The invention provides isolated polypeptide and nucleic acid sequences derived from Streptococcus pneumoniae that are useful in diagnosis and therapy of pathological conditions; antibodies against the polypeptides; and methods for the production of the polypeptides. The invention also provides methods for the detection, prevention and treatment of pathological conditions resulting from bacterial infection.

## Background
RELATED APPLICATIONS
This application is a continuation of U.S. application Ser. No. 10/640,833, filed Aug. 14, 2003 now abandoned, which is a continuation of U.S. application Ser. No. 09/583,110 (now U.S. Pat. No. 6,699,703) filed May 26, 2000, which is a continuation-in-part of U.S. application Ser. No. 09/107,433 (now U.S. Pat. No. 6,800,744), filed Jun. 30, 1998, which claims the benefit of U.S. Applications No. 60/085,131, filed May 12, 1998 and of U.S. Application No. 60/051,553, filed Jul. 2, 1997. The entire teachings of the above applications are incorporated herein by reference.


INCORPORATION BY REFERENCE OF MATERIAL ON COMPACT DISK
This application incorporates by reference the Sequence Listing contained on the two compact disks (Copy 1 and Copy 2), filed concurrently herewith, containing the following file:
File name: 3687.1000-009SequenceList.txt; created Dec. 27, 2004, 8,134 KB in size.
This application also incorporates by reference Table 2 contained on the two compact disks (Copy 1 and Copy 2), filed concurrently herewith, containing the following file:
File name: 521614—1.txt; created Dec. 23, 2004, 351 KB in size.












TABLES


The patent contains table(s) that have been included at the end of the specification.









FIELD OF THE INVENTION
The invention relates to isolated nucleic acids and polypeptides derived from Streptococcus pneumoniae that are useful as molecular targets for diagnostics, prophylaxis and treatment of pathological conditions, as well as materials and methods for the diagnosis, prevention, and amelioration of pathological conditions resulting from bacterial infection.
BACKGROUND OF THE INVENTION
Streptococcus pneumoniae (S. pneumoniae) is a common, spherical, gram-positive bacterium. Worldwide it is a leading cause of illness among children, the elderly, and individuals with debilitating medical conditions (Breiman, R. F. et al., 1994, JAMA 271: 1831). S. pneumoniae is estimated to be the causal agent in 3,000 cases of meningitis, 50,000 cases of bacteremia, 500,000 cases of pneumonia, and 7,000,000 cases of otitis media annually in the United States alone (Reichler, M. R. et al., 1992, J. Infect. Dis. 166: 1346; Stool, S. E. and Field, M. J., 1989 Pediatr. Infect. Dis J. 8: S11). In the United States alone, 40,000 deaths result annually from S. pneumoniae infections (Williams, W. W. et al., 1988 Ann. Intern. Med. 108: 616) with a death rate approaching 30% from bacteremia (Butler, J. C. et al., 1993, JAMA 270: 1826). Pneumococcal pneumonia is a serious problem among the elderly of industrialized nations (Käyhty, H. and Eskola, J., 1996 Emerg. Infect. Dis. 2: 289) and is a leading cause of death among children in developing nations (Käyhty, H. and Eskola, J., 1996 Emerg. Infect. Dis. 2: 289; Stansfield, S. K., 1987 Pediatr. Infect. Dis. 6: 622).
Vaccines against S. pneumoniae have been available for a number of years. There are a large number of serotypes based on the polysaccharide capsule (van Dam, J. E., Fleer, A., and Snippe, H., 1990 Antonie van Leeuwenhoek 58: 1) although only a fraction of the serotypes seem to be associated with infections (Martin, D. R. and Brett, M. S., 1996 N. Z. Med. J. 109: 288). A multivalent vaccine against capsular polysaccharides of 23 serotypes (Smart, L. E., Dougall, A. J. and Gridwood, R. W., 1987 J. Infect. 14: 209) has provided protection for some groups but not for several groups at risk for pneumococcal infections, such as infants and the elderly (Mäkel, P. H. et al., 1980 Lancet 2: 547; Sankilampi, U., 1996 J. Infect. Dis. 173: 387). Conjugated pneumococcal capsular polysaccharide vaccines have somewhat improved efficacy, but are costly and, therefore, are not likely to be in widespread use (Käyhty, H. and Eskola, J., 1996 Emerg. Infect. Dis. 2: 289).
At one time, S. pneumoniae strains were uniformly susceptible to penicillin. The report of a penicillin-resistant strain of (Hansman, D. and Bullen, M. M., 1967 Lancet 1: 264) was followed rapidly by many reports indicating the worldwide emergence of penicillin-resistant and penicillin non-susceptible strains (Klugman, K. P., 1990 Clin. Microbiol. Rev. 3: 171). S. pneumoniae strains which are resistant to multiple antibiotics (including penicillin) have also been observed recently within the United States (Welby, P. L., 1994 Pediatr. Infect. Dis. J. 13: 281; Ducin, J. S. et al., 1995 Pediatr. Infect. Dis. J. 14: 745; Butler, J. C., 1996 J. Infect. Dis. 174: 986) as well as internationally (Boswell, T. C. et al., 1996; J. Infect. 33: 17; Catchpole, C., Fraise, A., and Wise, R., 1996 Microb. Drug Resist. 2: 431; Tarasi, A. et al., 1997 Microb. Drug Resist. 3: 105).
A high incidence of morbidity is associated with invasive S. pneumoniae infections (Williams, W. W. et al., 1988 Ann. Intern. Med. 108: 616). Because of the incomplete effectiveness of currently available vaccines and antibiotics, the identification of new targets for antimicrobial therapies, including, but not limited to, the design of vaccines and antibiotics, which may help prevent infection or that may be useful in fighting existing infections, is highly desirable.
SUMMARY OF THE INVENTION
The present invention fulfills the need for diagnostic tools and therapeutics by providing bacterial-specific compositions and methods for detecting, treating, and preventing bacterial infection, in particular S. pneumoniae infection.
The present invention encompasses isolated polypeptides and nucleic acids derived from S. pneumoniae that are useful as reagents for diagnosis of bacterial infection, components of effective antibacterial vaccines, and/or as targets for antibacterial drugs, including anti-S. pneumoniae drugs. The nucleic acids and peptides of the present invention also have utility for diagnostics and therapeutics for S. pneumoniae and other Streptococcus species. They can also be used to detect the presence of S. pneumoniae and other Streptococcus species in a sample; and in screening compounds for the ability to interfere with the S. pneumoniae life cycle or to inhibit S. pneumoniae infection. More specifically, this invention features compositions of nucleic acids corresponding to entire coding sequences of S. pneumoniae proteins, including surface or secreted proteins or parts thereof, nucleic acids capable of binding mRNA from S. pneumoniae proteins to block protein translation, and methods for producing S. pneumoniae proteins or parts thereof using peptide synthesis and recombinant DNA techniques. This invention also features antibodies and nucleic acids useful as probes to detect S. pneumoniae infection. In addition, vaccine compositions and methods for the protection or treatment of infection by S. pneumoniae are within the scope of this invention.
The nucleotide sequences provided in SEQ ID NO: 1–SEQ ID NO: 2661, a fragment thereof, or a nucleotide sequence at least 99.5% identical to a sequence contained within SEQ ID NO: 1–SEQ ID NO: 2661 may be “provided” in a variety of medias to facilitate use thereof. As used herein, “provided” refers to a manufacture, other than an isolated nucleic acid molecule, which contains a nucleotide sequence of the present invention, i.e., the nucleotide sequence provided in SEQ ID NO: 1–SEQ ID NO: 2661, a fragment thereof, or a nucleotide sequence at least 99.5% identical to a sequence contained within SEQ ID NO: 1–SEQ ID NO: 2661. Uses for and methods for providing nucleotide sequences in a variety of media is well known in the art (see e.g., EPO Publication No. EP 0 756 006)
In one application of this embodiment, a nucleotide sequence of the present invention can be recorded on computer readable media. As used herein, “computer readable media” refers to any media which can be read and accessed directly by a computer. Such media include, but are not limited to: magnetic storage media, such as floppy discs, hard disc storage media, and magnetic tape; optical storage media such as CD-ROM; electrical storage media such as RAM and ROM; and hybrids of these categories such as magnetic/optical storage media. A person skilled in the art can readily appreciate how any of the presently known computer readable media can be used to create a manufacture comprising computer readable media having recorded thereon a nucleotide sequence of the present invention.
As used herein, “recorded” refers to a process for storing information on computer readable media. A person skilled in the art can readily adopt any of the presently known methods for recording information on computer readable media to generate manufactures comprising the nucleotide sequence information of the present invention.
A variety of data storage structures are available to a person skilled in the art for creating a computer readable media having recorded thereon a nucleotide sequence of the present invention. The choice of the data storage structure will generally be based on the means chosen to access the stored information. In addition, a variety of data processor programs and formats can be used to store the nucleotide sequence information of the present invention on computer readable media. The sequence information can be represented in a word processing text file, formatted in commercially-available software such as WordPerfect and Microsoft Word, or represented in the form of an ASCII file, stored in a database application, such as DB2, Sybase, Oracle, or the like. A person skilled in the art can readily adapt any number of data processor structuring formats (e.g. text file or database) in order to obtain computer readable media having recorded thereon the nucleotide sequence information of the present invention.
By providing the nucleotide sequence of SEQ ID NO: 1–SEQ ID NO: 2661, a fragment thereof, or a nucleotide sequence at least 99.5% identical to a sequence contained within SEQ ID NO: 1–SEQ ID NO: 2661 in computer readable form, a person skilled in the art can routinely access the sequence information for a variety of purposes. Computer software is publicly available which allows a person skilled in the art to access sequence information provided in a computer readable media. Examples of such computer software include programs of the “Staden Package”, “DNA Star”, “MacVector”, GCG “Wisconsin Package” (Genetics Computer Group, Madison, Wis.) and “NCBI toolbox” (National Center for Biotechnology Information).
Computer algorithms enable the identification of S. pneumoniae open reading frames (ORFs) within SEQ ID NO: 1–SEQ ID NO: 2661 which contain homology to ORFs or proteins from other organisms. Examples of such similarity-search algorithms include the BLAST [Altschul et al., J. Mol. Biol. 215:403–410 (1990)] and Smith-Waterman [Smith and Waterman (1981) Advances in Applied Mathematics, 2:482–489] search algorithms. These algorithms are utilized on computer systems as exemplified below. The ORFs so identified represent protein encoding fragments within the S. pneumoniae genome and are useful in producing commercially important proteins such as enzymes used in fermentation reactions and in the production of commercially useful metabolites.
The present invention further provides systems, particularly computer-based systems, which contain the sequence information described herein. Such systems are designed to identify commercially important fragments of the S. pneumoniae genome. As used herein, “a computer-based system” refers to the hardware means, software means, and data storage means used to analyze the nucleotide sequence information of the present invention. The minimum hardware means of the computer-based systems of the present invention comprises a central processing unit (CPU), input means, output means, and data storage means. A person skilled in the art can readily appreciate that any one of the currently available computer-based systems is suitable for use in the present invention. The computer-based systems of the present invention comprise a data storage means having stored therein a nucleotide sequence of the present invention and the necessary hardware means and software means for supporting and implementing a search means. As used herein, “data storage means” refers to memory which can store nucleotide sequence information of the present invention, or a memory access means which can access manufactures having recorded thereon the nucleotide sequence information of the present invention.
As used herein, “search means” refers to one or more programs which are implemented on the computer-based system to compare a target sequence or target structural motif with the sequence information stored within the data storage means. Search means are used to identify fragments or regions of the S. pneumoniae genome which are similar to, or “match”, a particular target sequence or target motif. A variety of known algorithms are known in the art and have been disclosed publicly, and a variety of commercially available software for conducting homology-based similarity searches are available and can be used in the computer-based systems of the present invention. Examples of such software include, but is not limited to, FASTA (GCG Wisconsin Package), Bic_SW (Compugen Bioccelerator, BLASTN2, BLASTP2 and BLASTX2 (NCBI) and Motifs (GCG). BLASTN2, A person skilled in the art can readily recognize that any one of the available algorithms or implementing software packages for conducting homology searches can be adapted for use in the present computer-based systems.
As used herein, a “target sequence” can be any DNA or amino acid sequence of six or more nucleotides or two or more amino acids. A person skilled in the art can readily recognize that the longer a target sequence is, the less likely a target sequence will be present as a random occurrence in the database. The most preferred sequence length of a target sequence is from about 10 to 100 amino acids or from about 30 to 300 nucleotide residues. However, it is well recognized that many genes are longer than 500 amino acids, or 1.5 kb in length, and that commercially important fragments of the S. pneumoniae genome, such as sequence fragments involved in gene expression and protein processing, will often be shorter than 30 nucleotides.
As used herein, “a target structural motif,” or “target motif,” refers to any rationally selected sequence or combination of sequences in which the sequence(s) are chosen based on a specific functional domain or three-dimensional configuration which is formed upon the folding of the target polypeptide. There are a variety of target motifs known in the art. Protein target motifs include, but are not limited to, enzymatic active sites, membrane spanning regions, and signal sequences. Nucleic acid target motifs include, but are not limited to, promoter sequences, hairpin structures and inducible expression elements (protein binding sequences).
A variety of structural formats for the input and output means can be used to input and output the information in the computer-based systems of the present invention. A preferred format for an output means ranks fragments of the S. pneumoniae genome possessing varying degrees of homology to the target sequence or target motif. Such presentation provides a person skilled in the art with a ranking of sequences which contain various amounts of the target sequence or target motif and identifies the degree of homology contained in the identified fragment.
A variety of comparing means can be used to compare a target sequence or target motif with the data storage means to identify sequence fragments of the S. pneumoniae genome. In the present examples, implementing software which implement the BLASTP2 and bic_SW algorithms (Altschul et al., J. Mol. Biol. 215:403–410 (1990); Compugen Biocellerator) was used to identify open reading frames within the S. pneumoniae genome. A person skilled in the art can readily recognize that any one of the publicly available homology search programs can be used as the search means for the computer-based systems of the present invention.
The invention features S. pneumoniae polypeptides, preferably a substantially pure preparation of an S. pneumoniae polypeptide, or a recombinant S. pneumoniae polypeptide. In preferred embodiments: the polypeptide has biological activity; the polypeptide has an amino acid sequence at least 60%, 70%, 80%, 90%, 95%, 98%, or 99% identical to an amino acid sequence of the invention contained in the Sequence Listing, preferably it has about 65% sequence identity with an amino acid sequence of the invention contained in the Sequence Listing, and most preferably it has about 92% to about 99% sequence identity with an amino acid sequence of the invention contained in the Sequence Listing; the polypeptide has an amino acid sequence essentially the same as an amino acid sequence of the invention contained in the Sequence Listing; the polypeptide is at least 5, 10, 20, 50, 100, or 150 amino acid residues in length; the polypeptide includes at least 5, preferably at least 10, more preferably at least 20, more preferably at least 50, 100, or 150 contiguous amino acid residues of the invention contained in the Sequence Listing. In yet another preferred embodiment, the amino acid sequence which differs in sequence identity by about 7% to about 8% from the S. pneumoniae amino acid sequences of the invention contained in the Sequence Listing is also encompassed by the invention.
In preferred embodiments: the S. pneumoniae polypeptide is encoded by a nucleic acid of the invention contained in the Sequence Listing, or by a nucleic acid having at least 60%, 70%, 80%, 90%, 95%, 98%, or 99% homology with a nucleic acid of the invention contained in the Sequence Listing.
In a preferred embodiment, the subject S. pneumoniae polypeptide differs in amino acid sequence at 1, 2, 3, 5, 10 or more residues from a sequence of the invention contained in the Sequence Listing. The differences, however, are such that the S. pneumoniae polypeptide exhibits an S. pneumoniae biological activity, e.g., the S. pneumoniae polypeptide retains a biological activity of a naturally occurring S. pneumoniae enzyme.
In preferred embodiments, the polypeptide includes all or a fragment of an amino acid sequence of the invention contained in the Sequence Listing; fused, in reading frame, to additional amino acid residues, preferably to residues encoded by genomic DNA 5′ or 3′ to the genomic DNA which encodes a sequence of the invention contained in the Sequence Listing.
In yet other preferred embodiments, the S. pneumoniae polypeptide is a recombinant fusion protein having a first S. pneumoniae polypeptide portion and a second polypeptide portion, e.g., a second polypeptide portion having an amino acid sequence unrelated to S. pneumoniae. The second polypeptide portion can be, e.g., any of glutathione-S-transferase, a DNA binding domain, or a polymerase activating domain. In preferred embodiment the fusion protein can be used in a two-hybrid assay.
Polypeptides of the invention include those which arise as a result of alternative transcription events, alternative RNA splicing events, and alternative translational and postranslational events.
In a preferred embodiment, the encoded S. pneumoniae polypeptide differs (e.g., by amino acid substitution, addition or deletion of at least one amino acid residue) in amino acid sequence at 1, 2, 3, 5, 10 or more residues, from a sequence of the invention contained in the Sequence Listing. The differences, however, are such that: the S. pneumoniae encoded polypeptide exhibits a S. pneumoniae biological activity, e.g., the encoded S. pneumoniae enzyme retains a biological activity of a naturally occurring S. pneumoniae. 
In preferred embodiments, the encoded polypeptide includes all or a fragment of an amino acid sequence of the invention contained in the Sequence Listing; fused, in reading frame, to additional amino acid residues, preferably to residues encoded by genomic DNA 5′ or 3′ to the genomic DNA which encodes a sequence of the invention contained in the Sequence Listing.
The S. pneumoniae strain, 14453, from which genomic sequences have been sequenced, has been deposited on Jun. 26, 1997 in the American Type Culture Collection, 10801 University Blvd., Manassas, Va. 200110-2209, and assigned the ATCC designation # 55987.
Included in the invention are: allelic variations; natural mutants; induced mutants; proteins encoded by DNA that hybridize under high or low stringency conditions to a nucleic acid which encodes a polypeptide of the invention contained in the Sequence Listing (for definitions of high and low stringency see Current Protocols in Molecular Biology, John Wiley & Sons, New York, 1989, 6.3.1–6.3.6, hereby incorporated by reference); and, polypeptides specifically bound by antisera to S. pneumoniae polypeptides, especially by antisera to an active site or binding domain of S. pneumoniae polypeptide. The invention also includes fragments, preferably biologically active fragments. These and other polypeptides are also referred to herein as S. pneumoniae polypeptide analogs or variants.
The invention further provides nucleic acids, e.g., RNA or DNA, encoding a polypeptide of the invention. This includes double stranded nucleic acids as well as coding and antisense single strands.
In preferred embodiments, the subject S. pneumoniae nucleic acid will include a transcriptional regulatory sequence, e.g. at least one of a transcriptional promoter or transcriptional enhancer sequence, operably linked to the S. pneumoniae gene sequence, e.g., to render the S. pneumoniae gene sequence suitable for expression in a recombinant host cell.
In yet a further preferred embodiment, the nucleic acid which encodes an S. pneumoniae polypeptide of the invention, hybridizes under stringent conditions to a nucleic acid probe corresponding to at least 8 consecutive nucleotides of the invention contained in the Sequence Listing; more preferably to at least 12 consecutive nucleotides of the invention contained in the Sequence Listing; more preferably to at least 20 consecutive nucleotides of the invention contained in the Sequence Listing; more preferably to at least 40 consecutive nucleotides of the invention contained in the Sequence Listing.
In another aspect, the invention provides a substantially pure nucleic acid having a nucleotide sequence which encodes an S. pneumoniae polypeptide. In preferred embodiments: the encoded polypeptide has biological activity; the encoded polypeptide has an amino acid sequence at least 60%, 70%, 80%, 90%, 95%, 98%, or 99% homologous to an amino acid sequence of the invention contained in the Sequence Listing; the encoded polypeptide has an amino acid sequence essentially the same as an amino acid sequence of the invention contained in the Sequence Listing; the encoded polypeptide is at least 5, 10, 20, 50, 100, or 150 amino acids in length; the encoded polypeptide comprises at least 5, preferably at least 10, more preferably at least 20, more preferably at least 50, 100, or 150 contiguous amino acids of the invention contained in the Sequence Listing.
In another aspect, the invention encompasses: a vector including a nucleic acid which encodes an S. pneumoniae polypeptide or an S. pneumoniae polypeptide variant as described herein; a host cell transfected with the vector; and a method of producing a recombinant S. pneumoniae polypeptide or S. pneumoniae polypeptide variant; including culturing the cell, e.g., in a cell culture medium, and isolating an S. pneumoniae polypeptide or an S. pneumoniae polypeptide variant, e.g., from the cell or from the cell culture medium.
In another series of embodiments, the invention provides isolated nucleic acids comprising sequences at least about 8 nucleotides in length, more preferably at least about 12 nucleotides in length, and most preferably at least about 15–20 nucleotides in length, that correspond to a subsequence of any one of SEQ ID NO: 1–SEQ ID NO: 2661 or complements thereof. Alternatively, the nucleic acids comprise sequences contained within any ORF (open reading frame), including a complete protein-coding sequence, of which any of SEQ ID NO: 1–SEQ ID NO: 2661 forms a part. The invention encompasses sequence-conservative variants and function-conservative variants of these sequences. The nucleic acids may be DNA, RNA, DNA/RNA duplexes, protein-nucleic acid (PNA), or derivatives thereof.
In another aspect, the invention features, a purified recombinant nucleic acid having at least 50%, 60%, 70%, 80%, 90%, 95%, 98%, or 99% homology with a sequence of the invention contained in the Sequence Listing.
In another aspect, the invention features nucleic acids capable of binding mRNA of S. pneumoniae. Such nucleic acid is capable of acting as antisense nucleic acid to control the translation of mRNA of S. pneumoniae. A further aspect features a nucleic acid which is capable of binding specifically to an S. pneumoniae nucleic acid. These nucleic acids are also referred to herein as complements and have utility as probes and as capture reagents.
In another aspect, the invention features an expression system comprising an open reading frame corresponding to S. pneumoniae nucleic acid. The nucleic acid further comprises a control sequence compatible with an intended host. The expression system is useful for making polypeptides corresponding to S. pneumoniae nucleic acid.
In another aspect, the invention features a cell transformed with the expression system to produce S. pneumoniae polypeptides.
In yet another embodiment, the invention encompasses reagents for detecting bacterial infection, including S. pneumoniae infection, which comprise at least one S. pneumoniae-derived nucleic acid defined by any one of SEQ ID NO: 1–SEQ ID NO: 2661, or sequence-conservative or function-conservative variants thereof. Alternatively, the diagnostic reagents comprise polypeptide sequences that are contained within any open reading frames (ORFs), including complete protein-coding sequences, contained within any of SEQ ID NO: 1–SEQ ID NO: 2661, or polypeptide sequences contained within any of SEQ ID NO: 2662–SEQ ID NO: 5322, or polypeptides of which any of the above sequences forms a part, or antibodies directed against any of the above peptide sequences or function-conservative variants and/or fragments thereof.
The invention further provides antibodies, preferably monoclonal antibodies, which specifically bind to the polypeptides of the invention. Methods are also provided for producing antibodies in a host animal. The methods of the invention comprise immunizing an animal with at least one S. pneumoniae-derived immunogenic component, wherein the immunogenic component comprises one or more of the polypeptides encoded by any one of SEQ ID NO: 1–SEQ ID NO: 2661 or sequence-conservative or function-conservative variants thereof; or polypeptides that are contained within any ORFs, including complete protein-coding sequences, of which any of SEQ ID NO: 1–SEQ ID NO: 2661 forms a part; or polypeptide sequences contained within any of SEQ ID NO: 2662–SEQ ID NO: 5322; or polypeptides of which any of SEQ ID NO: 2662–SEQ ID NO: 5322 forms a part. Host animals include any warm blooded animal, including without limitation mammals and birds. Such antibodies have utility as reagents for immunoassays to evaluate the abundance and distribution of S. pneumoniae-specific antigens.
In yet another aspect, the invention provides a method for detecting bacterial antigenic components in a sample, which comprises the steps of: (i) contacting a sample suspected to contain a bacterial antigenic component with a bacterial-specific antibody, under conditions in which a stable antigen-antibody complex can form between the antibody and bacterial antigenic components in the sample; and (ii) detecting any antigen-antibody complex formed in step (i), wherein detection of an antigen-antibody complex indicates the presence of at least one bacterial antigenic component in the sample. In different embodiments of this method, the antibodies used are directed against a sequence encoded by any of SEQ ID NO: 1–SEQ ID NO: 2661 or sequence-conservative or function-conservative variants thereof, or against a polypeptide sequence contained in any of SEQ ID NO: 2662–SEQ ID NO: 5322 or function-conservative variants thereof.
In yet another aspect, the invention provides a method for detecting antibacterial-specific antibodies in a sample, which comprises: (i) contacting a sample suspected to contain antibacterial-specific antibodies with a S. pneumoniae antigenic component, under conditions in which a stable antigen-antibody complex can form between the S. pneumoniae antigenic component and antibacterial antibodies in the sample; and (ii) detecting any antigen-antibody complex formed in step (i), wherein detection of an antigen-antibody complex indicates the presence of antibacterial antibodies in the sample. In different embodiments of this method, the antigenic component is encoded by a sequence contained in any of SEQ ID NO: 1–SEQ ID NO: 2661 or sequence-conservative and function-conservative variants thereof, or is a polypeptide sequence contained in any of SEQ ID NO: 2662–SEQ ID NO: 5322 or function-conservative variants thereof.
In another aspect, the invention features a method of generating vaccines for immunizing an individual against S. pneumoniae. The method includes: immunizing a subject with an S. pneumoniae polypeptide, e.g., a surface or secreted polypeptide, or active portion thereof, and a pharmaceutically acceptable carrier. Such vaccines have therapeutic and prophylactic utilities.
In another aspect, the invention features a method of evaluating a compound, e.g. a polypeptide, e.g., a fragment of a host cell polypeptide, for the ability to bind an S. pneumoniae polypeptide. The method includes: contacting the candidate compound with an S. pneumoniae polypeptide and determining if the compound binds or otherwise interacts with an S. pneumoniae polypeptide. Compounds which bind S. pneumoniae are candidates as activators or inhibitors of the bacterial life cycle. These assays can be performed in vitro or in vivo.
In another aspect, the invention features a method of evaluating a compound, e.g. a polypeptide, e.g., a fragment of a host cell polypeptide, for the ability to bind an S. pneumoniae nucleic acid, e.g., DNA or RNA. The method includes: contacting the candidate compound with an S. pneumoniae nucleic acid and determining if the compound binds or otherwise interacts with an S. pneumoniae polypeptide. Compounds which bind S. pneumoniae are candidates as activators or inhibitors of the bacterial life cycle. These assays can be performed in vitro or in vivo.


DETAILED DESCRIPTION OF THE INVENTION
The sequences of the present invention include the specific nucleic acid and amino acid sequences set forth in the Sequence Listing that forms a part of the present specification, and which are designated SEQ ID NO: 1–SEQ ID NO: 5322. Use of the terms “SEQ ID NO: 1–SEQ ID NO: 2661”, “SEQ ID NO: 2662–SEQ ID NO: 5322”, “the sequences depicted in Table 2”, etc., is intended, for convenience, to refer to each individual SEQ ID NO individually, and is not intended to refer to the genus of these sequences. In other words, it is a shorthand for listing all of these sequences individually. The invention encompasses each sequence individually, as well as any combination thereof.
Definitions
“Nucleic acid” or “polynucleotide” as used herein refers to purine- and pyrimidine-containing polymers of any length, either polyribonucleotides or polydeoxyribonucleotides or mixed polyribo-polydeoxyribo nucleotides. This includes single- and double-stranded molecules, i.e., DNA-DNA, DNA-RNA and RNA—RNA hybrids, as well as “protein nucleic acids” (PNA) formed by conjugating bases to an amino acid backbone. This also includes nucleic acids containing modified bases.
A nucleic acid or polypeptide sequence that is “derived from” a designated sequence refers to a sequence that corresponds to a region of the designated sequence. For nucleic acid sequences, this encompasses sequences that are homologous or complementary to the sequence, as well as “sequence-conservative variants” and “function-conservative variants.” For polypeptide sequences, this encompasses “function-conservative variants.” Sequence-conservative variants are those in which a change of one or more nucleotides in a given codon position results in no alteration in the amino acid encoded at that position. Function-conservative variants are those in which a given amino acid residue in a polypeptide has been changed without altering the overall conformation and function of the native polypeptide, including, but not limited to, replacement of an amino acid with one having similar physico-chemical properties (such as, for example, acidic, basic, hydrophobic, and the like). “Function-conservative” variants also include any polypeptides that have the ability to elicit antibodies specific to a designated polypeptide.
An “S. pneumoniae-derived” nucleic acid or polypeptide sequence may or may not be present in other bacterial species, and may or may not be present in all S. pneumoniae strains. This term is intended to refer to the source from which the sequence was originally isolated. Thus, a S. pneumoniae-derived polypeptide, as used herein, may be used, e.g., as a target to screen for a broad spectrum antibacterial agent, to search for homologous proteins in other species of bacteria or in eukaryotic organisms such as fungi and humans, etc.
A purified or isolated polypeptide or a substantially pure preparation of a polypeptide are used interchangeably herein and, as used herein, mean a polypeptide that has been separated from other proteins, lipids, and nucleic acids with which it naturally occurs. Preferably, the polypeptide is also separated from substances, e.g., antibodies or gel matrix, e.g., polyacrylamide, which are used to purify it. Preferably, the polypeptide constitutes at least 10, 20, 50 70, 80 or 95% dry weight of the purified preparation. Preferably, the preparation contains: sufficient polypeptide to allow protein sequencing; at least 1, 10, or 100 mg of the polypeptide.
A purified preparation of cells refers to, in the case of plant or animal cells, an in vitro preparation of cells and not an entire intact plant or animal. In the case of cultured cells or microbial cells, it consists of a preparation of at least 10% and more preferably 50% of the subject cells.
A purified or isolated or a substantially pure nucleic acid, e.g., a substantially pure DNA, (are terms used interchangeably herein) is a nucleic acid which is one or both of the following: not immediately contiguous with both of the coding sequences with which it is immediately contiguous (i.e., one at the 5′ end and one at the 3′ end) in the naturally-occurring genome of the organism from which the nucleic acid is derived; or which is substantially free of a nucleic acid with which it occurs in the organism from which the nucleic acid is derived. The term includes, for example, a recombinant DNA which is incorporated into a vector, e.g., into an autonomously replicating plasmid or virus, or into the genomic DNA of a prokaryote or eukaryote, or which exists as a separate molecule (e.g., a cDNA or a genomic DNA fragment produced by PCR or restriction endonuclease treatment) independent of other DNA sequences. Substantially pure DNA also includes a recombinant DNA which is part of a hybrid gene encoding additional S. pneumoniae DNA sequence.
A “contig” as used herein is a nucleic acid representing a continuous stretch of genomic sequence of an organism.
An “open reading frame”, also referred to herein as ORF, is a region of nucleic acid which encodes a polypeptide. This region usually represents the total coding region for the polypeptide and can be determined from a stop to stop codon or from a start to stop codon.
As used herein, a “coding sequence” is a nucleic acid which is transcribed into messenger RNA and/or translated into a polypeptide when placed under the control of appropriate regulatory sequences. The boundaries of the coding sequence are determined by a translation start codon at the five prime terminus and a translation stop codon at the three prime terminus. A coding sequence can include but is not limited to messenger RNA, synthetic DNA, and recombinant nucleic acid sequences.
A “complement” of a nucleic acid as used herein refers to an anti-parallel or antisense sequence that participates in Watson-Crick base-pairing with the original sequence.
A “gene product” is a protein or structural RNA which is specifically encoded by a gene.
As used herein, the term “probe” refers to a nucleic acid, peptide or other chemical entity which specifically binds to a molecule of interest. Probes are often associated with or capable of associating with a label. A label is a chemical moiety capable of detection. Typical labels comprise dyes, radioisotopes, luminescent and chemiluminescent moieties, fluorophores, enzymes, precipitating agents, amplification sequences, and the like. Similarly, a nucleic acid, peptide or other chemical entity which specifically binds to a molecule of interest and immobilizes such molecule is referred herein as a “capture ligand”. Capture ligands are typically associated with or capable of associating with a support such as nitro-cellulose, glass, nylon membranes, beads, particles and the like. The specificity of hybridization is dependent on conditions such as the base pair composition of the nucleotides, and the temperature and salt concentration of the reaction. These conditions are readily discernable to one of ordinary skill in the art using routine experimentation.
“Homologous” refers to the sequence similarity or sequence identity between two polypeptides or between two nucleic acid molecules. When a position in both of the two compared sequences is occupied by the same base or amino acid monomer subunit, e.g., if a position in each of two DNA molecules is occupied by adenine, then the molecules are homologous at that position. The percent of homology between two sequences is a function of the number of matching or homologous positions shared by the two sequences divided by the number of positions compared×100. For example, if 6 of 10 of the positions in two sequences are matched or homologous then the two sequences are 60% homologous. By way of example, the DNA sequences ATTGCC and TATGGC share 50% homology. Generally, a comparison is made when two sequences are aligned to give maximum homology.
Nucleic acids are hybridizable to each other when at least one strand of a nucleic acid can anneal to the other nucleic acid under defined stringency conditions. Stringency of hybridization is determined by: (a) the temperature at which hybridization and/or washing is performed; and (b) the ionic strength and polarity of the hybridization and washing solutions. Hybridization requires that the two nucleic acids contain complementary sequences; depending on the stringency of hybridization, however, mismatches may be tolerated. Typically, hybridization of two sequences at high stingency (such as, for example, in a solution of 0.5×SSC, at 65° C.) requires that the sequences be essentially completely homologous. Conditions of intermediate stringency (such as, for example, 2×SSC at 65° C.) and low stringency (such as, for example 2×SSC at 55° C.), require correspondingly less overall complementarity between the hybridizing sequences. (1×SSC is 0.15 M NaCl, 0.015 M Na citrate).
The terms peptides, proteins, and polypeptides are used interchangeably herein.
As used herein, the term “surface protein” refers to all surface accessible proteins, e.g. inner and outer membrane proteins, proteins adhering to the cell wall, and secreted proteins.
A polypeptide has S. pneumoniae biological activity if it has one, two and preferably more of the following properties: (1) if when expressed in the course of an S. pneumoniae infection, it can promote, or mediate the attachment of S. pneumoniae to a cell; (2) it has an enzymatic activity, structural or regulatory function characteristic of an S. pneumoniae protein; (3) or the gene which encodes it can rescue a lethal mutation in an S. pneumoniae gene. A polypeptide has biological activity if it is an antagonist, agonist, or super-agonist of a polypeptide having one of the above-listed properties.
A biologically active fragment or analog is one having an in vivo or in vitro activity which is characteristic of the S. pneumoniae polypeptides of the invention contained in the Sequence Listing, or of other naturally occurring S. pneumoniae polypeptides, e.g., one or more of the biological activities described herein. Especially preferred are fragments which exist in vivo, e.g., fragments which arise from post transcriptional processing or which arise from translation of alternatively spliced RNA's. Fragments include those expressed in native or endogenous cells as well as those made in expression systems, e.g., in CHO cells. Because peptides such as S. pneumoniae polypeptides often exhibit a range of physiological properties and because such properties may be attributable to different portions of the molecule, a useful S. pneumoniae fragment or S. pneumoniae analog is one which exhibits a biological activity in any biological assay for S. pneumoniae activity. Most preferably the fragment or analog possesses 10%, preferably 40%, more preferably 60%, 70%, 80% or 90% or greater of the activity of S. pneumoniae, in any in vivo or in vitro assay.
Analogs can differ from naturally occurring S. pneumoniae polypeptides in amino acid sequence or in ways that do not involve sequence, or both. Non-sequence modifications include changes in acetylation, methylation, phosphorylation, carboxylation, or glycosylation. Preferred analogs include S. pneumoniae polypeptides (or biologically active fragments thereof) whose sequences differ from the wild-type sequence by one or more conservative amino acid substitutions or by one or more non-conservative amino acid substitutions, deletions, or insertions which do not substantially diminish the biological activity of the S. pneumoniae polypeptide. Conservative substitutions typically include the substitution of one amino acid for another with similar characteristics, e.g., substitutions within the following groups: valine, glycine; glycine, alanine; valine, isoleucine, leucine; aspartic acid, glutamic acid; asparagine, glutamine; serine, threonine; lysine, arginine; and phenylalanine, tyrosine. Other conservative substitutions can be made in view of the table below.







TABLE 1







CONSERVATIVE AMINO ACID REPLACEMENTS









For Amino Acid
Code
Replace with any of





Alanine
A
D-Ala, Gly, beta-Ala, L-Cys, D-Cys


Arginine
R
D-Arg, Lys, D-Lys, homo-Arg, D-homo-Arg,




Met, Ile, D-Met, D-Ile, Orn, D-Orn


Asparagine
N
D-Asn, Asp, D-Asp, Glu, D-Glu, Gln, D-Gln


Aspartic Acid
D
D-Asp, D-Asn, Asn, Glu, D-Glu, Gln, D-Gln


Cysteine
C
D-Cys, S-Me-Cys, Met, D-Met, Thr, D-Thr


Glutamine
Q
D-Gln, Asn, D-Asn, Glu, D-Glu, Asp, D-Asp


Glutamic Acid
E
D-Glu, D-Asp, Asp, Asn, D-Asn, Gln, D-Gln


Glycine
G
Ala, D-Ala, Pro, D-Pro, β-Ala, Acp


Isoleucine
I
D-Ile, Val, D-Val, Leu, D-Leu, Met, D-Met


Leucine
L
D-Leu, Val, D-Val, Leu, D-Leu, Met, D-Met


Lysine
K
D-Lys, Arg, D-Arg, homo-Arg, D-homo-Arg,




Met, D-Met, Ile, D-Ile, Orn, D-Orn


Methionine
M
D-Met, S-Me-Cys, Ile, D-Ile,




Leu, D-Leu, Val, D-Val


Phenylalanine
F
D-Phe, Tyr, D-Thr, L-Dopa, His, D-His,




Trp, D-Trp, Trans-3,4, or 5-phenylproline,




cis-3,4, or 5-phenylproline


Proline
P
D-Pro, L-I-thioazolidine-4-carboxylic




acid, D-or L-1-oxazolidine-4-carboxylic acid


Serine
S
D-Ser, Thr, D-Thr, allo-Thr, Met, D-Met,




Met(O), D-Met(O), L-Cys, D-Cys


Threonine
T
D-Thr, Ser, D-Ser, allo-Thr, Met, D-Met,




Met(O), D-Met(O), Val, D-Val


Tyrosine
Y
D-Tyr, Phe, D-Phe, L-Dopa, His, D-His


Valine
V
D-Val, Leu, D-Leu, Ile, D-Ile, Met, D-Met









Other analogs within the invention are those with modifications which increase peptide stability; such analogs may contain, for example, one or more non-peptide bonds (which replace the peptide bonds) in the peptide sequence. Also included are: analogs that include residues other than naturally occurring L-amino acids, e.g., D-amino acids or non-naturally occurring or synthetic amino acids, e.g., β or γ amino acids; and cyclic analogs.
As used herein, the term “fragment”, as applied to an S. pneumoniae analog, will ordinarily be at least about 20 residues, more typically at least about 40 residues, preferably at least about 60 residues in length. Fragments of S. pneumoniae polypeptides can be generated by methods known to those skilled in the art. The ability of a candidate fragment to exhibit a biological activity of S. pneumoniae polypeptide can be assessed by methods known to those skilled in the art as described herein. Also included are S. pneumoniae polypeptides containing residues that are not required for biological activity of the peptide or that result from alternative mRNA splicing or alternative protein processing events.
An “immunogenic component” as used herein is a moiety, such as an S. pneumoniae polypeptide, analog or fragment thereof, that is capable of eliciting a humoral and/or cellular immune response in a host animal.
An “antigenic component” as used herein is a moiety, such as an S. pneumoniae polypeptide, analog or fragment thereof, that is capable of binding to a specific antibody with sufficiently high affinity to form a detectable antigen-antibody complex.
The term “antibody” as used herein is intended to include fragments thereof which are specifically reactive with S. pneumoniae polypeptides.
As used herein, the term “cell-specific promoter” means a DNA sequence that serves as a promoter, i.e., regulates expression of a selected DNA sequence operably linked to the promoter, and which effects expression of the selected DNA sequence in specific cells of a tissue. The term also covers so-called “leaky” promoters, which regulate expression of a selected DNA primarily in one tissue, but cause expression in other tissues as well.
Misexpression, as used herein, refers to a non-wild type pattern of gene expression. It includes: expression at non-wild type levels, i.e., over or under expression; a pattern of expression that differs from wild type in terms of the time or stage at which the gene is expressed, e.g., increased or decreased expression (as compared with wild type) at a predetermined developmental period or stage; a pattern of expression that differs from wild type in terms of decreased expression (as compared with wild type) in a predetermined cell type or tissue type; a pattern of expression that differs from wild type in terms of the splicing size, amino acid sequence, post-translational modification, or biological activity of the expressed polypeptide; a pattern of expression that differs from wild type in terms of the effect of an environmental stimulus or extracellular stimulus on expression of the gene, e.g., a pattern of increased or decreased expression (as compared with wild type) in the presence of an increase or decrease in the strength of the stimulus.
As used herein, “host cells” and other such terms denoting microorganisms or higher eukaryotic cell lines cultured as unicellular entities refers to cells which can become or have been used as recipients for a recombinant vector or other transfer DNA, and include the progeny of the original cell which has been transfected. It is understood by individuals skilled in the art that the progeny of a single parental cell may not necessarily be completely identical in genomic or total DNA compliment to the original parent, due to accident or deliberate mutation.
As used herein, the term “control sequence” refers to a nucleic acid having a base sequence which is recognized by the host organism to effect the expression of encoded sequences to which they are ligated. The nature of such control sequences differs depending upon the host organism; in prokaryotes, such control sequences generally include a promoter, ribosomal binding site, terminators, and in some cases operators; in eukaryotes, generally such control sequences include promoters, terminators and in some instances, enhancers. The term control sequence is intended to include at a minimum, all components whose presence is necessary for expression, and may also include additional components whose presence is advantageous, for example, leader sequences.
As used herein, the term “operably linked” refers to sequences joined or ligated to function in their intended manner. For example, a control sequence is operably linked to coding sequence by ligation in such a way that expression of the coding sequence is achieved under conditions compatible with the control sequence and host cell.
The “metabolism” of a substance, as used herein, means any aspect of the expression, function, action, or regulation of the substance. The metabolism of a substance includes modifications, e.g., covalent or non-covalent modifications of the substance. The metabolism of a substance includes modifications, e.g., covalent or non-covalent modification, the substance induces in other substances. The metabolism of a substance also includes changes in the distribution of the substance. The metabolism of a substance includes changes the substance induces in the distribution of other substances.
A “sample” as used herein refers to a biological sample, such as, for example, tissue or fluid isolated from an individual (including without limitation plasma, serum, cerebrospinal fluid, lymph, tears, saliva and tissue sections) or from in vitro cell culture constituents, as well as samples from the environment.
Technical and scientific terms used herein have the meanings commonly understood by one of ordinary skill in the art to which the present invention pertains, unless otherwise defined. Reference is made herein to various methodologies known to those of skill in the art. Publications and other materials setting forth such known methodologies to which reference is made are incorporated herein by reference in their entireties as though set forth in full. The practice of the invention will employ, unless otherwise indicated, conventional techniques of chemistry, molecular biology, microbiology, recombinant DNA, and immunology, which are within the skill of the art. Such techniques are explained fully in the literature. See e.g., Sambrook, Fritsch, and Maniatis, Molecular Cloning, Laboratory Manual 2nd ed. (1989); DNA Cloning, Volumes I and II (D. N Glover ed. 1985); Oligonucleotide Synthesis (M. J. Gait ed, 1984); Nucleic Acid Hybridization (B. D. Hames & S. J. Higgins eds. 1984); the series, Methods in Enzymoloqy (Academic Press, Inc.), particularly Vol. 154 and Vol. 155 (Wu and Grossman, eds.); PCR-A Practical Approach (McPherson, Quirke, and Taylor, eds., 1991); Immunology, 2d Edition, 1989, Roitt et al., C. V. Mosby Company, and New York; 3Advanced Immunology, 2d Edition, 1991, Male et al., Grower Medical Publishing, New York.; DNA Cloning: A Practical Approach, Volumes I and II, 1985 (D. N. Glover ed.); Oligonucleotide Synthesis, 1984, (M. L. Gait ed); Transcription and Translation, 1984 (Hames and Higgins eds.); Animal Cell Culture, 1986 (R. I. Freshney ed.); Immobilized Cells and Enzymes, 1986 (IRL Press); Perbal, 1984, A Practical Guide to Molecular Cloning; and Gene Transfer Vectors for Mammalian Cells, 1987 (J. H. Miller and M. P. Calos eds., Cold Spring Harbor Laboratory).
Any suitable materials and/or methods known to those of skill can be utilized in carrying out the present invention: however preferred materials and/or methods are described. Materials, reagents and the like to which reference is made in the following description and examples are obtainable from commercial sources, unless otherwise noted.
S. pneumoniae Genomic Sequence
This invention provides nucleotide sequences of the genome of S. pneumoniae which thus comprises a DNA sequence library of S. pneumoniae genomic DNA. The detailed description that follows provides nucleotide sequences of S. pneumoniae, and also describes how the sequences were obtained and how ORFs and protein-coding sequences were identified. Also described are methods of using the disclosed S. pneumoniae sequences in methods including diagnostic and therapeutic applications. Furthermore, the library can be used as a database for identification and comparison of medically important sequences in this and other strains of S. pneumoniae. 
To determine the genomic sequence of S. pneumoniae, DNA was isolated from strain 14453 of S. pneumoniae and mechanically sheared by nebulization to a median size of 2 kb. Following size fractionation by gel electrophoresis, the fragments were blunt-ended, ligated to adapter oligonucleotides, and cloned into each of 20 different pMPX vectors (Rice et al., abstracts of Meeting of Genome Mapping and Sequencing, Cold Spring Harbor, N.Y., May 5–15, 1994, p. 225) and the PUC19 vector to construct a series of “shotgun” subclone libraries.
DNA sequencing was achieved using two sequencing methods. The first method used multiplex sequencing procedures essentially as disclosed in Church et al., 1988, Science 240:185; U.S. Pat. Nos. 4,942,124 and 5,149,625). DNA was extracted from pooled cultures and subjected to chemical or enzymatic sequencing. Sequencing reactions were resolved by electrophoresis, and the products were transferred and covalently bound to nylon membranes. Finally, the membranes were sequentially hybridized with a series of labelled oligonucleotides complimentary to “tag” sequences present in the different shotgun cloning vectors. In this manner, a large number of sequences could be obtained from a single set of sequencing reactions. The remainder of the sequencing was performed on ABI377 automated DNA sequencers. The cloning and sequencing procedures are described in more detail in the Exemplification.
Individual sequence reads were assembled using PHRAP (P. Green, Abstracts of DOE Human Genome Program Contractor-Grantee Workshop V, January 1996, p. 157). The average contig length was about 3–4 kb.
A variety of approaches are used to order the contigs so as to obtain a continuous sequence representing the entire S. pneumoniae genome. Synthetic oligonucleotides are designed that are complementary to sequences at the end of each contig. These oligonucleotides may be hybridized to libaries of S. pneumoniae genomic DNA in, for example, lambda phage vectors or plasmid vectors to identify clones that contain sequences corresponding to the junctional regions between individual contigs. Such clones are then used to isolate template DNA and the same oligonucleotides are used as primers in polymerase chain reaction (PCR) to amplify junctional fragments, the nucleotide sequence of which is then determined.
The S. pneumoniae sequences were analyzed for the presence of open reading frames (ORFs) comprising at least 180 nucleotides. As a result of the initial analysis of ORFs based on stop-to-stop codon reads, it should be understood that these ORFs may not correspond to the ORF of a naturally-occurring S. pneumoniae polypeptide. These ORFs may contain start codons which indicate the initiation of protein synthesis of a naturally-occurring S. pneumoniae polypeptide. Such start codons within the ORFs provided herein can be identified by those of ordinary skill in the relevant art, and the resulting ORF and the encoded S. pneumoniae polypeptide is within the scope of this invention. For example, within the ORFs a codon such as AUG or GUG (encoding methionine or valine) which is part of the initiation signal for protein synthesis can be identified and the portion of an ORF to corresponding to a naturally-occurring S. pneumoniae polypeptide can be recognized.
The second analysis of the ORFs included identifying the start codons and the predicted coding regions. These ORFs provided in this invention were defined by one or more of the following methods: evaluating the coding potential of such sequences with the program GENEMARKTM (Borodovsky and McIninch, 1993, Comp. 17:123), distinguishing the coding from noncoding regions using the program Glimmer (Fraser et al, Nature, 1997), determining codon usage (Staden et al., Nucleic Acid Research 10: 141), and each predicted ORF amino acid sequence was compared with all protein sequences found in current GENBANK, SWISS-PROT, and PIR databases using the BLAST algorithm. BLAST identifies local alignments occurring by chance between the ORF sequence and the sequence in the databank (Altschal et al., 1990, L Mol. Biol. 215:403–410). Homologous ORFs (probabilities less than 10−5 by chance) and ORF's that are probably non-homologous (probabilities greater than 10−5 by chance) but have good codon usage were identified. Both homologous, sequences and non-homologous sequences with good codon usage are likely to encode proteins and are encompassed by the invention.
S. pneumoniae Nucleic Acids
The nucleic acids of this invention may be obtained directly from the DNA of the above referenced S. pneumoniae strain by using the polymerase chain reaction (PCR). See “PCR, A Practical Approach” (McPherson, Quirke, and Taylor, eds., IRL Press, Oxford, UK, 1991) for details about the PCR. High fidelity PCR can be used to ensure a faithful DNA copy prior to expression. In addition, the authenticity of amplified products can be verified by conventional sequencing methods. Clones carrying the desired sequences described in this invention may also be obtained by screening the libraries by means of the PCR or by hybridization of synthetic oligonucleotide probes to filter lifts of the library colonies or plaques as known in the art (see, e.g., Sambrook et al., Molecular Cloning, A Laboratory Manual 2nd edition, 1989, Cold Spring Harbor Press, NY).
It is also possible to obtain nucleic acids encoding S. pneumoniae polypeptides from a cDNA library in accordance with protocols herein described. A cDNA encoding an S. pneumoniae polypeptide can be obtained by isolating total mRNA from an appropriate strain. Double stranded cDNAs can then be prepared from the total mRNA. Subsequently, the cDNAs can be inserted into a suitable plasmid or viral (e.g., bacteriophage) vector using any one of a number of known techniques. Genes encoding S. pneumoniae polypeptides can also be cloned using established polymerase chain reaction techniques in accordance with the nucleotide sequence information provided by the invention. The nucleic acids of the invention can be DNA or RNA. Preferred nucleic acids of the invention are contained in the Sequence Listing.
The nucleic acids of the invention can also be chemically synthesized using standard techniques. Various methods of chemically synthesizing polydeoxynucleotides are known, including solid-phase synthesis which, like peptide synthesis, has been fully automated in commercially available DNA synthesizers (See e.g., Itakura et al. U.S. Pat. No. 4,598,049; Caruthers et al. U.S. Pat. No. 4,458,066; and Itakura U.S. Pat. Nos. 4,401,796 and 4,373,071, incorporated by reference herein).
Nucleic acids isolated or synthesized in accordance with features of the present invention are useful, by way of example, without limitation, as probes, primers, capture ligands, antisense genes and for developing expression systems for the synthesis of proteins and peptides corresponding to such sequences. As probes, primers, capture ligands and antisense agents, the nucleic acid normally consists of all or part (approximately twenty or more nucleotides for specificity as well as the ability to form stable hybridization products) of the nucleic acids of the invention contained in the Sequence Listing. These uses are described in further detail below.
Probes
A nucleic acid isolated or synthesized in accordance with the sequence of the invention contained in the Sequence Listing can be used as a probe to specifically detect S. pneumoniae. With the sequence information set forth in the present application, sequences of twenty or more nucleotides are identified which provide the desired inclusivity and exclusivity with respect to S. pneumoniae, and extraneous nucleic acids likely to be encountered during hybridization conditions. More preferably, the sequence will comprise at least twenty to thirty nucleotides to convey stability to the hybridization product formed between the probe and the intended target molecules.
Sequences larger than 1000 nucleotides in length are difficult to synthesize but can be generated by recombinant DNA techniques. Individuals skilled in the art will readily recognize that the nucleic acids, for use as probes, can be provided with a label to facilitate detection of a hybridization product.
Nucleic acid isolated and synthesized in accordance with the sequence of the invention contained in the Sequence Listing can also be useful as probes to detect homologous regions (especially homologous genes) of other Streptococcus species using appropriate stringency hybridization conditions as described herein.
Capture Ligand
For use as a capture ligand, the nucleic acid selected in the manner described above with respect to probes, can be readily associated with a support. The manner in which nucleic acid is associated with supports is well known. Nucleic acid having twenty or more nucleotides in a sequence of the invention contained in the Sequence Listing have utility to separate S. pneumoniae nucleic acid from the nucleic acid of each other and other organisms. Nucleic acid having twenty or more nucleotides in a sequence of the invention contained in the Sequence Listing can also have utility to separate other Streptococcus species from each other and from other organisms. Preferably, the sequence will comprise at least twenty nucleotides to convey stability to the hybridization product formed between the probe and the intended target molecules. Sequences larger than 1000 nucleotides in length are difficult to synthesize but can be generated by recombinant DNA techniques.
Primers
Nucleic acid isolated or synthesized in accordance with the sequences described herein have utility as primers for the amplification of S. pneumoniae nucleic acid. These nucleic acids may also have utility as primers for the amplification of nucleic acids in other Streptococcus species. With respect to polymerase chain reaction (PCR) techniques, nucleic acid sequences of ≧10–15 nucleotides of the invention contained in the Sequence Listing have utility in conjunction with suitable enzymes and reagents to create copies of S. pneumoniae nucleic acid. More preferably, the sequence will comprise twenty or more nucleotides to convey stability to the hybridization product formed between the primer and the intended target molecules. Binding conditions of primers greater than 100 nucleotides are more difficult to control to obtain specificity. High fidelity PCR can be used to ensure a faithful DNA copy prior to expression. In addition, amplified products can be checked by conventional sequencing methods.
The copies can be used in diagnostic assays to detect specific sequences, including genes from S. pneumoniae and/or other Streptococcus species. The copies can also be incorporated into cloning and expression vectors to generate polypeptides corresponding to the nucleic acid synthesized by PCR, as is described in greater detail herein.
Antisense
Nucleic acid or nucleic acid-hybridizing derivatives isolated or synthesized in accordance with the sequences described herein have utility as antisense agents to prevent the expression of S. pneumoniae genes. These sequences also have utility as antisense agents to prevent expression of genes of other Streptococcus species.
In one embodiment, nucleic acid or derivatives corresponding to S. pneumoniae nucleic acids is loaded into a suitable carrier such as a liposome or bacteriophage for introduction into bacterial cells. For example, a nucleic acid having twenty or more nucleotides is capable of binding to bacteria nucleic acid or bacteria messenger RNA. Preferably, the antisense nucleic acid is comprised of 20 or more nucleotides to provide necessary stability of a hybridization product of non-naturally occurring nucleic acid and bacterial nucleic acid and/or bacterial messenger RNA. Nucleic acid having a sequence greater than 1000 nucleotides in length is difficult to synthesize but can be generated by recombinant DNA techniques. Methods for loading antisense nucleic acid in liposomes is known in the art as exemplified by U.S. Pat. No. 4,241,046 issued Dec. 23, 1980 to Papahadjopoulos et al.
The present invention encompasses isolated polypeptides and nucleic acids derived from S. pneumoniae that are useful as reagents for diagnosis of bacterial infection, components of effective antibacterial vaccines, and/or as targets for antibacterial drugs, including anti-S. pneumoniae drugs.
Expression of S. pneumoniae Nucleic Acids
Table 2 provides a list of open reading frames (ORFs) in both strands. An ORF is a region of nucleic acid which encodes a polypeptide. This region normally represents a complete coding sequence or a total sequence and was determined from an initial analysis of stop to stop codons followed by the prediction of start codons. The first column lists the ORF designation. The second and third columns list the SEQ ID numbers for the nucleic acid and amino acid sequences corresponding to each ORF, respectively. The fourth and fifth columns list the length of the nucleic acid ORF and the length of the amino acid ORF, respectively. Most of the nucleotide sequences corresponding to each ORF begin at the first nucleotide of the start codon and end at the nucleotide immediately preceding the next downstream stop codon in the same reading frame. It will be recognized by one skilled in the art that the natural translation initiation sites will correspond to ATG, GTG, or TTG codons located within the ORFs. The natural initiation sites depend not only on the sequence of a start codon but also on the context of the DNA sequence adjacent to the start codon. Usually, a recognizable ribosome binding site is found within 20 nucleotides upstream from the initiation codon. In some cases where genes are translationally coupled and coordinately expressed together in “operons”, ribosome binding sites are not present, but the initiation codon of a downstream gene may occur very close to, or overlap, the stop codon of the an upstream gene in the same operon. The correct start codons can be generally identified rapidly and efficiently because only a few codons need be tested. It is recognized that the translational machinery in bacteria initiates most polypeptide chains with the amino acid methionine. In some cases, polypeptides are post-translationally modified, resulting in an N-terminal amino acid other than methionine in vivo. The sixth and seventh columns provide metrics for assessing the likelihood of the homology match (determined by the BLASTP2 algorithm), as is known in the art, to the genes indicated in the description field. Specifically, the sixth column represents the “Score” for the match (a higher score is a better match), and the seventh column represents the “P-value” for the match (the probability that such a match could have occurred by chance; the lower the value, the more likely the match is valid). If a BLASTP2 score of less than 46 was obtained, no value is reported in the table the “P-value”. The description field provides, where available, the accession number (AC) or the Swissprot accession number (SP), the locus name (LN), Superfamily Classification (CL), the Organism (OR), Source of variant (SR), E.C. number (EC), the gene name (GN), the product name (PN), the Function Description (FN), the Map Position (MP), Left End (LE), Right End (RE), Coding Direction (DI), the Database from which the sequence originates (DB), and the description (DE) or notes (NT) for each ORF. This information allows one of ordinary skill in the art to determine a potential use and function for each identified coding sequence and, as a result, allows the use of the polypeptides of the present invention for commercial and industrial purposes.
Using the information provided in SEQ ID NO: 1–SEQ ID NO: 2661 and in Table 2 together with routine cloning and sequencing methods, one of ordinary skill in the art will be able to clone and sequence all the nucleic acid fragments of interest including open reading frames (ORFs) encoding a large variety proteins of S. pneumoniae. 
Nucleic acid isolated or synthesized in accordance with the sequences described herein have utility to generate polypeptides. The nucleic acid of the invention exemplified in SEQ ID NO: 1–SEQ ID NO: 2661 and in Table 2 or fragments of said nucleic acid encoding active portions of S. pneumoniae polypeptides can be cloned into suitable vectors or used to isolate nucleic acid. The isolated nucleic acid is combined with suitable DNA linkers and cloned into a suitable vector.
The function of a specific gene or operon can be ascertained by expression in a bacterial strain under conditions where the activity of the gene product(s) specified by the gene or operon in question can be specifically measured. Alternatively, a gene product may be produced in large quantities in an expressing strain for use as an antigen, an industrial reagent, for structural studies, etc. This expression can be accomplished in a mutant strain which lacks the activity of the gene to be tested, or in a strain that does not produce the same gene product(s). This includes, but is not limited to, Eucaryotic species such as the yeast Saccharomyces cerevisiae, Methanobacterium strains or other Archaea, and Eubacteria such as E. coli, B. subtilis, S. aureus, S. pneumonia or Pseudomonas putida. In some cases the expression host will utilize the natural S. pneumoniae promoter whereas in others, it will be necessary to drive the gene with a promoter sequence derived from the expressing organism (e.g., an E. coli beta-galactosidase promoter for expression in E. coli).
To express a gene product using the natural S. pneumoniae promoter, a procedure such as the following can be used. A restriction fragment containing the gene of interest, together with its associated natural promoter element and regulatory sequences (identified using the DNA sequence data) is cloned into an appropriate recombinant plasmid containing an origin of replication that functions in the host organism and an appropriate selectable marker. This can be accomplished by a number of procedures known to those skilled in the art. It is most preferably done by cutting the plasmid and the fragment to be cloned with the same restriction enzyme to produce compatible ends that can be ligated to join the two pieces together. The recombinant plasmid is introduced into the host organism by, for example, electroporation and cells containing the recombinant plasmid are identified by selection for the marker on the plasmid. Expression of the desired gene product is detected using an assay specific for that gene product.
In the case of a gene that requires a different promoter, the body of the gene (coding sequence) is specifically excised and cloned into an appropriate expression plasmid. This subcloning can be done by several methods, but is most easily accomplished by PCR amplification of a specific fragment and ligation into an expression plasmid after treating the PCR product with a restriction enzyme or exonuclease to create suitable ends for cloning.
A suitable host cell for expression of a gene can be any procaryotic or eucaryotic cell. For example, an S. pneumoniae polypeptide can be expressed in bacterial cells such as E. coli or B. subtilis, insect cells (baculovirus), yeast, or mammalian cells such as Chinese hamster ovary cell (CHO). Other suitable host cells are known to those skilled in the art.
Expression in eucaryotic cells such as mammalian, yeast, or insect cells can lead to partial or complete glycosylation and/or formation of relevant inter- or intra-chain disulfide bonds of a recombinant peptide product. Examples of vectors for expression in yeast S. cerivisae include p YepSec1 (Baldari. et al., (1987) Embo J. 6:229–234), pMFa (Kurjan and Herskowitz, (1982) Cell 30:933–943), pJRY88 (Schultz et al., (1987) Gene 54:113–123), and pYES2 (Invitrogen Corporation, San Diego, Calif.). Baculovirus vectors available for expression of proteins in cultured insect cells (SF 9 cells) include the pAc series (Smith et al., (1983) Mol. Cell Biol. 3:2156–2165) and the pVL series (Lucklow, V. A., and Summers, M. D., (1989) Virology 170:31–39). Generally, COS cells (Gluzman, Y., (1981) Cell 23:175–182) are used in conjunction with such vectors as pCDM 8 (Aruffo, A. and Seed, B., (1987) Proc. Natl. Acad. Sci. USA 84:8573–8577) for transient amplification/expression in mammalian cells, while CHO (dhfr− Chinese Hamster Ovary) cells are used with vectors such as pMT2PC (Kaufman et al. (1987), EMBO J. 6:187–195) for stable amplification/expression in mammalian cells. Vector DNA can be introduced into mammalian cells via conventional techniques such as calcium phosphate or calcium chloride co-precipitation, DEAE-dextran-mediated transfection, or electroporation. Suitable methods for transforming host cells can be found in Sambrook et al. (Molecular Cloning: A Laboratory Manual, 2nd Edition, Cold Spring Harbor Laboratory press (1989)), and other laboratory textbooks.
Expression in procaryotes is most often carried out in E. coli with either fusion or non-fusion inducible expression vectors. Fusion vectors usually add a number of NH2 terminal amino acids to the expressed target gene. These NH2 terminal amino acids often are referred to as a reporter group or an affinity purification group. Such reporter groups usually serve two purposes: 1) to increase the solubility of the target recombinant protein; and 2) to aid in the purification of the target recombinant protein by acting as a ligand in affinity purification. Often, in fusion expression vectors, a proteolytic cleavage site is introduced at the junction of the reporter group and the target recombinant protein to enable separation of the target recombinant protein from the reporter group subsequent to purification of the fusion protein. Such enzymes, and their cognate recognition sequences, include Factor Xa, thrombin and enterokinase. Typical fusion expression vectors include pGEX (Amrad Corp., Melbourne, Australia), pMAL (New England Biolabs, Beverly, Mass.) and pRIT5 (Pharmacia, Piscataway, N.J.) which fuse glutathione S-transferase, maltose E binding protein, or protein A, respectively, to the target recombinant protein. A preferred reporter group is poly(His), which may be fused to the amino or carboxy terminus of the protein and which renders the recombinant fusion protein easily purifiable by metal chelate chromatography.
Inducible non-fusion expression vectors include pTrc (Amann et al., (1988) Gene 69:301–315) and pET11d (Studier et al., Gene Expression Technology: Methods in Enzymology 185, Academic Press, San Diego, Calif. (1990) 60–89). While target gene expression relies on host RNA polymerase transcription from the hybrid trp-lac fusion promoter in pTrc, expression of target genes inserted into pET11d relies on transcription from the T7 gn10-lac 0 fusion promoter mediated by coexpressed viral RNA polymerase (T7 gn1). This viral polymerase is supplied by host strains BL21(DE3) or HMS174(DE3) from a resident λ prophage harboring a T7 gn1 under the transcriptional control of the lacUV 5 promoter.
For example, a host cell transfected with a nucleic acid vector directing expression of a nucleotide sequence encoding an S. pneumoniae polypeptide can be cultured under appropriate conditions to allow expression of the polypeptide to occur. The polypeptide may be secreted and isolated from a mixture of cells and medium containing the peptide. Alternatively, the polypeptide may be retained cytoplasmically and the cells harvested, lysed and the protein isolated. A cell culture includes host cells, media and other byproducts. Suitable media for cell culture are well known in the art. Polypeptides of the invention can be isolated from cell culture medium, host cells, or both using techniques known in the art for purifying proteins including ion-exchange chromatography, gel filtration chromatography, ultrafiltration, electrophoresis, and immunoaffinity purification with antibodies specific for such polypeptides. Additionally, in many situations, polypeptides can be produced by chemical cleavage of a native protein (e.g., tryptic digestion) and the cleavage products can then be purified by standard techniques.
In the case of membrane bound proteins, these can be isolated from a host cell by contacting a membrane-associated protein fraction with a detergent forming a solubilized complex, where the membrane-associated protein is no longer entirely embedded in the membrane fraction and is solubilized at least to an extent which allows it to be chromatographically isolated from the membrane fraction. Several different criteria are used for choosing a detergent suitable for solubilizing these complexes. For example, one property considered is the ability of the detergent to solubilize the S. pneumoniae protein within the membrane fraction at minimal denaturation of the membrane-associated protein allowing for the activity or functionality of the membrane-associated protein to return upon reconstitution of the protein. Another property considered when selecting the detergent is the critical micelle concentration (CMC) of the detergent in that the detergent of choice preferably has a high CMC value allowing for ease of removal after reconstitution. A third property considered when selecting a detergent is the hydrophobicity of the detergent. Typically, membrane-associated proteins are very hydrophobic and therefore detergents which are also hydrophobic, e.g., the triton series, would be useful for solubilizing the hydrophobic proteins. Another property important to a detergent can be the capability of the detergent to remove the S. pneumoniae protein with minimal protein-protein interaction facilitating further purification. A fifth property of the detergent which should be considered is the charge of the detergent. For example, if it is desired to use ion exchange resins in the purification process then preferably detergent should be an uncharged detergent. Chromatographic techniques which can be used in the final purification step are known in the art and include hydrophobic interaction, lectin affinity, ion exchange, dye affinity and immunoaffinity.
One strategy to maximize recombinant S. pneumoniae peptide expression in E. coli is to express the protein in a host bacteria with an impaired capacity to proteolytically cleave the recombinant protein (Gottesman, S., Gene Expression Technology: Methods in Enzymology 185, Academic Press, San Diego, Calif. (1990) 119–128). Another strategy would be to alter the nucleic acid encoding an S. pneumoniae peptide to be inserted into an expression vector so that the individual codons for each amino acid would be those preferentially utilized in highly expressed E. coli proteins (Wada et al., (1992) Nuc. Acids Res. 20:2111–2118). Such alteration of nucleic acids of the invention can be carried out by standard DNA synthesis techniques.
The nucleic acids of the invention can also be chemically synthesized using standard techniques. Various methods of chemically synthesizing polydeoxynucleotides are known, including solid-phase synthesis which, like peptide synthesis, has been fully automated in commercially available DNA synthesizers (See, e.g., Itakura et al. U.S. Pat. No. 4,598,049; Caruthers et al. U.S. Pat. No. 4,458,066; and Itakura U.S. Pat. Nos. 4,401,796 and 4,373,071, incorporated by reference herein).
The present invention provides a library of S. pneumoniae-derived nucleic acid sequences. The libraries provide probes, primers, and markers which can be used as markers in epidemiological studies. The present invention also provides a library of S. pneumoniae-derived nucleic acid sequences which comprise or encode targets for therapeutic drugs.
Nucleic acids comprising any of the sequences disclosed herein or sub-sequences thereof can be prepared by standard methods using the nucleic acid sequence information provided in SEQ ID NO: 1–SEQ ID NO: 2661. For example, DNA can be chemically synthesized using, e.g., the phosphoramidite solid support method of Matteucci et al., 1981, J. Am. Chem. Soc. 103:3185, the method of Yoo et al., 1989, J. Biol. Chem. 764:17078, or other well known methods. This can be done by sequentially linking a series of oligonucleotide cassettes comprising pairs of synthetic oligonucleotides, as described below.
Of course, due to the degeneracy of the genetic code, many different nucleotide sequences can encode polypeptides having the amino acid sequences defined by SEQ ID NO: 2662–SEQ ID NO: 5322 or sub-sequences thereof. The codons can be selected for optimal expression in prokaryotic or eukaryotic systems. Such degenerate variants are also encompassed by this invention.
Insertion of nucleic acids (typically DNAs) encoding the polypeptides of the invention into a vector is easily accomplished when the termini of both the DNAs and the vector comprise compatible restriction sites. If this cannot be done, it may be necessary to modify the termini of the DNAs and/or vector by digesting back single-stranded DNA overhangs generated by restriction endonuclease cleavage to produce blunt ends, or to achieve the same result by filling in the single-stranded termini with an appropriate DNA polymerase.
Alternatively, any site desired may be produced, e.g., by ligating nucleotide sequences (linkers) onto the termini. Such linkers may comprise specific oligonucleotide sequences that define desired restriction sites. Restriction sites can also be generated by the use of the polymerase chain reaction (PCR). See, e.g., Saiki et al., 1988, Science 239:48. The cleaved vector and the DNA fragments may also be modified if required by homopolymeric tailing.
In certain embodiments, the invention encompasses isolated nucleic acid fragments comprising all or part of the individual nucleic acid sequences disclosed herein. The fragments are at least about 8 nucleotides in length, preferably at least about 12 nucleotides in length, and most preferably at least about 15–20 nucleotides in length.
The nucleic acids may be isolated directly from cells. Alternatively, the polymerase chain reaction (PCR) method can be used to produce the nucleic acids of the invention, using either chemically synthesized strands or genomic material as templates. Primers used for PCR can be synthesized using the sequence information provided herein and can further be designed to introduce appropriate new restriction sites, if desirable, to facilitate incorporation into a given vector for recombinant expression.
The nucleic acids of the present invention may be flanked by natural S. pneumoniae regulatory sequences, or may be associated with heterologous sequences, including promoters, enhancers, response elements, signal sequences, polyadenylation sequences, introns, 5′- and 3′-noncoding regions, and the like. The nucleic acids may also be modified by many means known in the art. Non-limiting examples of such modifications include methylation, “caps”, substitution of one or more of the naturally occurring nucleotides with an analog, internucleotide modifications such as, for example, those with uncharged linkages (e.g., methyl phosphonates, phosphotriesters, phosphoroamidates, carbamates, etc.) and with charged linkages (e.g., phosphorothioates, phosphorodithioates, etc.). Nucleic acids may contain one or more additional covalently linked moieties, such as, for example, proteins (e.g., nucleases, toxins, antibodies, signal peptides, poly-L-lysine, etc.), intercalators (e.g., acridine, psoralen, etc.), chelators (e.g., metals, radioactive metals, iron, oxidative metals, etc.), and alkylators. PNAs are also included. The nucleic acid may be derivatized by formation of a methyl or ethyl phosphotriester or an alkyl phosphoramidate linkage. Furthermore, the nucleic acid sequences of the present invention may also be modified with a label capable of providing a detectable signal, either directly or indirectly. Exemplary labels include radioisotopes, fluorescent molecules, biotin, and the like.
The invention also provides nucleic acid vectors comprising the disclosed S. pneumoniae-derived sequences or derivatives or fragments thereof. A large number of vectors, including plasmid and fungal vectors, have been described for replication and/or expression in a variety of eukaryotic and prokaryotic hosts, and may be used for gene therapy as well as for simple cloning or protein expression.
The encoded S. pneumoniae polypeptides may be expressed by using many known vectors, such as pUC plasmids, pET plasmids (Novagen, Inc., Madison, Wis.), or pRSET or pREP (Invitrogen, San Diego, Calif.), and many appropriate host cells, using methods disclosed or cited herein or otherwise known to those skilled in the relevant art. The particular choice of vector/host is not critical to the practice of the invention.
Recombinant cloning vectors will often include one or more replication systems for cloning or expression, one or more markers for selection in the host, e.g. antibiotic resistance, and one or more expression cassettes. The inserted S. pneumoniae coding sequences may be synthesized by standard methods, isolated from natural sources, or prepared as hybrids, etc. Ligation of the S. pneumoniae coding sequences to transcriptional regulatory elements and/or to other amino acid coding sequences may be achieved by known methods. Suitable host cells may be transformed/transfected/infected as appropriate by any suitable method including electroporation, CaCl2 mediated DNA uptake, fungal infection, microinjection, microprojectile, or other established methods.
Appropriate host cells include bacteria, archebacteria, fungi, especially yeast, and plant and animal cells, especially mammalian cells. Of particular interest are S. pneumoniae, E. coli, B. Subtilis, Saccharomyces cerevisiae, Saccharomyces carlsbergensis, Schizosaccharomyces pombi, SF9 cells, C129 cells, 293 cells, Neurospora, and CHO cells, COS cells, HeLa cells, and immortalized mammalian myeloid and lymphoid cell lines. Preferred replication systems include M13, ColE1, SV40, baculovirus, lambda, adenovirus, and the like. A large number of transcription initiation and termination regulatory regions have been isolated and shown to be effective in the transcription and translation of heterologous proteins in the various hosts. Examples of these regions, methods of isolation, manner of manipulation, etc. are known in the art. Under appropriate expression conditions, host cells can be used as a source of recombinantly produced S. pneumoniae-derived peptides and polypeptides.
Advantageously, vectors may also include a transcription regulatory element (i.e., a promoter) operably linked to the S. pneumoniae portion. The promoter may optionally contain operator portions and/or ribosome binding sites. Non-limiting examples of bacterial promoters compatible with E. coli include: b-lactamase (penicillinase) promoter; lactose promoter; tryptophan (trp) promoter; araBAD (arabinose) operon promoter; lambda-derived P1 promoter and N gene ribosome binding site; and the hybrid tac promoter derived from sequences of the trp and lac UV5 promoters. Non-limiting examples of yeast promoters include 3-phosphoglycerate kinase promoter, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) promoter, galactokinase (GAL1) promoter, galactoepimerase promoter, and alcohol dehydrogenase (ADH) promoter. Suitable promoters for mammalian cells include without limitation viral promoters such as that from Simian Virus 40 (SV40), Rous sarcoma virus (RSV), adenovirus (ADV), and bovine papilloma virus (BPV). Mammalian cells may also require terminator sequences, polyA addition sequences and enhancer sequences to increase expression. Sequences which cause amplification of the gene may also be desirable. Furthermore, sequences that facilitate secretion of the recombinant product from cells, including, but not limited to, bacteria, yeast, and animal cells, such as secretory signal sequences and/or prohormone pro region sequences, may also be included. These sequences are well described in the art.
Nucleic acids encoding wild-type or variant S. pneumoniae-derived polypeptides may also be introduced into cells by recombination events. For example, such a sequence can be introduced into a cell, and thereby effect homologous recombination at the site of an endogenous gene or a sequence with substantial identity to the gene. Other recombination-based methods such as nonhomologous recombinations or deletion of endogenous genes by homologous recombination may also be used.
The nucleic acids of the present invention find use as templates for the recombinant production of S. pneumoniae-derived peptides or polypeptides.
Identification and Use of S. pneumoniae Nucleic Acid Sequences
The disclosed S. pneumoniae polypeptide and nucleic acid sequences, or other sequences that are contained within ORFs, including complete protein-coding sequences, of which any of the disclosed S. pneumoniae-specific sequences forms a part, are useful as target components for diagnosis and/or treatment of S. pneumoniae-caused infection
It will be understood that the sequence of an entire protein-coding sequence of which each disclosed nucleic acid sequence forms a part can be isolated and identified based on each disclosed sequence. This can be achieved, for example, by using an isolated nucleic acid encoding the disclosed sequence, or fragments thereof, to prime a sequencing reaction with genomic S. pneumoniae DNA as template; this is followed by sequencing the amplified product. The isolated nucleic acid encoding the disclosed sequence, or fragments thereof, can also be hybridized to S. pneumoniae genomic libraries to identify clones containing additional complete segments of the protein-coding sequence of which the shorter sequence forms a part. Then, the entire protein-coding sequence, or fragments thereof, or nucleic acids encoding all or part of the sequence, or sequence-conservative or function-conservative variants thereof, may be employed in practicing the present invention.
Preferred sequences are those that are useful in diagnostic and/or therapeutic applications. Diagnostic applications include without limitation nucleic-acid-based and antibody-based methods for detecting bacterial infection. Therapeutic applications include without limitation vaccines, passive immunotherapy, and drug treatments directed against gene products that are both unique to bacteria and essential for growth and/or replication of bacteria.
Identification of Nucleic Acids Encoding Vaccine Components and Targets for Agents Effective Against S. pneumoniae 
The disclosed S. pneumoniae genome sequence includes segments that direct the synthesis of ribonucleic acids and polypeptides, as well as origins of replication, promoters, other types of regulatory sequences, and intergenic nucleic acids. The invention encompasses nucleic acids encoding immunogenic components of vaccines and targets for agents effective against S. pneumoniae. Identification of said immunogenic components involved in the determination of the function of the disclosed sequences, which can be achieved using a variety of approaches. Non-limiting examples of these approaches are described briefly below.
Homology to Known Sequences:
Computer-assisted comparison of the disclosed S. pneumoniae sequences with previously reported sequences present in publicly available databases is useful for identifying functional S. pneumoniae nucleic acid and polypeptide sequences. It will be understood that protein-coding sequences, for example, may be compared as a whole, and that a high degree of sequence homology between two proteins (such as for example, >80–90%) at the amino acid level indicates that the two proteins also possess some degree of functional homology, such as, for example, among enzymes involved in metabolism, DNA synthesis, or cell wall synthesis, and proteins involved in transport, cell division, etc. In addition, many structural features of particular protein classes have been identified and correlate with specific consensus sequences, such as, for example, binding domains for nucleotides, DNA, metal ions, and other small molecules; sites for covalent modifications such as phosphorylation, acylation, and the like; sites of protein:protein interactions, etc. These consensus sequences may be quite short and thus may represent only a fraction of the entire protein-coding sequence. Identification of such a feature in an S. pneumoniae sequence is therefore useful in determining the function of the encoded protein and identifying useful targets of antibacterial drugs.
Of particular relevance to the present invention are structural features that are common to secretory, transmembrane, and surface proteins, including secretion signal peptides and hydrophobic transmembrane domains. S. pneumoniae proteins identified as containing putative signal sequences and/or transmembrane domains are useful as immunogenic components of vaccines.
Targets for therapeutic drugs according to the invention include, but are not limited to, polypeptides of the invention, whether unique to S. pneumoniae or not, that are essential for growth and/or viability of S. pneumoniae under at least one growth condition. Polypeptides essential for growth and/or viability can be determined by examining the effect of deleting and/or disrupting the genes, i.e., by so-called gene “knockout”. Alternatively, genetic footprinting can be used (Smith et al., 1995, Proc. Natl. Acad. Sci. USA 92:5479–6433; Published International Application WO 94/26933; U.S. Pat. No. 5,612,180). Still other methods for assessing essentiality includes the ability to isolate conditional lethal mutations in the specific gene (e.g., temperature sensitive mutations). Other useful targets for therapeutic drugs, which include polypeptides that are not essential for growth or viability per se but lead to loss of viability of the cell, can be used to target therapeutic agents to cells.
Strain-Specific Sequences:
Because of the evolutionary relationship between different S. pneumoniae strains, it is believed that the presently disclosed S. pneumoniae sequences are useful for identifying, and/or discriminating between, previously known and new S. pneumoniae strains. It is believed that other S. pneumoniae strains will exhibit at least 70% sequence homology with the presently disclosed sequence. Systematic and routine analyses of DNA sequences derived from samples containing S. pneumoniae strains, and comparison with the present sequence allows for the identification of sequences that can be used to discriminate between strains, as well as those that are common to all S. pneumoniae strains. In one embodiment, the invention provides nucleic acids, including probes, and peptide and polypeptide sequences that discriminate between different strains of S. pneumoniae. Strain-specific components can also be identified functionally by their ability to elicit or react with antibodies that selectively recognize one or more S. pneumoniae strains.
In another embodiment, the invention provides nucleic acids, including probes, and peptide and polypeptide sequences that are common to all S. pneumoniae strains but are not found in other bacterial species.
S. pneumoniae Polypeptides
This invention encompasses isolated S. pneumoniae polypeptides encoded by the disclosed S. pneumoniae genomic sequences, including the polypeptides of the invention contained in the Sequence Listing. Polypeptides of the invention are preferably at least 5 amino acid residues in length. Using the DNA sequence information provided herein, the amino acid sequences of the polypeptides encompassed by the invention can be deduced using methods well-known in the art. It will be understood that the sequence of an entire nucleic acid encoding an S. pneumoniae polypeptide can be isolated and identified based on an ORF that encodes only a fragment of the cognate protein-coding region. This can be achieved, for example, by using the isolated nucleic acid encoding the ORF, or fragments thereof, to prime a polymerase chain reaction with genomic S. pneumoniae DNA as template; this is followed by sequencing the amplified product.
The polypeptides of the present invention, including function-conservative variants of the disclosed ORFs, may be isolated from wild-type or mutant S. pneumoniae cells, or from heterologous organisms or cells (including, but not limited to, bacteria, fungi, insect, plant, and mammalian cells) including S. pneumoniae into which a S. pneumoniae-derived protein-coding sequence has been introduced and expressed. Furthermore, the polypeptides may be part of recombinant fusion proteins.
S. pneumoniae polypeptides of the invention can be chemically synthesized using commercially automated procedures such as those referenced herein, including, without limitation, exclusive solid phase synthesis, partial solid phase methods, fragment condensation or classical solution synthesis. The polypeptides are preferably prepared by solid phase peptide synthesis as described by Merrifield, 1963, J. Am. Chem. Soc. 85:2149. The synthesis is carried out with amino acids that are protected at the alpha-amino terminus. Trifunctional amino acids with labile side-chains are also protected with suitable groups to prevent undesired chemical reactions from occurring during the assembly of the polypeptides. The alpha-amino protecting group is selectively removed to allow subsequent reaction to take place at the amino-terminus. The conditions for the removal of the alpha-amino protecting group do not remove the side-chain protecting groups.
The alpha-amino protecting groups are those known to be useful in the art of stepwise polypeptide synthesis. Included are acyl type protecting groups, e.g., formyl, trifluoroacetyl, acetyl, aromatic urethane type protecting groups, e.g., benzyloxycarbonyl (Cbz), substituted benzyloxycarbonyl and 9-fluorenylmethyloxycarbonyl (Fmoc), aliphatic urethane protecting groups, e.g., t-butyloxycarbonyl (Boc), isopropyloxycarbonyl, cyclohexyloxycarbonyl, and alkyl type protecting groups, e.g., benzyl, triphenylmethyl. The preferred protecting group is Boc. The side-chain protecting groups for Tyr include tetrahydropyranyl, tert-butyl, trityl, benzyl, Cbz, 4-Br-Cbz and 2,6-dichlorobenzyl. The preferred side-chain protecting group for Tyr is 2,6-dichlorobenzyl. The side-chain protecting groups for Asp include benzyl, 2,6-dichlorobenzyl, methyl, ethyl and cyclohexyl. The preferred side-chain protecting group for Asp is cyclohexyl. The side-chain protecting groups for Thr and Ser include acetyl, benzoyl, trityl, tetrahydropyranyl, benzyl, 2,6-dichlorobenzyl and Cbz. The preferred protecting group for Thr and Ser is benzyl. The side-chain protecting groups for Arg include nitro, Tos, Cbz, adamantyloxycarbonyl and Boc. The preferred protecting group for Arg is Tos. The side-chain amino group of Lys may be protected with Cbz, 2-Cl-Cbz, Tos or Boc. The 2-Cl-Cbz group is the preferred protecting group for Lys.
The side-chain protecting groups selected must remain intact during coupling and not be removed during the deprotection of the amino-terminus protecting group or during coupling conditions. The side-chain protecting groups must also be removable upon the completion of synthesis, using reaction conditions that will not alter the finished polypeptide.
Solid phase synthesis is usually carried out from the carboxy-terminus by coupling the alpha-amino protected (side-chain protected) amino acid to a suitable solid support. An ester linkage is formed when the attachment is made to a chloromethyl or hydroxymethyl resin, and the resulting polypeptide will have a free carboxyl group at the C-terminus. Alternatively, when a benzhydrylamine or p-methylbenzhydrylamine resin is used, an amide bond is formed and the resulting polypeptide will have a carboxamide group at the C-terminus. These resins are commercially available, and their preparation was described by Stewart et al., 1984, Solid Phase Peptide Synthesis (2nd Edition), Pierce Chemical Co., Rockford, Ill.
The C-terminal amino acid, protected at the side chain if necessary and at the alpha-amino group, is coupled to the benzhydrylamine resin using various activating agents including dicyclohexylcarbodiimide (DCC), N,N′-diisopropyl-carbodiimide and carbonyldiimidazole. Following the attachment to the resin support, the alpha-amino protecting group is removed using trifluoroacetic acid (TFA) or HCl in dioxane at a temperature between 0 and 25° C. Dimethylsulfide is added to the TFA after the introduction of methionine (Met) to suppress possible S-alkylation. After removal of the alpha-amino protecting group, the remaining protected amino acids are coupled stepwise in the required order to obtain the desired sequence.
Various activating agents can be used for the coupling reactions including DCC, N,N′-diisopropyl-carbodiimide, benzotriazol-1-yl-oxy-tris-(dimethylamino)-phosphonium hexa-fluorophosphate (BOP) and DCC-hydroxybenzotriazole (HOBt). Each protected amino acid is used in excess (>2.0 equivalents), and the couplings are usually carried out in N-methylpyrrolidone (NMP) or in DMF, CH2Cl2 or mixtures thereof. The extent of completion of the coupling reaction is monitored at each stage, e.g., by the ninhydrin reaction as described by Kaiser et al., 1970, Anal. Biochem. 34:595. In cases where incomplete coupling is found, the coupling reaction is repeated. The coupling reactions can be performed automatically with commercially available instruments.
After the entire assembly of the desired polypeptide, the polypeptide-resin is cleaved with a reagent such as liquid HF for 1–2 hours at 0° C., which cleaves the polypeptide from the resin and removes all side-chain protecting groups. A scavenger such as anisole is usually used with the liquid HF to prevent cations formed during the cleavage from alkylating the amino acid residues present in the polypeptide. The polypeptide-resin may be deprotected with TFA/dithioethane prior to cleavage if desired.
Side-chain to side-chain cyclization on the solid support requires the use of an orthogonal protection scheme which enables selective cleavage of the side-chain functions of acidic amino acids (e.g., Asp) and the basic amino acids (e.g., Lys). The 9-fluorenylmethyl (Fm) protecting group for the side-chain of Asp and the 9-fluorenylmethyloxycarbonyl (Fmoc) protecting group for the side-chain of Lys can be used for this purpose. In these cases, the side-chain protecting groups of the Boc-protected polypeptide-resin are selectively removed with piperidine in DMF. Cyclization is achieved on the solid support using various activating agents including DCC, DCC/HOBt or BOP. The HF reaction is carried out on the cyclized polypeptide-resin as described above.
Methods for polypeptide purification are well-known in the art, including, without limitation, preparative disc-gel electrophoresis, isoelectric focusing, HPLC, reversed-phase HPLC, gel filtration, ion exchange and partition chromatography, and countercurrent distribution. For some purposes, it is preferable to produce the polypeptide in a recombinant system in which the S. pneumoniae protein contains an additional sequence tag that facilitates purification, such as, but not limited to, a polyhistidine sequence. The polypeptide can then be purified from a crude lysate of the host cell by chromatography on an appropriate solid-phase matrix. Alternatively, antibodies produced against a S. pneumoniae protein or against peptides derived therefrom can be used as purification reagents. Other purification methods are possible.
The present invention also encompasses derivatives and homologues of S. pneumoniae-encoded polypeptides. For some purposes, nucleic acid sequences encoding the peptides may be altered by substitutions, additions, or deletions that provide for functionally equivalent molecules, i.e., function-conservative variants. For example, one or more amino acid residues within the sequence can be substituted by another amino acid of similar properties, such as, for example, positively charged amino acids (arginine, lysine, and histidine); negatively charged amino acids (aspartate and glutamate); polar neutral amino acids; and non-polar amino acids. The isolated polypeptides may be modified by, for example, phosphorylation, sulfation, acylation, or other protein modifications. They may also be modified with a label capable of providing a detectable signal, either directly or indirectly, including, but not limited to, radioisotopes and fluorescent compounds.
To identify S. pneumoniae-derived polypeptides for use in the present invention, essentially the complete genomic sequence of a virulent, methicillin-resistant isolate of Streptococcus pneumoniae isolate was analyzed. While, in very rare instances, a nucleic acid sequencing error may be revealed, resolving a rare sequencing error is well within the art, and such an occurrence will not prevent one skilled in the art from practicing the invention.
Also encompassed are any S. pneumoniae polypeptide sequences that are contained within the open reading frames (ORFs), including complete protein-coding sequences, of which any of SEQ ID NO: 2662–SEQ ID NO: 5322 forms a part. Table 2, which is appended herewith and which forms part of the present specification, provides a putative identification of the particular function of a polypeptide which is encoded by each ORF. As a result, one skilled in the art can use the polypeptides of the present invention for commercial and industrial purposes consistent with the type of putative identification of the polypeptide.
The present invention provides a library of S. Pneumoniae-derived polypeptide sequences, and a corresponding library of nucleic acid sequences encoding the polypeptides, wherein the polypeptides themselves, or polypeptides contained within ORFs of which they form a part, comprise sequences that are contemplated for use as components of vaccines. Non-limiting examples of such sequences are listed by SEQ ID NO in Table 2, which is appended herewith and which forms part of the present specification.
The present invention also provides a library of S. pneumoniae-derived polypeptide sequences, and a corresponding library of nucleic acid sequences encoding the polypeptides, wherein the polypeptides themselves, or polypeptides contained within ORFs of which they form a part, comprise sequences lacking homology to any known prokaryotic or eukaryotic sequences. Such libraries provide probes, primers, and markers which can be used to diagnose S. pneumoniae infection, including use as markers in epidemiological studies. Non-limiting examples of such sequences are listed by SEQ ID NO in Table 2, which is appended
The present invention also provides a library of S. pneumoniae-derived polypeptide sequences, and a corresponding library of nucleic acid sequences encoding the polypeptides, wherein the polypeptides themselves, or polypeptides contained within ORFs of which they form a part, comprise targets for therapeutic drugs.
Specific Example: Determination of Candidate Protein Antigens for Antibody and Vaccine Development
The selection of candidate protein antigens for vaccine development can be derived from the nucleic acids encoding S. pneumoniae polypeptides. First, the ORF's can be analyzed for homology to other known exported or membrane proteins and analyzed using the discriminant analysis described by Klein, et al. (Klein, P., Kanehsia, M., and DeLisi, C. (1985) Biochimica et Biophysica Acta 815, 468–476) for predicting exported and membrane proteins.
Homology searches can be performed using the BLAST algorithm contained in the Wisconsin Sequence Analysis Package (Genetics Computer Group, University Research Park, 575 Science Drive, Madison, Wis. 53711) to compare each predicted ORF amino acid sequence with all sequences found in the current GenBank, SWISS-PROT and PIR databases. BLAST searches for local alignments between the ORF and the databank sequences and reports a probability score which indicates the probability of finding this sequence by chance in the database. ORF's with significant homology (e.g. probabilities lower than 1×10−6 that the homology is only due to random chance) to membrane or exported proteins represent protein antigens for vaccine development. Possible functions can be provided to S. pneumoniae genes based on sequence homology to genes cloned in other organisms.
Discriminant analysis (Klein, et al. supra) can be used to examine the ORF amino acid sequences. This algorithm uses the intrinsic information contained in the ORF amino acid sequence and compares it to information derived from the properties of known membrane and exported proteins. This comparison predicts which proteins will be exported, membrane associated or cytoplasmic. ORF amino acid sequences identified as exported or membrane associated by this algorithm are likely protein antigens for vaccine development.
Production of Fragments and Analogs of S. pneumoniae Nucleic Acids and Polypeptides
Based on the discovery of the S. pneumoniae gene products of the invention provided in the Sequence Listing, one skilled in the art can alter the disclosed structure (of S. pneumoniae genes), e.g., by producing fragments or analogs, and test the newly produced structures for activity. Examples of techniques known to those skilled in the relevant art which allow the production and testing of fragments and analogs are discussed below. These, or analogous methods can be used to make and screen libraries of polypeptides, e.g., libraries of random peptides or libraries of fragments or analogs of cellular proteins for the ability to bind S. pneumoniae polypeptides. Such screens are useful for the identification of inhibitors of S. pneumoniae. 
Generation of Fragments
Fragments of a protein can be produced in several ways, e.g., recombinantly, by proteolytic digestion, or by chemical synthesis. Internal or terminal fragments of a polypeptide can be generated by removing one or more nucleotides from one end (for a terminal fragment) or both ends (for an internal fragment) of a nucleic acid which encodes the polypeptide. Expression of the mutagenized DNA produces polypeptide fragments. Digestion with “end-nibbling” endonucleases can thus generate DNA's which encode an array of fragments. DNA's which encode fragments of a protein can also be generated by random shearing, restriction digestion or a combination of the above-discussed methods.
Fragments can also be chemically synthesized using techniques known in the art such as conventional Merrifield solid phase f-Moc or t-Boc chemistry. For example, peptides of the present invention may be arbitrarily divided into fragments of desired length with no overlap of the fragments, or divided into overlapping fragments of a desired length.
Alteration of Nucleic Acids and Polypeptides: Random Methods
Amino acid sequence variants of a protein can be prepared by random mutagenesis of DNA which encodes a protein or a particular domain or region of a protein. Useful methods include PCR mutagenesis and saturation mutagenesis. A library of random amino acid sequence variants can also be generated by the synthesis of a set of degenerate oligonucleotide sequences. (Methods for screening proteins in a library of variants are elsewhere herein).
PCR Mutagenesis
In PCR mutagenesis, reduced Taq polymerase fidelity is used to introduce random mutations into a cloned fragment of DNA (Leung et al., 1989, Technique 1:11–15). The DNA region to be mutagenized is amplified using the polymerase chain reaction (PCR) under conditions that reduce the fidelity of DNA synthesis by Taq DNA polymerase, e.g., by using a dGTP/dATP ratio of five and adding Mn2+ to the PCR reaction. The pool of amplified DNA fragments are inserted into appropriate cloning vectors to provide random mutant libraries.
Saturation Mutagenesis
Saturation mutagenesis allows for the rapid introduction of a large number of single base substitutions into cloned DNA fragments (Mayers et al., 1985, Science 229:242). This technique includes generation of mutations, e.g., by chemical treatment or irradiation of single-stranded DNA in vitro, and synthesis of a complimentary DNA strand. The mutation frequency can be modulated by modulating the severity of the treatment, and essentially all possible base substitutions can be obtained. Because this procedure does not involve a genetic selection for mutant fragments both neutral substitutions, as well as those that alter function, are obtained. The distribution of point mutations is not biased toward conserved sequence elements.
Degenerate Oligonucleotides
A library of homologs can also be generated from a set of degenerate oligonucleotide sequences. Chemical synthesis of a degenerate sequences can be carried out in an automatic DNA synthesizer, and the synthetic genes then ligated into an appropriate expression vector. The synthesis of degenerate oligonucleotides is known in the art (see for example, Narang, S A (1983) Tetrahedron 39:3; Itakura et al. (1981) Recombinant DNA, Proc 3rd Cleveland Sympos. Macromolecules, ed. A G Walton, Amsterdam: Elsevier pp273–289; Itakura et al. (1984) Annu. Rev. Biochem. 53:323; Itakura et al. (1984) Science 198:1056; Ike et al. (1983) Nucleic Acid Res. 11:477. Such techniques have been employed in the directed evolution of other proteins (see, for example, Scott et al. (1990) Science 249:386–390; Roberts et al. (1992) PNAS 89:2429–2433; Devlin et al. (1990) Science 249: 404–406; Cwirla et al. (1990) PNAS 87: 6378–6382; as well as U.S. Pat. Nos. 5,223,409, 5,198,346, and 5,096,815).
Alteration of Nucleic Acids and Polypeptides: Methods for Directed Mutagenesis
Non-random or directed, mutagenesis techniques can be used to provide specific sequences or mutations in specific regions. These techniques can be used to create variants which include, e.g., deletions, insertions, or substitutions, of residues of the known amino acid sequence of a protein. The sites for mutation can be modified individually or in series, e.g., by (1) substituting first with conserved amino acids and then with more radical choices depending upon results achieved, (2) deleting the target residue, or (3) inserting residues of the same or a different class adjacent to the located site, or combinations of options 1–3.
Alanine Scanning Mutagenesis
Alanine scanning mutagenesis is a useful method for identification of certain residues or regions of the desired protein that are preferred locations or domains for mutagenesis, Cunningham and Wells (Science 244:1081–1085, 1989). In alanine scanning, a residue or group of target residues are identified (e.g., charged residues such as Arg, Asp, His, Lys, and Glu) and replaced by a neutral or negatively charged amino acid (most preferably alanine or polyalanine). Replacement of an amino acid can affect the interaction of the amino acids with the surrounding aqueous environment in or outside the cell. Those domains demonstrating functional sensitivity to the substitutions are then refined by introducing further or other variants at or for the sites of substitution. Thus, while the site for introducing an amino acid sequence variation is predetermined, the nature of the mutation per se need not be predetermined. For example, to optimize the performance of a mutation at a given site, alanine scanning or random mutagenesis may be conducted at the target codon or region and the expressed desired protein subunit variants are screened for the optimal combination of desired activity.
Oligonucleotide-Mediated Mutagenesis
Oligonucleotide-mediated mutagenesis is a useful method for preparing substitution, deletion, and insertion variants of DNA, see, e.g., Adelman et al., (DNA 2:183, 1983). Briefly, the desired DNA is altered by hybridizing an oligonucleotide encoding a mutation to a DNA template, where the template is the single-stranded form of a plasmid or bacteriophage containing the unaltered or native DNA sequence of the desired protein. After hybridization, a DNA polymerase is used to synthesize an entire second complementary strand of the template that will thus incorporate the oligonucleotide primer, and will code for the selected alteration in the desired protein DNA. Generally, oligonucleotides of at least 25 nucleotides in length are used. An optimal oligonucleotide will have 12 to 15 nucleotides that are completely complementary to the template on either side of the nucleotide(s) coding for the mutation. This ensures that the oligonucleotide will hybridize properly to the single-stranded DNA template molecule. The oligonucleotides are readily synthesized using techniques known in the art such as that described by Crea et al. (Proc. Natl. Acad. Sci. USA, 75: 5765[1978]).
Cassette Mutagenesis
Another method for preparing variants, cassette mutagenesis, is based on the technique described by Wells et al. (Gene, 34:315[1985]). The starting material is a plasmid (or other vector) which includes the protein subunit DNA to be mutated. The codon(s) in the protein subunit DNA to be mutated are identified. There must be a unique restriction endonuclease site on each side of the identified mutation site(s). If no such restriction sites exist, they may be generated using the above-described oligonucleotide-mediated mutagenesis method to introduce them at appropriate locations in the desired protein subunit DNA. After the restriction sites have been introduced into the plasmid, the plasmid is cut at these sites to linearize it. A double-stranded oligonucleotide encoding the sequence of the DNA between the restriction sites but containing the desired mutation(s) is synthesized using standard procedures. The two strands are synthesized separately and then hybridized together using standard techniques. This double-stranded oligonucleotide is referred to as the cassette. This cassette is designed to have 3′ and 5′ ends that are comparable with the ends of the linearized plasmid, such that it can be directly ligated to the plasmid. This plasmid now contains the mutated desired protein subunit DNA sequence.
Combinatorial Mutagenesis
Combinatorial mutagenesis can also be used to generate mutants (Ladner et al., WO 88/06630). In this method, the amino acid sequences for a group of homologs or other related proteins are aligned, preferably to promote the highest homology possible. All of the amino acids which appear at a given position of the aligned sequences can be selected to create a degenerate set of combinatorial sequences. The variegated library of variants is generated by combinatorial mutagenesis at the nucleic acid level, and is encoded by a variegated gene library. For example, a mixture of synthetic oligonucleotides can be enzymatically ligated into gene sequences such that the degenerate set of potential sequences are expressible as individual peptides, or alternatively, as a set of larger fusion proteins containing the set of degenerate sequences.
Other Modifications of S. pneumoniae Nucleic Acids and Polypeptides
It is possible to modify the structure of an S. pneumoniae polypeptide for such purposes as increasing solubility, enhancing stability (e.g., shelf life ex vivo and resistance to proteolytic degradation in vivo). A modified S. pneumoniae protein or peptide can be produced in which the amino acid sequence has been altered, such as by amino acid substitution, deletion, or addition as described herein.
An S. pneumoniae peptide can also be modified by substitution of cysteine residues preferably with alanine, serine, threonine, leucine or glutamic acid residues to minimize dimerization via disulfide linkages. In addition, amino acid side chains of fragments of the protein of the invention can be chemically modified. Another modification is cyclization of the peptide.
In order to enhance stability and/or reactivity, an S. pneumoniae polypeptide can be modified to incorporate one or more polymorphisms in the amino acid sequence of the protein resulting from any natural allelic variation. Additionally, D-amino acids, non-natural amino acids, or non-amino acid analogs can be substituted or added to produce a modified protein within the scope of this invention. Furthermore, an S. pneumoniae polypeptide can be modified using polyethylene glycol (PEG) according to the method of A. Sehon and co-workers (Wie et al., supra) to produce a protein conjugated with PEG. In addition, PEG can be added during chemical synthesis of the protein. Other modifications of S. pneumoniae proteins include reduction/alkylation (Tarr, Methods of Protein Microcharacterization, J. E. Silver ed., Humana Press, Clifton N.J. 155–194 (1986)); acylation (Tarr, supra); chemical coupling to an appropriate carrier (Mishell and Shiigi, eds, Selected Methods in Cellular Immunology, W H Freeman, San Francisco, Calif. (1980), U.S. Pat. No. 4,939,239; or mild formalin treatment (Marsh, (1971) Int. Arch. of Allergy and Appl. Immunol., 41: 199–215).
To facilitate purification and potentially increase solubility of an S. pneumoniae protein or peptide, it is possible to add an amino acid fusion moiety to the peptide backbone. For example, hexa-histidine can be added to the protein for purification by immobilized metal ion affinity chromatography (Hochuli, E. et al., (1988) Bio/Technology, 6: 1321–1325). In addition, to facilitate isolation of peptides free of irrelevant sequences, specific endoprotease cleavage sites can be introduced between the sequences of the fusion moiety and the peptide.
To potentially aid proper antigen processing of epitopes within an S. pneumoniae polypeptide, canonical protease sensitive sites can be engineered between regions, each comprising at least one epitope via recombinant or synthetic methods. For example, charged amino acid pairs, such as KK or RR, can be introduced between regions within a protein or fragment during recombinant construction thereof. The resulting peptide can be rendered sensitive to cleavage by cathepsin and/or other trypsin-like enzymes which would generate portions of the protein containing one or more epitopes. In addition, such charged amino acid residues can result in an increase in the solubility of the peptide.
Primary Methods for Screening Polypeptides and Analogs
Various techniques are known in the art for screening generated mutant gene products. Techniques for screening large gene libraries often include cloning the gene library into replicable expression vectors, transforming appropriate cells with the resulting library of vectors, and expressing the genes under conditions in which detection of a desired activity, e.g., in this case, binding to S. pneumoniae polypeptide or an interacting protein, facilitates relatively easy isolation of the vector encoding the gene whose product was detected. Each of the techniques described below is amenable to high through-put analysis for screening large numbers of sequences created, e.g., by random mutagenesis techniques.
Two Hybrid Systems
Two hybrid assays such as the system described above (as with the other screening methods described herein), can be used to identify polypeptides, e.g., fragments or analogs of a naturally-occurring S. pneumoniae polypeptide, e.g., of cellular proteins, or of randomly generated polypeptides which bind to an S. pneumoniae protein. (The S. pneumoniae domain is used as the bait protein and the library of variants are expressed as prey fusion proteins.) In an analogous fashion, a two hybrid assay (as with the other screening methods described herein), can be used to find polypeptides which bind a S. pneumoniae polypeptide.
Display Libraries
In one approach to screening assays, the candidate peptides are displayed on the surface of a cell or viral particle, and the ability of particular cells or viral particles to bind an appropriate receptor protein via the displayed product is detected in a “panning assay”. For example, the gene library can be cloned into the gene for a surface membrane protein of a bacterial cell, and the resulting fusion protein detected by panning (Ladner et al., WO 88/06630; Fuchs et al. (1991) Bio/Technology 9:1370–1371; and Goward et al. (1992) TIBS 18:136–140). In a similar fashion, a detectably labeled ligand can be used to score for potentially functional peptide homologs. Fluorescently labeled ligands, e.g., receptors, can be used to detect homologs which retain ligand-binding activity. The use of fluorescently labeled ligands, allows cells to be visually inspected and separated under a fluorescence microscope, or, where the morphology of the cell permits, to be separated by a fluorescence-activated cell sorter.
A gene library can be expressed as a fusion protein on the surface of a viral particle. For instance, in the filamentous phage system, foreign peptide sequences can be expressed on the surface of infectious phage, thereby conferring two significant benefits. First, since these phage can be applied to affinity matrices at concentrations well over 1013 phage per milliliter, a large number of phage can be screened at one time. Second, since each infectious phage displays a gene product on its surface, if a particular phage is recovered from an affinity matrix in low yield, the phage can be amplified by another round of infection. The group of almost identical E. coli filamentous phages M13, fd., and fl are most often used in phage display libraries. Either of the phage gIII or gVIII coat proteins can be used to generate fusion proteins without disrupting the ultimate packaging of the viral particle. Foreign epitopes can be expressed at the NH2-terminal end of pIII and phage bearing such epitopes recovered from a large excess of phage lacking this epitope (Ladner et al. PCT publication WO 90/02909; Garrard et al., PCT publication WO 92/09690; Marks et al. (1992) J. Biol. Chem. 267:16007–16010; Griffiths et al. (1993) EMBO J. 12:725–734; Clackson et al. (1991) Nature 352:624–628; and Barbas et al. (1992) PNAS 89:4457–4461).
A common approach uses the maltose receptor of E. coli (the outer membrane protein, LamB) as a peptide fusion partner (Charbit et al. (1986) EMBO 5, 3029–3037). Oligonucleotides have been inserted into plasmids encoding the LamB gene to produce peptides fused into one of the extracellular loops of the protein. These peptides are available for binding to, ligands, e.g., to antibodies, and can elicit an immune response when the cells are administered to animals. Other cell surface proteins, e.g., OmpA (Schorr et al. (1991) Vaccines 91, pp. 387–392), PhoE (Agterberg, et al. (1990) Gene 88, 37–45), and PAL (Fuchs et al. (1991) Bio/Tech 9, 1369–1372), as well as large bacterial surface structures have served as vehicles for peptide display. Peptides can be fused to pilin, a protein which polymerizes to form the pilus-a conduit for interbacterial exchange of genetic information (Thiry et al. (1989) Appl. Environ. Microbiol. 55, 984–993). Because of its role in interacting with other cells, the pilus provides a useful support for the presentation of peptides to the extracellular environment. Another large surface structure used for peptide display is the bacterial motive organ, the flagellum. Fusion of peptides to the subunit protein flagellin offers a dense array of many peptide copies on the host cells (Kuwajima et al. (1988) Bio/Tech. 6, 1080–1083). Surface proteins of other bacterial species have also served as peptide fusion partners. Examples include the Staphylococcus protein A and the outer membrane IgA protease of Neisseria (Hansson et al. (1992) J. Bacteriol. 174, 4239–4245 and Klauser et al. (1990) EMBO J. 9, 1991–1999).
In the filamentous phage systems and the LamB system described above, the physical link between the peptide and its encoding DNA occurs by the containment of the DNA within a particle (cell or phage) that carries the peptide on its surface. Capturing the peptide captures the particle and the DNA within. An alternative scheme uses the DNA-binding protein Lacd to form a link between peptide and DNA (Cull et al. (1992) PNAS USA 89:1865–1869). This system uses a plasmid containing the LacI gene with an oligonucleotide cloning site at its 3′-end. Under the controlled induction by arabinose, a LacI-peptide fusion protein is produced. This fusion retains the natural ability of LacI to bind to a short DNA sequence known as LacO operator (LacO). By installing two copies of LacO on the expression plasmid, the LacI-peptide fusion binds tightly to the plasmid that encoded it. Because the plasmids in each cell contain only a single oligonucleotide sequence and each cell expresses only a single peptide sequence, the peptides become specifically and stablely associated with the DNA sequence that directed its synthesis. The cells of the library are gently lysed and the peptide-DNA complexes are exposed to a matrix of immobilized receptor to recover the complexes containing active peptides. The associated plasmid DNA is then reintroduced into cells for amplification and DNA sequencing to determine the identity of the peptide ligands. As a demonstration of the practical utility of the method, a large random library of dodecapeptides was made and selected on a monoclonal antibody raised against the opioid peptide dynorphin B. A cohort of peptides was recovered, all related by a consensus sequence corresponding to a six-residue portion of dynorphin B. (Cull et al. (1992) Proc. Natl. Acad. Sci. U.S.A. 89–1869)
This scheme, sometimes referred to as peptides-on-plasmids, differs in two important ways from the phage display methods. First, the peptides are attached to the C-terminus of the fusion protein, resulting in the display of the library members as peptides having free carboxy termini. Both of the filamentous phage coat proteins, pIII and pVIII, are anchored to the phage through their C-termini, and the guest peptides are placed into the outward-extending N-terminal domains. In some designs, the phage-displayed peptides are presented right at the amino terminus of the fusion protein. (Cwirla, et al. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 6378–6382) A second difference is the set of biological biases affecting the population of peptides actually present in the libraries. The LacI fusion molecules are confined to the cytoplasm of the host cells. The phage coat fusions are exposed briefly to the cytoplasm during translation but are rapidly secreted through the inner membrane into the periplasmic compartment, remaining anchored in the membrane by their C-terminal hydrophobic domains, with the N-termini, containing the peptides, protruding into the periplasm while awaiting assembly into phage particles. The peptides in the LacI and phage libraries may differ significantly as a result of their exposure to different proteolytic activities. The phage coat proteins require transport across the inner membrane and signal peptidase processing as a prelude to incorporation into phage. Certain peptides exert a deleterious effect on these processes and are underrepresented in the libraries (Gallop et al. (1994) J. Med. Chem. 37(9): 1233–1251). These particular biases are not a factor in the LacI display system.
The number of small peptides available in recombinant random libraries is enormous. Libraries of 107–109 independent clones are routinely prepared. Libraries as large as 1011 recombinants have been created, but this size approaches the practical limit for clone libraries. This limitation in library size occurs at the step of transforming the DNA containing randomized segments into the host bacterial cells. To circumvent this limitation, an in vitro system based on the display of nascent peptides in polysome complexes has recently been developed. This display library method has the potential of producing libraries 3–6 orders of magnitude larger than the currently available phage/phagemid or plasmid libraries. Furthermore, the construction of the libraries, expression of the peptides, and screening, is done in an entirely cell-free format.
In one application of this method (Gallop et al. (1994) J. Med. Chem. 37(9): 1233–1251), a molecular DNA library encoding 1012 decapeptides was constructed and the library expressed in an E. coli S30 in vitro coupled transcription/translation system. Conditions were chosen to stall the ribosomes on the mRNA, causing the accumulation of a substantial proportion of the RNA in polysomes and yielding complexes containing nascent peptides still linked to their encoding RNA. The polysomes are sufficiently robust to be affinity purified on immobilized receptors in much the same way as the more conventional recombinant peptide display libraries are screened. RNA from the bound complexes is recovered, converted to cDNA, and amplified by PCR to produce a template for the next round of synthesis and screening. The polysome display method can be coupled to the phage display system. Following several rounds of screening, cDNA from the enriched pool of polysomes was cloned into a phagemid vector. This vector serves as both a peptide expression vector, displaying peptides fused to the coat proteins, and as a DNA sequencing vector for peptide identification. By expressing the polysome-derived peptides on phage, one can either continue the affinity selection procedure in this format or assay the peptides on individual clones for binding activity in a phage ELISA, or for binding specificity in a completion phage ELISA (Barret, et al. (1992) Anal. Biochem 204,357–364). To identify the sequences of the active peptides one sequences the DNA produced by the phagemid host.
Secondary Screening of Polypeptides and Analogs
The high through-put assays described above can be followed by secondary screens in order to identify further biological activities which will, e.g., allow one skilled in the art to differentiate agonists from antagonists. The type of a secondary screen used will depend on the desired activity that needs to be tested. For example, an assay can be developed in which the ability to inhibit an interaction between a protein of interest and its respective ligand can be used to identify antagonists from a group of peptide fragments isolated though one of the primary screens described above.
Therefore, methods for generating fragments and analogs and testing them for activity are known in the art. Once the core sequence of interest is identified, it is routine for one skilled in the art to obtain analogs and fragments.
Peptide Mimetics of S. pneumoniae Polypeptides
The invention also provides for reduction of the protein binding domains of the subject S. pneumoniae polypeptides to generate mimetics, e.g. peptide or non-peptide agents. The peptide mimetics are able to disrupt binding of a polypeptide to its counter ligand, e.g., in the case of an S. pneumoniae polypeptide binding to a naturally occurring ligand. The critical residues of a subject S. pneumoniae polypeptide which are involved in molecular recognition of a polypeptide can be determined and used to generate S. pneumoniae-derived peptidomimetics which competitively or noncompetitively inhibit binding of the S. pneumoniae polypeptide with an interacting polypeptide (see, for example, European patent applications EP-412,762A and EP-B31,080A).
For example, scanning mutagenesis can be used to map the amino acid residues of a particular S. pneumoniae polypeptide involved in binding an interacting polypeptide, peptidomimetic compounds (e.g. diazepine or isoquinoline derivatives) can be generated which mimic those residues in binding to an interacting polypeptide, and which therefore can inhibit binding of an S. pneumoniae polypeptide to an interacting polypeptide and thereby interfere with the function of S. pneumoniae polypeptide. For instance, non-hydrolyzable peptide analogs of such residues can be generated using benzodiazepine (e.g., see Freidinger et al. in Peptides: Chemistry and Biology, G. R. Marshall ed., ESCOM Publisher: Leiden, Netherlands, 1988), azepine (e.g., see Huffman et al. in Peptides: Chemistry and Biology, G. R. Marshall ed., ESCOM Publisher: Leiden, Netherlands, 1988), substituted gama lactam rings (Garvey et al. in Peptides. Chemistry and Biology, G. R. Marshall ed., ESCOM Publisher: Leiden, Netherlands, 1988), keto-methylene pseudopeptides (Ewenson et al. (1986) J Med Chem 29:295; and Ewenson et al. in Peptides: Structure and Function (Proceedings of the 9th American Peptide Symposium) Pierce Chemical Co. Rockland, Ill., 1985), b-turn dipeptide cores (Nagai et al. (1985) Tetrahedron Lett 26:647; and Sato et al. (1986) J Chem Soc Perkin Trans 1:1231), and b-aminoalcohols (Gordon et al. (1985) Biochem Biophys Res Commun 126:419; and et al. (1986) Biochem Biophys Res Commun 134:71).
Vaccine Formulations for S. pneumoniae Nucleic Acids and Polypeptides
This invention also features vaccine compositions for protection against infection by S. pneumoniae or for treatment of S. pneumoniae infection, a gram-negative spiral microaerophilic bacterium. In one embodiment, the vaccine compositions contain one or more immunogenic components such as a surface protein from S. pneumoniae, or portion thereof, and a pharmaceutically acceptable carrier. Nucleic acids within the scope of the invention are exemplified by the nucleic acids of the invention contained in the Sequence Listing which encode S. pneumoniae surface proteins. Any nucleic acid encoding an immunogenic S. pneumoniae protein, or portion thereof, which is capable of expression in a cell, can be used in the present invention. These vaccines have therapeutic and prophylactic utilities.
One aspect of the invention provides a vaccine composition for protection against infection by S. pneumoniae which contains at least one immunogenic fragment of an S. pneumoniae protein and a pharmaceutically acceptable carrier. Preferred fragments include peptides of at least about 10 amino acid residues in length, preferably about 10–20 amino acid residues in length, and more preferably about 12–16 amino acid residues in length.
Immunogenic components of the invention can be obtained, for example, by screening polypeptides recombinantly produced from the corresponding fragment of the nucleic acid encoding the full-length S. pneumoniae protein. In addition, fragments can be chemically synthesized using techniques known in the art such as conventional Merrifield solid phase f-Moc or t-Boc chemistry.
In one embodiment, immunogenic components are identified by the ability of the peptide to stimulate T cells. Peptides which stimulate T cells, as determined by, for example, T cell proliferation or cytokine secretion are defined herein as comprising at least one T cell epitope. T cell epitopes are believed to be involved in initiation and perpetuation of the immune response to the protein allergen which is responsible for the clinical symptoms of allergy. These T cell epitopes are thought to trigger early events at the level of the T helper cell by binding to an appropriate HLA molecule on the surface of an antigen presenting cell, thereby stimulating the T cell subpopulation with the relevant T cell receptor for the epitope. These events lead to T cell proliferation, lymphokine secretion, local inflammatory reactions, recruitment of additional immune cells to the site of antigen/T cell interaction, and activation of the B cell cascade, leading to the production of antibodies. A T cell epitope is the basic element, or smallest unit of recognition by a T cell receptor, where the epitope comprises amino acids essential to receptor recognition (e.g., approximately 6 or 7 amino acid residues). Amino acid sequences which mimic those of the T cell epitopes are within the scope of this invention.
Screening immunogenic components can be accomplished using one or more of several different assays. For example, in vitro, peptide T cell stimulatory activity is assayed by contacting a peptide known or suspected of being immunogenic with an antigen presenting cell which presents appropriate MHC molecules in a T cell culture. Presentation of an immunogenic S. pneumoniae peptide in association with appropriate MHC molecules to T cells in conjunction with the necessary co-stimulation has the effect of transmitting a signal to the T cell that induces the production of increased levels of cytokines, particularly of interleukin-2 and interleukin-4. The culture supernatant can be obtained and assayed for interleukin-2 or other known cytokines. For example, any one of several conventional assays for interleukin-2 can be employed, such as the assay described in Proc. Natl. Acad. Sci USA, 86: 1333 (1989) the pertinent portions of which are incorporated herein by reference. A kit for an assay for the production of interferon is also available from Genzyme Corporation (Cambridge, Mass.).
Alternatively, a common assay for T cell proliferation entails measuring tritiated thymidine incorporation. The proliferation of T cells can be measured in vitro by determining the amount of 3H-labeled thymidine incorporated into the replicating DNA of cultured cells. Therefore, the rate of DNA synthesis and, in turn, the rate of cell division can be quantified.
Vaccine compositions of the invention containing immunogenic components (e.g., S. pneumoniae polypeptide or fragment thereof or nucleic acid encoding an S. pneumoniae polypeptide or fragment thereof) preferably include a pharmaceutically acceptable carrier. The term “pharmaceutically acceptable carrier” refers to a carrier that does not cause an allergic reaction or other untoward effect in patients to whom it is administered. Suitable pharmaceutically acceptable carriers include, for example, one or more of water, saline, phosphate buffered saline, dextrose, glycerol, ethanol and the like, as well as combinations thereof. Pharmaceutically acceptable carriers may further comprise minor amounts of auxiliary substances such as wetting or emulsifying agents, preservatives or buffers, which enhance the shelf life or effectiveness of the antibody. For vaccines of the invention containing S. pneumoniae polypeptides, the polypeptide is co-administered with a suitable adjuvant.
It will be apparent to those of skill in the art that the therapeutically effective amount of DNA or protein of this invention will depend, inter alia, upon the administration schedule, the unit dose of antibody administered, whether the protein or DNA is administered in combination with other therapeutic agents, the immune status and health of the patient, and the therapeutic activity of the particular protein or DNA.
Vaccine compositions are conventionally administered parenterally, e.g., by injection, either subcutaneously or intramuscularly. Methods for intramuscular immunization are described by Wolff et al. (1990) Science 247: 1465–1468 and by Sedegah et al. (1994) Immunology 91: 9866–9870. Other modes of administration include oral and pulmonary formulations, suppositories, and transdermal applications. Oral immunization is preferred over parenteral methods for inducing protection against infection by S. pneumoniae. Cain et. al. (1993) Vaccine 11: 637–642. Oral formulations include such normally employed excipients as, for example, pharmaceutical grades of mannitol, lactose, starch, magnesium stearate, sodium saccharine, cellulose, magnesium carbonate, and the like.
The vaccine compositions of the invention can include an adjuvant, including, but not limited to aluminum hydroxide; N-acetyl-muramyl-L-threonyl-D-isoglutamine (thr-MDP); N-acetyl-nor-muramyl-L-alanyl-D-isoglutamine (CGP 11637, referred to as nor-MDP); N-acetylmuramyl-L-alanyl-D-isoglutaminyl-L-alanine-2-(1′-2′-dipalmitoyl-sn-glycero-3-hydroxyphos-phoryloxy)-ethylamine (CGP 19835A, referred to a MTP-PE); RIBI, which contains three components from bacteria; monophosphoryl lipid A; trehalose dimycoloate; cell wall skeleton (MPL+TDM+CWS) in a 2% squalene/Tween 80 emulsion; and cholera toxin. Others which may be used are non-toxic derivatives of cholera toxin, including its B subunit, and/or conjugates or genetically engineered fusions of the S. pneumoniae polypeptide with cholera toxin or its B subunit, procholeragenoid, fungal polysaccharides, including schizophyllan, muramyl dipeptide, muramyl dipeptide derivatives, phorbol esters, labile toxin of E. coli, non-S. pneumoniae bacterial lysates, block polymers or saponins.
Other suitable delivery methods include biodegradable microcapsules or immuno-stimulating complexes (ISCOMs), cochleates, or liposomes, genetically engineered attenuated live vectors such as viruses or bacteria, and recombinant (chimeric) virus-like particles, e.g., bluetongue. The amount of adjuvant employed will depend on the type of adjuvant used. For example, when the mucosal adjuvant is cholera toxin, it is suitably used in an amount of 5 mg to 50 mg, for example 10 mg to 35 mg. When used in the form of microcapsules, the amount used will depend on the amount employed in the matrix of the microcapsule to achieve the desired dosage. The determination of this amount is within the skill of a person of ordinary skill in the art.
Carrier systems in humans may include enteric release capsules protecting the antigen from the acidic environment of the stomach, and including S. pneumoniae polypeptide in an insoluble form as fusion proteins. Suitable carriers for the vaccines of the invention are enteric coated capsules and polylactide-glycolide microspheres. Suitable diluents are 0.2 N NaHCO3 and/or saline.
Vaccines of the invention can be administered as a primary prophylactic agent in adults or in children, as a secondary prevention, after successful eradication of S. pneumoniae in an infected host, or as a therapeutic agent in the aim to induce an immune response in a susceptible host to prevent infection by S. pneumoniae. The vaccines of the invention are administered in amounts readily determined by persons of ordinary skill in the art. Thus, for adults a suitable dosage will be in the range of 10 mg to 10 g, preferably 10 mg to 100 mg. A suitable dosage for adults will also be in the range of 5 mg to 500 mg. Similar dosage ranges will be applicable for children. Those skilled in the art will recognize that the optimal dose may be more or less depending upon the patient's body weight, disease, the route of administration, and other factors. Those skilled in the art will also recognize that appropriate dosage levels can be obtained based on results with known oral vaccines such as, for example, a vaccine based on an E. coli lysate (6 mg dose daily up to total of 540 mg) and with an enterotoxigenic E. coli purified antigen (4 doses of 1 mg) (Schulman et al., J. Urol. 150:917–921 (1993); Boedecker et al., American Gastroenterological Assoc. 999:A-222 (1993)). The number of doses will depend upon the disease, the formulation, and efficacy data from clinical trials. Without intending any limitation as to the course of treatment, the treatment can be administered over 3 to 8 doses for a primary immunization schedule over 1 month (Boedeker, American Gastroenterological Assoc. 888:A-222 (1993)).
In a preferred embodiment, a vaccine composition of the invention can be based on a killed whole E. coli preparation with an immunogenic fragment of an S. pneumoniae protein of the invention expressed on its surface or it can be based on an E. coli lysate, wherein the killed E. coli acts as a carrier or an adjuvant.
It will be apparent to those skilled in the art that some of the vaccine compositions of the invention are useful only for preventing S. pneumoniae infection, some are useful only for treating S. pneumoniae infection, and some are useful for both preventing and treating S. pneumoniae infection. In a preferred embodiment, the vaccine composition of the invention provides protection against S. pneumoniae infection by stimulating humoral and/or cell-mediated immunity against S. pneumoniae. It should be understood that amelioration of any of the symptoms of S. pneumoniae infection is a desirable clinical goal, including a lessening of the dosage of medication used to treat S. pneumoniae-caused disease, or an increase in the production of antibodies in the serum or mucous of patients.
Antibodies Reactive with S. pneumoniae Polypeptides
The invention also includes antibodies specifically reactive with the subject S. pneumoniae polypeptide. Anti-protein/anti-peptide antisera or monoclonal antibodies can be made by standard protocols (See, for example, Antibodies: A Laboratory Manual ed. by Harlow and Lane (Cold Spring Harbor Press: 1988)). A mammal such as a mouse, a hamster or rabbit can be immunized with an immunogenic form of the peptide. Techniques for conferring immunogenicity on a protein or peptide include conjugation to carriers or other techniques well known in the art. An immunogenic portion of the subject S. pneumoniae polypeptide can be administered in the presence of adjuvant. The progress of immunization can be monitored by detection of antibody titers in plasma or serum. Standard ELISA or other immunoassays can be used with the immunogen as antigen to assess the levels of antibodies.
In a preferred embodiment, the subject antibodies are immunospecific for antigenic determinants of the S. pneumoniae polypeptides of the invention, e.g. antigenic determinants of a polypeptide of the invention contained in the Sequence Listing, or a closely related human or non-human mammalian homolog (e.g., 90% homologous, more preferably at least 95% homologous). In yet a further preferred embodiment of the invention, the anti-S. pneumoniae antibodies do not substantially cross react (i.e., react specifically) with a protein which is for example, less than 80% percent homologous to a sequence of the invention contained in the Sequence Listing. By “not substantially cross react”, it is meant that the antibody has a binding affinity for a non-homologous protein which is less than 10 percent, more preferably less than 5 percent, and even more preferably less than 1 percent, of the binding affinity for a protein of the invention contained in the Sequence Listing. In a most preferred embodiment, there is no cross-reactivity between bacterial and mammalian antigens.
The term antibody as used herein is intended to include fragments thereof which are also specifically reactive with S. pneumoniae polypeptides. Antibodies can be fragmented using conventional techniques and the fragments screened for utility in the same manner as described above for whole antibodies. For example, F(ab′)2 fragments can be generated by treating antibody with pepsin. The resulting F(ab′)2 fragment can be treated to reduce disulfide bridges to produce Fab′ fragments. The antibody of the invention is further intended to include bispecific and chimeric molecules having an anti-S. pneumoniae portion.
Both monoclonal and polyclonal antibodies (Ab) directed against S. pneumoniae polypeptides or S. pneumoniae polypeptide variants, and antibody fragments such as Fab′ and F(ab′)2, can be used to block the action of S. pneumoniae polypeptide and allow the study of the role of a particular S. pneumoniae polypeptide of the invention in aberrant or unwanted intracellular signaling, as well as the normal cellular function of the S. pneumoniae and by microinjection of anti-S. pneumoniae polypeptide antibodies of the present invention.
Antibodies which specifically bind S. pneumoniae epitopes can also be used in immunohistochemical staining of tissue samples in order to evaluate the abundance and pattern of expression of S. pneumoniae antigens. Anti S. pneumoniae polypeptide antibodies can be used diagnostically in immuno-precipitation and immuno-blotting to detect and evaluate S. pneumoniae levels in tissue or bodily fluid as part of a clinical testing procedure. Likewise, the ability to monitor S. pneumoniae polypeptide levels in an individual can allow determination of the efficacy of a given treatment regimen for an individual afflicted with such a disorder. The level of an S. pneumoniae polypeptide can be measured in cells found in bodily fluid, such as in urine samples or can be measured in tissue, such as produced by gastric biopsy. Diagnostic assays using anti-S. pneumoniae antibodies can include, for example, immunoassays designed to aid in early diagnosis of S. pneumoniae infections. The present invention can also be used as a method of detecting antibodies contained in samples from individuals infected by this bacterium using specific S. pneumoniae antigens.
Another application of anti-S. pneumoniae polypeptide antibodies of the invention is in the immunological screening of cDNA libraries constructed in expression vectors such as lgt11, lgt18–23, lZAP, and lORF8. Messenger libraries of this type, having coding sequences inserted in the correct reading frame and orientation, can produce fusion proteins. For instance, lgt11 will produce fusion proteins whose amino termini consist of β-galactosidase amino acid sequences and whose carboxy termini consist of a foreign polypeptide. Antigenic epitopes of a subject S. pneumoniae polypeptide can then be detected with antibodies, as, for example, reacting nitrocellulose filters lifted from infected plates with anti-S. pneumoniae polypeptide antibodies. Phage, scored by this assay, can then be isolated from the infected plate. Thus, the presence of S. pneumoniae gene homologs can be detected and cloned from other species, and alternate isoforms (including splicing variants) can be detected and cloned.
Kits Containing Nucleic Acids, Polypeptides or Antibodies of the Invention
The nucleic acid, polypeptides and antibodies of the invention can be combined with other reagents and articles to form kits. Kits for diagnostic purposes typically comprise the nucleic acid, polypeptides or antibodies in vials or other suitable vessels. Kits typically comprise other reagents for performing hybridization reactions, polymerase chain reactions (PCR), or for reconstitution of lyophilized components, such as aqueous media, salts, buffers, and the like. Kits may also comprise reagents for sample processing such as detergents, chaotropic salts and the like. Kits may also comprise immobilization means such as particles, supports, wells, dipsticks and the like. Kits may also comprise labeling means such as dyes, developing reagents, radioisotopes, fluorescent agents, luminescent or chemiluminescent agents, enzymes, intercalating agents and the like. With the nucleic acid and amino acid sequence information provided herein, individuals skilled in art can readily assemble kits to serve their particular purpose. Kits further can include instructions for use.
Bio Chips and Microarrays
The nucleic acid sequence of the present invention may be used to detect S. pneumoniae or other species of Streptococcus acid sequence using bio chip technology. Bio chips containing arrays of nucleic acid sequence can also be used to measure expression of genes of S. pneumoniae or other species of Streptococcus. For example, to diagnose a patient with a S. pneumoniae or other Streptococcus infection, a sample from a human or animal can be used as a probe on a bio chip containing an array of nucleic acid sequence from the present invention. In addition, a sample from a disease state can be compared to a sample from a non-disease state which would help identify a gene that is up-regulated or expressed in the disease state. This would provide valuable insight as to the mechanism by which the disease manifests. Changes in gene expression can also be used to identify critical pathways involved in drug transport or metabolism, and may enable the identification of novel targets involved in virulence or host cell interactions involved in maintenance of an infection. Procedures using such techniques have been described by Brown et al., 1995, Science 270: 467–470.
Bio chips can also be used to monitor the genetic changes of potential therapeutic compounds including, deletions, insertions or mismatches. Once the therapeutic is added to the patient, changes to the genetic sequence can be evaluated for its efficacy. In addition, the nucleic acid sequence of the present invention can be used to determine essential genes in cell cycling. As described in Iyer et al., 1999 (Science, 283:83–87) genes essential in the cell cycle can be identified using bio chips. Furthermore, the present invention provides nucleic acid sequence which can be used with bio chip technology to understand regulatory networks in bacteria, measure the response to environmental signals or drugs as in drug screening, and study virulence induction. (Mons et al., 1998, Nature Biotechnology, 16: 45–48. Patents teaching this technology include U.S. Pat. Nos. 5,445,934, 5,744,305, and 5800992.
Drug Screening Assays Using S. pneumoniae Polypeptides
By making available purified and recombinant S. pneumoniae polypeptides, the present invention provides assays which can be used to screen for drugs which are either agonists or antagonists of the normal cellular function, in this case, of the subject S. pneumoniae polypeptides, or of their role in intracellular signaling. Such inhibitors or potentiators may be useful as new therapeutic agents to combat S. pneumoniae infections in humans. A variety of assay formats will suffice and, in light of the present inventions, will be comprehended by the skilled artisan.
In many drug screening programs which test libraries of compounds and natural extracts, high throughput assays are desirable in order to maximize the number of compounds surveyed in a given period of time. Assays which are performed in cell-free systems, such as may be derived with purified or semi-purified proteins, are often preferred as “primary” screens in that they can be generated to permit rapid development and relatively easy detection of an alteration in a molecular target which is mediated by a test compound. Moreover, the effects of cellular toxicity and/or bioavailability of the test compound can be generally ignored in the in vitro system, the assay instead being focused primarily on the effect of the drug on the molecular target as may be manifest in an alteration of binding affinity with other proteins or change in enzymatic properties of the molecular target. Accordingly, in an exemplary screening assay of the present invention, the compound of interest is contacted with an isolated and purified S. pneumoniae polypeptide.
Screening assays can be constructed in vitro with a purified S. pneumoniae polypeptide or fragment thereof, such as an S. pneumoniae polypeptide having enzymatic activity, such that the activity of the polypeptide produces a detectable reaction product. The efficacy of the compound can be assessed by generating dose response curves from data obtained using various concentrations of the test compound. Moreover, a control assay can also be performed to provide a baseline for comparison. Suitable products include those with distinctive absorption, fluorescence, or chemi-luminescence properties, for example, because detection may be easily automated. A variety of synthetic or naturally occurring compounds can be tested in the assay to identify those which inhibit or potentiate the activity of the S. pneumoniae polypeptide. Some of these active compounds may directly, or with chemical alterations to promote membrane permeability or solubility, also inhibit or potentiate the same activity (e.g., enzymatic activity) in whole, live S. pneumoniae cells.
Overexpression Assays
Overexpression assays are based on the premise that overproduction of a protein would lead to a higher level of resistance to compounds that selectively interfere with the function of that protein. Overexpression assays may be used to identify compounds that interfere with the function of virtually any type of protein, including without limitation enzymes, receptors, DNA- or RNA-binding proteins, or any proteins that are directly or indirectly involved in regulating cell growth.
Typically, two bacterial strains are constructed. One contains a single copy of the gene of interest, and a second contains several copies of the same gene. Identification of useful inhibitory compounds of this type of assay is based on a comparison of the activity of a test compound in inhibiting growth and/or viability of the two strains. The method involves constructing a nucleic acid vector that directs high level expression of a particular target nucleic acid. The vectors are then transformed into host cells in single or multiple copies to produce strains that express low to moderate and high levels of protein encoding by the target sequence (strain A and B, respectively). Nucleic acid comprising sequences encoding the target gene can, of course, be directly integrated into the host cell.
Large numbers of compounds (or crude substances which may contain active compounds) are screened for their effect on the growth of the two strains. Agents which interfere with an unrelated target equally inhibit the growth of both strains. Agents which interfere with the function of the target at high concentration should inhibit the growth of both strains. It should be possible, however, to titrate out the inhibitory effect of the compound in the overexpressing strain. That is, if the compound is affecting the particular target that is being tested, it should be possible to inhibit the growth of strain A at a concentration of the compound that allows strain B to grow.
Alternatively, a bacterial strain is constructed that contains the gene of interest under the control of an inducible promoter. Identification of useful inhibitory agents using this type of assay is based on a comparison of the activity of a test compound in inhibiting growth and/or viability of this strain under both inducing and non-inducing conditions. The method involves constructing a nucleic acid vector that directs high-level expression of a particular target nucleic acid. The vector is then transformed into host cells that are grown under both non-inducing and inducing conditions (conditions A and B, respectively).
Large numbers of compounds (or crude substances which may contain active compounds) are screened for their effect on growth under these two conditions. Agents that interfere with the function of the target should inhibit growth under both conditions. It should be possible, however, to titrate out the inhibitory effect of the compound in the overexpressing strain. That is, if the compound is affecting the particular target that is being tested, it should be possible to inhibit growth under condition A at a concentration that allows the strain to grow under condition B.
Ligand-Binding Assays
Many of the targets according to the invention have functions that have not yet been identified. Ligand-binding assays are useful to identify inhibitor compounds that interfere with the function of a particular target, even when that function is unknown. These assays are designed to detect binding of test compounds to particular targets. The detection may involve direct measurement of binding. Alternatively, indirect indications of binding may involve stabilization of protein structure or disruption of a biological function. Non-limiting examples of useful ligand-binding assays are detailed below.
A useful method for the detection and isolation of binding proteins is the Biomolecular Interaction Assay (BIAcore) system developed by Pharmacia Biosensor and described in the manufacturer's protocol (LKB Pharmacia, Sweden). The BIAcore system uses an affinity purified anti-GST antibody to immobilize GST-fusion proteins onto a sensor chip. The sensor utilizes surface plasmon resonance which is an optical phenomenon that detects changes in refractive indices. In accordance with the practice of the invention, a protein of interest is coated onto a chip and test compounds are passed over the chip. Binding is detected by a change in the refractive index (surface plasmon resonance).
A different type of ligand-binding assay involves scintillation proximity assays (SPA, described in U.S. Pat. No. 4,568,649).
Another type of ligand binding assay, also undergoing development, is based on the fact that proteins containing mitochondrial targeting signals are imported into isolated mitochondria in vitro (Hurt et al., 1985, Embo J. 4:2061–2068; Eilers and Schatz, Nature, 1986, 322:228–231). In a mitochondrial import assay, expression vectors are constructed in which nucleic acids encoding particular target proteins are inserted downstream of sequences encoding mitochondrial import signals. The chimeric proteins are synthesized and tested for their ability to be imported into isolated mitochondria in the absence and presence of test compounds. A test compound that binds to the target protein should inhibit its uptake into isolated mitochondria in vitro.
Another ligand-binding assay is the yeast two-hybrid system (Fields and Song, 1989, Nature 340:245–246). The yeast two-hybrid system takes advantage of the properties of the GAL4 protein of the yeast Saccharomyces cerevisiae. The GAL4 protein is a transcriptional activator required for the expression of genes encoding enzymes of galactose utilization. This protein consists of two separable and functionally essential domains: an N-terminal domain which binds to specific DNA sequences (UASG); and a C-terminal domain containing acidic regions, which is necessary to activate transcription. The native GAL4 protein, containing both domains, is a potent activator of transcription when yeast are grown on galactose media. The N-terminal domain binds to DNA in a sequence-specific manner but is unable to activate transcription. The C-terminal domain contains the activating regions but cannot activate transcription because it fails to be localized to UASG. In the two-hybrid system, a system of two hybrid proteins containing parts of GAL4: (1) a GAL4 DNA-binding domain fused to a protein ‘X’ and (2) a GAL4 activation region fused to a protein ‘Y’. If X and Y can form a protein-protein complex and reconstitute proximity of the GAL4 domains, transcription of a gene regulated by UASG occurs. Creation of two hybrid proteins, each containing one of the interacting proteins X and Y, allows the activation region of UASG to be brought to its normal site of action.
The binding assay described in Fodor et al., 1991, Science 251:767–773, which involves testing the binding affinity of test compounds for a plurality of defined polymers synthesized on a solid substrate, may also be useful.
Compounds which bind to the polypeptides of the invention are potentially useful as antibacterial agents for use in therapeutic compositions.
Pharmaceutical formulations suitable for antibacterial therapy comprise the antibacterial agent in conjunction with one or more biologically acceptable carriers. Suitable biologically acceptable carriers include, but are not limited to, phosphate-buffered saline, saline, deionized water, or the like. Preferred biologically acceptable carriers are physiologically or pharmaceutically acceptable carriers.
The antibacterial compositions include an antibacterial effective amount of active agent. Antibacterial effective amounts are those quantities of the antibacterial agents of the present invention that afford prophylactic protection against bacterial infections or which result in amelioration or cure of an existing bacterial infection. This antibacterial effective amount will depend upon the agent, the location and nature of the infection, and the particular host. The amount can be determined by experimentation known in the art, such as by establishing a matrix of dosages and frequencies and comparing a group of experimental units or subjects to each point in the matrix.
The antibacterial active agents or compositions can be formed into dosage unit forms, such as for example, creams, ointments, lotions, powders, liquids, tablets, capsules, suppositories, sprays, aerosols or the like. If the antibacterial composition is formulated into a dosage unit form, the dosage unit form may contain an antibacterial effective amount of active agent. Alternatively, the dosage unit form may include less than such an amount if multiple dosage unit forms or multiple dosages are to be used to administer a total dosage of the active agent. Dosage unit forms can include, in addition, one or more excipient(s), diluent(s), disintegrant(s), lubricant(s), plasticizer(s), colorant(s), dosage vehicle(s), absorption enhancer(s), stabilizer(s), bactericide(s), or the like.
For general information concerning formulations, see, e.g., Gilman et al. (eds.), 1990, Goodman and Gilman's: The Pharmacological Basis of Therapeutics, 8th ed., Pergamon Press; and Remington's Pharmaceutical Sciences, 17th ed., 1990, Mack Publishing Co., Easton, Pa.; Avis et al. (eds.), 1993, Pharmaceutical Dosage Forms: Parenteral Medications, Dekker, New York; Lieberman et al (eds.), 1990, Pharmaceutical Dosage Forms: Disperse Systems, Dekker, New York.
The antibacterial agents and compositions of the present invention are useful for preventing or treating S. pneumoniae infections. Infection prevention methods incorporate a prophylactically effective amount of an antibacterial agent or composition. A prophylactically effective amount is an amount effective to prevent S. pneumoniae infection and will depend upon the specific bacterial strain, the agent, and the host. These amounts can be determined experimentally by methods known in the art and as described above.
S. pneumoniae infection treatment methods incorporate a therapeutically effective amount of an antibacterial agent or composition. A therapeutically effective amount is an amount sufficient to ameliorate or eliminate the infection. The prophylactically and/or therapeutically effective amounts can be administered in one administration or over repeated administrations. Therapeutic administration can be followed by prophylactic administration, once the initial bacterial infection has been resolved.
The antibacterial agents and compositions can be administered topically or systemically. Topical application is typically achieved by administration of creams, ointments, lotions, or sprays as described above. Systemic administration includes both oral and parental routes. Parental routes include, without limitation, subcutaneous, intramuscular, intraperitoneal, intravenous, transdermal, inhalation and intranasal administration.
Exemplification
I. Cloning and Sequencing of S. pneumoniae DNA
S. pneumoniae chromosomal DNA was isolated according to a basic DNA protocol outlined in Schleif R. F. and Wensink P. C., Practical Methods in Molecular Biology, p. 98, Springer-Verlag, NY, 1981, with minor modifications. Briefly, cells were pelleted, resuspended in TE (10 mM Tris, 1 mM EDTA, pH 7.6) and GES lysis buffer (5.1 M guanidium thiocyanate, 0.1 M EDTA, pH 8.0, 0.5% N-laurylsarcosine) was added. Suspension was chilled and ammonium acetate (NH4Ac) was added to final concentration of 2.0 M. DNA was extracted, first with chloroform, then with phenol-chloroform, and reextracted with chloroform. DNA was precipitated with isopropanol, washed twice with 70% EtOH, dried and resuspended in TE.
Following isolation whole genomic S. pneumoniae DNA was nebulized (Bodenteich et al., Automated DNA Sequencing and Analysis (J. C. Venter, ed.), Academic Press, 1994) to a median size of 2000 bp. After nebulization, the DNA was concentrated and separated on a standard 1% agarose gel. Several fractions, corresponding to approximate sizes 1000–1500 bp, 1500–2000 bp, 2000–2500 bp, 2500–3000 bp, were excised from the gel and purified by the GeneClean procedure (Bio101, Inc.).
The purified DNA fragments were then blunt-ended using T4 DNA polymerase. The healed DNA was then ligated to unique BstXI-linker adapters (5′ GTCTTCACCACGGGG (SEQ ID NO: 5323) and 5′ GTGGTGAAGAC (SEQ ID NO: 5324) in 100–1000 fold molar excess). These linkers are complimentary to the BstXI-cut pMPX vectors, while the overhang is not self-complimentary. Therefore, the linkers will not concatemerize nor will the cut-vector religate itself easily. The linker-adopted inserts were separated from the unincorporated linkers on a 1% agarose gel and purified using GeneClean. The linker-adopted inserts were then ligated to each of 20 pMPX vectors to construct a series of “shotgun” subclone libraries. Blunt ended vector was used for cloning into the PUC19 vector. The vectors contain an out-of-frame lacZ gene at the cloning site which becomes in-frame in the event that an adapter-dimer is cloned, allowing these to be avoided by their blue-color.
All subsequent steps were based either on the multiplex DNA sequencing protocols outlined in Church G. M. and Kieffer-Higgins S., Science 240:185–188, 1988 or by ABI377 automated DNA sequencing methods. Only major modifications to the protocols are highlighted. Briefly, each of the 20 vectors was then transformed into DH5a competent cells (Gibco/BRL, DH5a transformation protocol). The libraries were assessed by plating onto antibiotic plates containing ampicillin, methicillin and IPTG/Xgal. The plates were incubated overnight at 37° C. Successful transformants were then used for plating of clones and pooling into the multiplex pools. The clones were picked and pooled into 40 ml growth medium cultures. The cultures were grown overnight at 37° C. DNA was purified using the Qiagen Midi-prep kits and Tip-100 columns (Qiagen, Inc.). In this manner, 100 mg of DNA was obtained per pool.
These purified DNA samples were then sequenced either using the multiplex DNA sequencing based on chemical degradation methods (Church G. M. and Kieffer-Higgins S., Science 240:185–188, 1988) or by Sequithrem (Epicenter Technologies) dideoxy sequencing protocols or by ABI dye-terminator chemistry. For the multiplex portion the sequencing reactions were electrophoresed and transferred onto nylon membranes by direct transfer electrophoresis from 40 cm gels (Richterich P. and Church G. M., Methods in Enzymology 218:187–222, 1993). The DNA was covalently bound to the membranes by exposure to ultraviolet light, and hybridized with labeled oligonucleotides complimentary to tag sequences on the vectors (Church, supra). The membranes were washed to rinse off non-specifically bound probe, and exposed to X-ray film to visualize individual sequence ladders. After autoradiography, the hybridized probe was removed by incubation at 65° C., and the hybridization cycle repeated with another tag sequence until the membrane had been probed 41 times. Thus, each gel produced a large number of films, each containing new sequencing information. Whenever a new blot was processed, it was initially probed for an internal standard sequence added to each of the pools. Digital images of the films were generated using a laser-scanning densitometer (Molecular Dynamics, Sunnyvale, Calif.). The digitized images were processed on computer workstations (VaxStation 4000's) using the program REPLICATM (Church et al., Automated DNA Sequencing and Analysis (J. C. Venter, ed.), Academic Press, 1994). Image processing included lane straightening, contrast adjustment to smooth out intensity differences, and resolution enhancement by iterative gaussian deconvolution. The sequences were then converted to an SCF format so that processing and assembly could proceed on UNIX machines. The ABI dye terminator sequence reads were run on ABI377 machines and the data was directly transferred to UNIX machines following lane tracking of the gels. All multiplex and ABI reads were assembled using PHRAP (P. Green, Abstracts of DOE Human Genome Program Contractor-Grantee Workshop V, January 1996, p. 157) with default parameters and not using quality scores. The initial assembly was done at 7fold coverage and yielded 511 contigs. Short read length fragments of 200 bp or less found on the ends of contigs facing in the appropriate direction were used to extend off the end of the contigs. These reads were then resequenced with primers using ABI technology to give sequences with a read length of 500 or more bases. This allowed end extensions to be performed without ordering new primers. In addition, missing mates (sequences from clones that only gave one strand reads) were identified and sequenced with ABI technology to allow the identification of additional overlapping contigs.
End-sequencing of randomly picked genomic lambda was also performed. Sequencing on a both sides was done for all lambda sequences. The lambda library backbone helped to verify the integrity of the assembly and allowed closure of some of the physical gaps.
To identify S. pneumoniae polypeptides the complete genomic sequence of S. pneumoniae were analyzed essentially as follows: First, all possible stop-to-stop open reading frames (ORFs) greater than 180 nucleotides in all six reading frames were translated into amino acid sequences. Second, the identified ORFs were analyzed for homology to known (archeabacter, prokaryotic and eukaryotic) protein sequences. Third, the predicted coding regions of the sequences and start codons were evaluated with the programs GENEMARKTM (Borodovsky and McIninch, 1993, Comp. Chem. 17:123) and Glimmer (Fraser et al, Nature, 1997).
Identification Cloning and Expression of S. pneumoniae Nucleic Acids
Expression and purification of the S. pneumoniae polypeptides of the invention can be performed essentially as outlined below.
To facilitate the cloning, expression and purification of membrane and secreted proteins from S. pneumoniae, a gene expression system, such as the pET System (Novagen), for cloning and expression of recombinant proteins in E. coli, is selected. Also, a DNA sequence encoding a peptide tag, the His-Tag, is fused to the 3′ end of DNA sequences of interest in order to facilitate purification of the recombinant protein products. The 3′ end is selected for fusion in order to avoid alteration of any 5′ terminal signal sequence.
PCR Amplification and Cloning of Nucleic Acids Containing ORF's Encoding Enzymes
Nucleic acids chosen (for example, from the nucleic acids set forth in SEQ ID NO: 1–SEQ ID NO: 2661) for cloning from the 14453 strain of S. pneumoniae are prepared for amplification cloning by polymerase chain reaction (PCR). Synthetic oligonucleotide primers specific for the 5′ and 3′ ends of open reading frames (ORFs) are designed and purchased from GibcoBRL Life Technologies (Gaithersburg, Md., USA). All forward primers (specific for the 5′ end of the sequence) are designed to include an NcoI cloning site at the extreme 5′ terminus. These primers are designed to permit initiation of protein translation at a methionine residue followed by a valine residue and the coding sequence for the remainder of the native S. pneumoniae DNA sequence. All reverse primers (specific for the 3′ end of any S. pneumoniae ORF) include a EcoRI site at the extreme 5′ terminus to permit cloning of each S. pneumoniae sequence into the reading frame of the pET-28b. The pET-28b vector provides sequence encoding an additional 20 carboxy-terminal amino acids including six histidine residues (at the extreme C-terminus), which comprise the His-Tag.
Genomic DNA prepared from strain 14453 of S. pneumoniae is used as the source of template DNA for PCR amplification reactions (Current Protocols in Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994). To amplify a DNA sequence containing an S. pneumoniae ORF, genomic DNA (50 nanograms) is introduced into a reaction vial containing 2 mM MgCl2, 1 micromolar synthetic oligonucleotide primers (forward and reverse primers) complementary to and flanking a defined S. pneumoniae ORF, 0.2 mM of each deoxynucleotide triphosphate; dATP, dGTP, dCTP, dTTP and 2.5 units of heat stable DNA polymerase (Amplitaq, Roche Molecular Systems, Inc., Branchburg, N.J., USA) in a final volume of 100 microliters.
Upon completion of thermal cycling reactions, each sample of amplified DNA is washed and purified using the Qiaquick Spin PCR purification kit (Qiagen, Gaithersburg, Md., USA). All amplified DNA samples are subjected to digestion with the restriction endonucleases, e.g., NcoI and EcoRI (New England BioLabs, Beverly, Mass., USA)(Current Protocols in Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994). DNA samples are then subjected to electrophoresis on 1.0% NuSeive (FMC BioProducts, Rockland, Me. USA) agarose gels. DNA is visualized by exposure to ethidium bromide and long wave uv irradiation. DNA contained in slices isolated from the agarose gel is purified using the Bio 101 GeneClean Kit protocol (Bio 101 Vista, Calif., USA).
Cloning of S. pneumoniae Nucleic Acids into an Expression Vector
The pET-28b vector is prepared for cloning by digestion with endonucleases, e.g., NcoI and EcoRI (Current Protocols in Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994). The pET-28a vector, which encodes a His-Tag that can be fused to the 5′ end of an inserted gene, is prepared by digestion with appropriate restriction endonucleases.
Following digestion, DNA inserts are cloned (Current Protocols in Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994) into the previously digested pET-28b expression vector. Products of the ligation reaction are then used to transform the BL21 strain of E. coli (Current Protocols in Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994) as described below.
Transformation of Competent Bacteria with Recombinant Plasmids
Competent bacteria, E coli strain BL21 or E. coli strain BL21 (DE3), are transformed with recombinant pET expression plasmids carrying the cloned S. pneumoniae sequences according to standard methods (Current Protocols in Molecular, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994). Briefly, 1 microliter of ligation reaction is mixed with 50 microliters of electrocompetent cells and subjected to a high voltage pulse, after which, samples are incubated in 0.45 milliliters SOC medium (0.5% yeast extract, 2.0% tryptone, 10 mM NaCl, 2.5 mM KCl, 10 mM MgCl2, 10 mM MgSO4 and 20, mM glucose) at 37° C. with shaking for 1 hour. Samples are then spread on LB agar plates containing 25 microgram/ml kanamycin sulfate for growth overnight. Transformed colonies of BL21 are then picked and analyzed to evaluate cloned inserts as described below.
Identification of Recombinant Expression Vectors with S. pneumoniae Nucleic Acids
Individual BL21 clones transformed with recombinant pET-28b S. pneumoniae ORFs are analyzed by PCR amplification of the cloned inserts using the same forward and reverse primers, specific for each S. pneumoniae sequence, that were used in the original PCR amplification cloning reactions. Successful amplification verifies the integration of the S. pneumoniae sequences in the expression vector (Current Protocols in Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994).
Isolation and Preparation of Nucleic Acids From Transformants
Individual clones of recombinant pET-28b vectors carrying properly cloned S. pneumoniae ORFs are picked and incubated in 5 mls of LB broth plus 25 microgram/ml kanamycin sulfate overnight. The following day plasmid DNA is isolated and purified using the Qiagen plasmid purification protocol (Qiagen Inc., Chatsworth, Calif., USA).
Expression of Recombinant S. pneumoniae Sequences in E. coli 
The pET vector can be propagated in any E. coli K-12 strain e.g. HMS174, HB101, JM109, DH5, etc. for the purpose of cloning or plasmid preparation. Hosts for expression include E. coli strains containing a chromosomal copy of the gene for T7 RNA polymerase. These hosts are lysogens of bacteriophage DE3, a lambda derivative that carries the lacI gene, the lacUV5 promoter and the gene for T7 RNA polymerase. T7 RNA polymerase is induced by addition of isopropyl-B-D-thiogalactoside (IPTG), and the T7 RNA polymerase transcribes any target plasmid, such as pET-28b, carrying its gene of interest. Strains used include: BL21(DE3) (Studier, F. W., Rosenberg, A. H., Dunn, J. J., and Dubendorff, J. W. (1990) Meth. Enzymol. 185, 60–89).
To express recombinant S. pneumoniae sequences, 50 nanograms of plasmid DNA isolated as described above is used to transform competent BL21(DE3) bacteria as described above (provided by Novagen as part of the pET expression system kit). The lacZ gene (beta-galactosidase) is expressed in the pET-System as described for the S. pneumoniae recombinant constructions. Transformed cells are cultured in SOC medium for 1 hour, and the culture is then plated on LB plates containing 25 micrograms/ml kanamycin sulfate. The following day, bacterial colonies are pooled and grown in LB medium containing kanamycin sulfate (25 micrograms/ml) to an optical density at 600 nM of 0.5 to 1.0 O.D. units, at which point, 1 millimolar IPTG was added to the culture for 3 hours to induce gene expression of the S. pneumoniae recombinant DNA constructions.
After induction of gene expression with IPTG, bacteria are pelleted by centrifugation in a Sorvall RC-3B centrifuge at 3500×g for 15 minutes at 4° C. Pellets are resuspended in 50 milliliters of cold 10 mM Tris-HCl, pH 8.0, 0.1 M NaCl and 0.1 mM EDTA (STE buffer). Cells are then centrifuged at 2000×g for 20 min at 4° C. Wet pellets are weighed and frozen at −80° C. until ready for protein purification.
A variety of methodologies known in the art can be utilized to purify the isolated proteins. (Current Protocols in Protein Science, John Wiley and Sons, Inc., J. E. Coligan et al., eds., 1995). For example, the frozen cells may be thawed, resupended in buffer and ruptured by several passages through a small volume microfluidizer (Model M-110S, Microfluidics International Corporation, Newton, Mass.). The resultant homogenate may be centrifuged to yield a clear supernatant (crude extract) and following filtration the crude extract may be fractionated over columns. Fractions may be monitored by absorbance at OD280 nm. and peak fractions may analyzed by SDS-PAGE
The concentrations of purified protein preparations may be quantified spectrophotometrically using absorbance coefficients calculated from amino acid content (Perkins, S. J. 1986 Eur. J. Biochem. 157, 169–180). Protein concentrations are also measured by the method of Bradford, M. M. (1976) Anal. Biochem. 72, 248–254, and Lowry, O. H., Rosebrough, N., Farr, A. L. & Randall, R. J. (1951) J. Biol. Chem. 193, pages 265–275, using bovine serum albumin as a standard.
SDS-polyacrylamide gels of various concentrations may be purchased from BioRad (Hercules, Calif., USA), and stained with Coomassie blue. Molecular weight markers may include rabbit skeletal muscle myosin (200 kDa), E. coli (-galactosidase (116 kDa), rabbit muscle phosphorylase B (97.4 kDa), bovine serum albumin (66.2 kDa), ovalbumin (45 kDa), bovine carbonic anhydrase (31 kDa), soybean trypsin inhibitor (21.5 kDa), egg white lysozyme (14.4 kDa) and bovine aprotinin (6.5 kDa).
Equivalents
While this invention has been particularly shown and described with references to preferred embodiments thereof, it will be understood by those skilled in the art that various changes in form and details may be made therein without departing from the scope of the invention encompassed by the appended claims.

















ORF NAME
NT ID
AA ID
AA LN
NT LN
SCORE
P-VALUE
DESCRIPTION























SPX0001
1
2662
111
333
552
2.20E−74
[GI:2804700]
87


ORF NAME
NT ID
AA ID
AA LN
NT LN
SCORE
P-VALUE
DESCRIPTION


SPX0001
1
2662
111
333
552
2.20E-74
[GI:2804700]
87









[LN:AF030361]









[AC:AF030361]









[PN:transposase]









[OR:Streptococcus pneumoniae]


SPX0002
2
2663
173
519
885
3.60E-120
[GI:663278]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX0003
3
2664
109
327
281
1.40E-34
[GI:2804700]
87









[LN:AF030361]









[AC:AF030361]









[PN:transposase]









[OR:Streptococcus pneumoniae]


SPX0004
4
2665
190
570
948
7.40E-131
[GI:663279]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX0005
5
2666
122
366


NO-HIT
6


SPX0006
6
2667
401
1203
815
7.40E-125
[LN:RS1_LEULA]
116









[AC:P50889:P71450]









[GN:RPS1]









[OR:Leuconostoc lactis]









[DE:40S RIBOSOMAL PROTEIN S1]









[SP:P50889:P71450]


SPX0007
7
2668
79
237
89
2.90E-05
[LN:E64801]
77









[AC:E64801]









[PN:hypothetical protein b0663]









[OR:Escherichia coli]


SPX0008
8
2669
77
231


NO-HIT
6


SPX0009
9
2670
215
645
832
6.30E-114
[LN:PCP_STRPY]
149









[AC:Q01328]









[GN:PCP]









[OR:Streptococcus pyogenes]









[EC:3.4.19.3]









[DE:PEPTIDASE) (PYROGLUTAMYL-PEPTIDASE I) (PGP-I) (PYRASE)]









[SP:Q01328]


SPX0010
10
2671
308
924
234
3.90E-61
[LN:A81402]
119









[AC:A81402]









[PN:probable integral membrane protein Cj0553 [imported]]









[GN:Cj0553]









[OR:Campylobacter jejuni]


SPX0011
11
2672
237
711
208
1.30E-37
[GI:6002226]
128









[LN:SC51A]









[AC:AL121596]









[PN:possible integral membrane protein]









[GN:SCF51A.18c]









[OR:Streptomyces coelicolor A3(2)]


SPX0012
12
2673
235
705
213
1.30E-53
[GI:2804687]
114









[LN:AF030359]









[AC:AF030359]









[PN:oligopeptide binding protein]









[GN:aliA]









[OR:Streptococcus pneumoniae]


SPX0013
13
2674
341
1023
1359
9.60E-184
[GI:6979306]
190









[LN:AF164204]









[AC:AF164204]









[PN:branched-chain amino acid aminotransferase]









[GN:bcaT]









[FN:catalyzes the first reaction in the catabolism]









[OR:Lactococcus lactis subsp. cremoris]


SPX0014
14
2675
824
2472
4143
0
[GI:6851038]
105









[LN:SPPARCETP]









[AC:Z67739]









[PN:DNA topoisomerase IV]









[GN:parC]









[OR:Streptococcus pneumoniae]


SPX0015
15
2676
648
1944
3318
0
[GI:6851037]
105









[LN:SPPARCETP]









[AC:Z67739]









[PN:DNA topoisomerase IV]









[GN:parE]









[OR:Streptococcus pneumoniae]


SPX0016
16
2677
214
642
1073
2.50E-150
[LN:YPAE_STRPN]
127









[AC:Q54916]









[OR:Streptococcus pneumoniae]









[DE:HYPOTHETICAL 23.0 KD PROTEIN IN PARE 5′REGION (ORF2)]









[SP:Q54916]


SPX0017
17
2678
410
1230
1044
8.20E-270
[GI:2804700]
87









[LN:AF030361]









[AC:AF030361]









[PN:transposase]









[OR:Streptococcus pneumoniae]


SPX0018
18
2679
278
834
591
9.50E-139
[LN:A33595]
107









[AC:A33595:A30868]









[PN:probable transposase]









[CL:transposase IS3]









[OR:Streptococcus agalactiae]


SPX0019
19
2680
191
573
422
2.30E-53
[LN:B30868]
81









[AC:B30868]









[PN:hypothetical protein 1]









[OR:Streptococcus agalactiae]


SPX0020
20
2681
34
102
124
5.30E-12
[LN:B30868]
81









[AC:B30868]









[PN:hypothetical protein 1]









[OR:Streptococcus agalactiae]


SPX0021
21
2682
319
957
1002
3.80E-138
[LN:F70009]
141









[AC:F70009]









[PN:conserved hypothetical protein yufQ]









[GN:yufQ]









[CL:probable ribose ABC transporter rbsC-2]









[OR:Bacillus subtilis]


SPX0022
22
2683
362
1086
385
3.70E-85
[LN:E70009]
97









[AC:E70009]









[PN:conserved hypothetical protein yufP]









[GN:yufP]









[OR:Bacillus subtilis]


SPX0023
23
2684
512
1536
1623
2.30E-217
[LN:D70009]
174









[AC:D70009]









[PN:probable ABC transporter yufO]









[GN:yufO]









[CL:Bacillus subtilis probable ABC transporter yufO:ATP-binding cassette homology]









[OR:Bacillus subtilis]


SPX0024
24
2685
140
420
83
1.80E-06
[LN:G72493]
92









[AC:G72493]









[PN:hypothetical protein APE2590]









[GN:APE2590]









[OR:Aeropyrum pernix]


SPX0025
25
2686
364
1092
354
8.80E-82
[LN:YUFN_BACSU]
117









[AC:O05252]









[GN:YUFN]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL LIPOPROTEIN YUFN PRECURSOR]









[SP:O05252]


SPX0026
26
2687
130
390
324
5.40E-40
[GI:6478520]
100









[LN:AF187304]









[AC:AF187304]









[PN:cytidine deaminase]









[GN:cdd]









[OR:Bacillus caldolyticus]


SPX0027
27
2688
100
300
276
2.40E-33
[LN:D75424]
136









[AC:D75424]









[PN:deoxyribose-phosphate aldolase]









[GN:DR1205]









[CL:deoxyribose-phosphate aldolase]









[OR:Deinococcus radiodurans]


SPX0028
28
2689
61
183


NO-HIT
6


SPX0029
29
2690
119
357
344
3.30E-42
[LN:DEOC_BACSU]
109









[AC:P39121]









[GN:DRA]









[OR:Bacillus subtilis]









[EC:4.1.2.4]









[DE:(DEOXYRIBOALDOLASE)]









[SP:P39121]


SPX0030
30
2691
426
1278
921
9.70E-147
“[LN:PDP_BACST]
144









[AC:P77836]









[GN:PYN]









[OR:Bacillus stearothermophilus]









[EC:2.4.2.2]









[DE:PYRIMIDINE-NUCLEOSIDE PHOSPHORYLASE, (PYNP)]









[SP:P77836]”


SPX0031
31
2692
197
591
250
2.00E-56
[LN:S59955]
113









[AC:S59955]









[PN:hypothetical protein 202]









[CL:hypothetical protein MJ0882]









[OR:Staphylococcus aureus]


SPX0032
32
2693
73
219


NO-HIT
6


SPX0033
33
2694
100
300


NO-HIT
6


SPX0034
34
2695
317
951
345
3.80E-79
[GI:6960352]
134









[LN:STYSTMF1]









[AC:AF170176]









[PN:96% identity over 316 amino acids with E. coli]









[GN:coaA]









[OR:Salmonella typhimurium LT2]


SPX0035
35
2696
79
237
98
8.40E-17
[LN:R3EC20]
214









[AC:A30425:A02748:S40547:G64722:S07374]









[PN:ribosomal protein S20/L26 [validated]









:ribosomal protein L26:ribosomal protein S20]









[GN:rpsT]









[CL:Escherichia coli ribosomal protein S20]









[OR:Escherichia coli]


SPX0036
36
2697
175
525
270
6.30E-50
[GI:6434823]
86









[LN:SPU78969]









[AC:U78969]









[PN:FlaR]









[GN:flaR]









[OR:Streptococcus pyogenes]


SPX0037
37
2698
237
711
1042
4.10E-140
[LN:DEOD_STRTR]
116









[AC:Q56037]









[GN:DEOD]









[OR:Streptococcus thermophilus]









[EC:2.4.2.1]









[DE:(PNP) (FRAGMENT)]









[SP:Q56037]


SPX0038
38
2699
171
513
271
1.10E-30
[GI:6729344]
150









[LN:AB029317]









[AC:AB029317]









[PN:intermedilysin]









[GN:ily]









[OR:Streptococcus intermedius]









[SR:Streptococcus intermedius (strain:UNS46) DNA]


SPX0039
39
2700
192
576
117
2.80E-07
“[LN:PXN1_XENLA]
137









[AC:P49263]









[GN:PXN1]









[OR:Xenopus laevis]









[SR:,African clawed frog]









[DE:PENTRAXIN FUSION PROTEIN PRECURSOR]









[SP:P49263]”


SPX0040
40
2701
136
408
92
0.00026
“[LN:CP23_CHICK]
135









[AC:P23614]









[OR:Gallus gallus]









[SR:,Chicken]









[DE:23 KD CORTICAL CYTOSKELETON-ASSOCIATED PROTEIN (CAP-23)]









[SP:P23614]”


SPX0041
41
2702
270
810
395
1.40E-105
[LN:DEOD_BACSU]
100









[AC:P46354]









[GN:DEOD:PNP]









[OR:Bacillus subtilis]









[EC:2.4.2.1]









[DE:(PNP)]









[SP:P46354]


SPX0042
42
2703
181
543


NO-HIT
6


SPX0043
43
2704
404
1212
736
2.30E-199
“[LN:DEOB_LACLC]
181









[AC:O32808]









[GN:DEOB]









[OR:Lactococcus lactis]









[SR:,subspcremoris:Streptococcus cremoris]









[EC:5.4.2.7]









[DE:PHOSPHOPENTOMUTASE, (PHOSPHODEOXYRIBOMUTASE)]









[SP:O32808]”


SPX0044
44
2705
247
741
206
1.40E-52
[LN:G69180]
168









[AC:G69180]









[PN:ribose 5-phosphate isomerase]









[GN:MTH608]









[CL:Haemophilus influenzae ribose-5-phosphate isomerase]









[OR:Methanobacterium thermoautotrophicum]


SPX0045
45
2706
62
186


NO-HIT
6


SPX0046
46
2707
291
873
386
5.80E-99
[LN:YFOL_STRTR]
86









[AC:P96051]









[OR:Streptococcus thermophilus]









[DE:(ORF1091)]









[SP:P96051]


SPX0047
47
2708
307
921
1049
3.00E-140
[LN:FOLD_STRTR]
121









[AC:P96050]









[GN:FOLD]









[OR:Streptococcus thermophilus]









[EC:1.5.1.5:3.5.4.9]









[DE:(EC 3.5.4.9)]]










[SP:P96050]


SPX0048
48
2709
72
216
99
5.40E-08
[LN:G72510]
92









[AC:G72510]









[PN:hypothetical protein APE2061]









[GN:APE2061]









[OR:Aeropyrum pernix]


SPX0049
49
2710
245
735
796
7.00E-105
[LN:H69334]
162









[AC:H69334]









[PN:glutamine transport protein glnQ]









[GN:glnQ]









[CL:inner membrane protein malK:ATP-binding cassette homology]









[OR:Archaeoglobus fulgidus]


SPX0050
50
2711
128
384
88
5.60E-05
[LN:D72757]
92









[AC:D72757]









[PN:hypothetical protein APE0049]









[GN:APE0049]









[OR:Aeropyrum pernix]


SPX0051
51
2712
228
684
314
1.10E-52
“[LN:H69278]
151









[AC:H69278]









[PN:glutamine ABC transporter, permease protein (glnP) homolog]









[CL:histidine permease protein M]









[OR:Archaeoglobus fulgidus]”


SPX0052
52
2713
77
231
89
8.60E-09
[LN:G69865]
87









[AC:G69865]









[PN:hypothetical protein ykuJ]









[GN:ykuJ]









[OR:Bacillus subtilis]


SPX0053
53
2714
753
2259
2641
0
[GI:4103470]
84









[LN:AF023421]









[AC:AF023421]









[PN:ClpE]









[GN:clpE]









[OR:Lactococcus lactis]


SPX0054
54
2715
83
249
116
9.50E-10
[GI:4098132]
83









[LN:MBU73653]









[AC:U73653]









[PN:63 kDa protein]









[OR:Mycobacterium bovis]


SPX0055
55
2716
61
183


NO-HIT
6


SPX0056
56
2717
70
210


NO-HIT
6


SPX0057
57
2718
114
342
477
2.00E-73
[GI:5019553]
97









[LN:SPN239004]









[AC:AJ239004]









[PN:putative transposase]









[OR:Streptococcus pneumoniae]


SPX0058
58
2719
116
348
569
6.90E-75
[GI:4200438]
96









[LN:AF026471]









[AC:AF026471]









[PN:putative transposase]









[OR:Streptococcus pneumoniae]


SPX0059
59
2720
141
423
101
5.60E-07
[LN:A70315]
147









[AC:A70315]









[PN:AP4A hydrolase]









[GN:apfA]









[CL:Methanococcus jannaschii mutator protein mutT:mutT domain homology]









[OR:Aquifex aeolicus]


SPX0060
60
2721
100
300


NO-HIT
6


SPX0061
61
2722
198
594
597
3.80E-95
[LN:A33595]
107









[AC:A33595:A30868]









[PN:probable transposase]









[CL:transposase IS3]









[OR:Streptococcus agalactiae]


SPX0062
62
2723
88
264
308
1.70E-38
[LN:A33595]
107









[AC:A33595:A30868]









[PN:probable transposase]









[CL:transposase IS3]









[OR:Streptococcus agalactiae]


SPX0063
63
2724
34
102
126
2.60E-12
[LN:B30868]
81









[AC:B30868]









[PN:hypothetical protein 1]









[OR:Streptococcus agalactiae]


SPX0064
64
2725
117
351
210
5.10E-24
“[LN:JC1151]
89









[AC:JC1151]









[PN:hypothetical protein, 20.3K]









[OR:Agrobacterium tumefaciens]”


SPX0065
65
2726
102
306
154
5.60E-19
[GI:722339]
100









[LN:AXU22323]









[AC:U22323]









[PN:unknown]









[OR:Acetobacter xylinus]









[SR:Acetobacter xylinum]


SPX0066
66
2727
89
267


NO-HIT
6


SPX0067
67
2728
576
1728
285
5.20E-53
[LN:G70002]
87









[AC:G70002]









[PN:hypothetical protein ytwP]









[GN:ytwP]









[OR:Bacillus subtilis]


SPX0068
68
2729
649
1947
3322
0
[GI:1490397]
95









[LN:SPGYRBORF]









[AC:Z67740]









[PN:DNA gyrase]









[GN:gyrB]









[OR:Streptococcus pneumoniae]


SPX0069
69
2730
191
573
709
2.40E-93
[GI:1052803]
81









[LN:SPGYRBG]









[AC:X83917]









[GN:orflgyrb]









[OR:Streptococcus pneumoniae]


SPX0070
70
2731
185
555
118
9.00E-28
“[LN:D70177]
211









[AC:D70177]









[PN:4-methyl-5(b-hydroxyethyl)-thiazole monophosphate biosynthesis protein (thiJ) homolog]









[CL:signal transduction protein DJ-1]









[OR:Borrelia burgdorferi]









[SR:, Lyme disease spirochete]”


SPX0071
71
2732
417
1251
398
1.00E-50
[LN:S22738]
86









[AC:S22738:S22728]









[PN:hypothetical protein]









[OR:Streptococcus salivarius]


SPX0072
72
2733
817
2451
203
3.80E-66
[LN:DING_BACSU]
122









[AC:P54394]









[GN:DING]









[OR:Bacillus subtilis]









[DE:PROBABLE ATP-DEPENDENT HELICASE DING HOMOLOG]









[SP:P54394]


SPX0073
73
2734
310
930
189
6.20E-42
[LN:G69979]
85









[AC:G69979]









[PN:proteinase homolog yrrN]









[GN:yrrN]









[OR:Bacillus subtilis]


SPX0074
74
2735
96
288


NO-HIT
6


SPX0075
75
2736
445
1335
2202
4.50E-301
“[LN:CIAH_STRPN]
120









[AC:Q54955]









[GN:CIAH]









[OR:Streptococcus pneumoniae]









[EC:2.7.3.-]









[DE:SENSOR PROTEIN CIAH,]









[SP:Q54955]”


SPX0076
76
2737
225
675
1130
1.70E-152
[LN:CIAR_STRPN]
124









[AC:Q54954]









[GN:CIAR]









[OR:Streptococcus pneumoniae]









[DE:TRANSCRIPTIONAL REGULATORY PROTEIN CIAR]









[SP:Q54954]


SPX0077
77
2738
849
2547
1653
0
[GI:5524752]
105









[LN:STH007700]









[AC:AJ007700]









[PN:aminopeptidase N]









[GN:pepN]









[OR:Streptococcus thermophilus]


SPX0078
78
2739
147
441
176
1.80E-20
[LN:T35570]
113









[AC:T35570]









[PN:hypothetical protein SC6G4.19c SC6G4.19c]









[GN:SC6G4.19c]









[OR:Streptomyces coelicolor]


SPX0079
79
2740
292
876
80
8.00E-10
[LN:PPSA_PYRFU]
131









[AC:P42850:Q59672]









[GN:PPSA]









[OR:Pyrococcus furiosus]









[EC:2.7.9.2]









[DE:DIKINASE) (PEP SYNTHASE)]









[SP:P42850:Q59672]


SPX0080
80
2741
243
729


NO-HIT
6


SPX0081
81
2742
160
480
113
1.60E-07
[LN:C72513]
92









[AC:C72513]









[PN:hypothetical protein APE2080]









[GN:APE2080]









[OR:Aeropyrum pernix]


SPX0082
82
2743
76
228


NO-HIT
6


SPX0083
83
2744
233
699
231
3.20E-28
[LN:GNO_GLUOX]
104









[AC:P50199]









[GN:GNO]









[OR:Gluconobacter oxydans]









[EC:1.1.1.69]









[DE:REDUCTASE)]









[SP:P50199]


SPX0084
84
2745
89
267


NO-HIT
6


SPX0085
85
2746
309
927
210
2.40E-41
[LN:YDHF_ECOLI]
135









[AC:P76187]









[GN:YDHF]









[OR:Escherichia coli]









[DE:HYPOTHETICAL OXIDOREDUCTASE IN SODC-NEMA INTERGENIC REGION]









[SP:P76187]


SPX0086
86
2747
272
816
114
3.70E-09
[GI:3043880]
94









[LN:LLU95841]









[AC:U95841]









[PN:transmembrane protein Tmp6]









[OR:Lactococcus lactis]


SPX0087
87
2748
72
216
146
1.50E-15
[GI:3582220]
114









[LN:AE001272]









[AC:AE001272]









[PN:conserved hypothetical protein]









[GN:ORF00047]









[OR:Lactococcus lactis]


SPX0088
88
2749
79
237


NO-HIT
6


SPX0089
89
2750
82
246
269
2.80E-32
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX0090
90
2751
680
2040
734
6.10E-239
[LN:SYM_BACST]
108









[AC:P23920]









[GN:METS]









[OR:Bacillus stearothermophilus]









[EC:6.1.1.10]









[DE:(METRS)]









[SP:P23920]


SPX0091
91
2752
420
1260
287
2.30E-62
[LN:E69858]
97









[AC:E69858]









[PN:conserved hypothetical protein yknZ]









[GN:yknZ]









[OR:Bacillus subtilis]


SPX0092
92
2753
234
702
663
9.00E-86
[GI:2822199]
120









[LN:SCU96166]









[AC:U96166:AF227987]









[PN:ATP-binding cassette protein]









[GN:tptC]









[OR:Streptococcus cristatus]


SPX0093
93
2754
400
1200
144
5.60E-36
[LN:C69858]
97









[AC:C69858]









[PN:conserved hypothetical protein yknX]









[GN:yknX]









[OR:Bacillus subtilis]


SPX0094
94
2755
449
1347
730
1.70E-192
“[LN:S41386]
182









[AC:S41386]









[PN:glutathione reductase (NADPH),]









[CL:dihydrolipoamide dehydrogenase:dihydrolipoamide dehydrogenase homology]









[OR:Streptococcus thermophilus]









[EC:1.6.4.2]”


SPX0095
95
2756
179
537
218
6.90E-30
[LN:H72334]
78









[AC:H72334]









[PN:bioY protein]









[GN:TM0799]









[OR:Thermotoga maritima]


SPX0096
96
2757
112
336


NO-HIT
6


SPX0097
97
2758
80
240
171
1.50E-18
[LN:Y352_TREPA]
108









[AC:O83371]









[GN:TP0352]









[OR:Treponema pallidum]









[DE:HYPOTHETICAL PROTEIN TP0352]









[SP:O83371]


SPX0098
98
2759
107
321


NO-HIT
6


SPX0099
99
2760
113
339
109
1.40E-12
[GI:4098081]
128









[LN:LLU73336]









[AC:U73336]









[PN:anaerobic ribonucleotide reductase]









[GN:nrdD]









[OR:Lactococcus lactis subsp. cremoris]


SPX0100
100
2761
240
720
372
1.30E-85
[LN:TRMD_BACSU]
142









[AC:O31741]









[GN:TRMD]









[OR:Bacillus subtilis]









[EC:2.1.1.31]









[DE:METHYLTRANSFERASE) (TRNA [GM37]









METHYLTRANSFERASE)]









[SP:O31741]


SPX0101
101
2762
173
519
292
5.20E-61
[LN:RIMM_BACSU]
119









[AC:O31740]









[GN:RIMM]









[OR:Bacillus subtilis]









[DE:PROBABLE 16S RRNA PROCESSING PROTEIN RIMM]









[SP:O31740]


SPX0102
102
2763
267
801


NO-HIT
6


SPX0103
103
2764
80
240
141
9.70E-15
[LN:C69880]
147









[AC:C69880]









[PN:conserved hypothetical protein ylqC]









[GN:ylqC]









[CL:Bacillus conserved hypothetical protein ylqC]









[OR:Bacillus subtilis]


SPX0104
104
2765
91
273
315
5.10E-39
[LN:C47154]
176









[AC:C47154:S11366:G69700]









[PN:ribosomal protein S16 (BS17) rpsP:ribosomal protein BS17]









[GN:rpsP]









[CL:Escherichia coli ribosomal protein S16]









[OR:Bacillus subtilis]


SPX0105
105
2766
70
210


NO-HIT
6


SPX0106
106
2767
135
405


NO-HIT
6


SPX0107
107
2768
71
213


NO-HIT
6


SPX0108
108
2769
268
804
243
3.60E-38
[LN:T41399]
140









[AC:T41399]









[PN:probable cyclophilin-related peptidyl prolyl cis-trans isomerase]









[GN:SPCC553.04]









[OR:Schizosaccharomyces pombe]


SPX0109
109
2770
120
360
83
5.110E-05
[GI:1773206]
60









[LN:ECU82664]









[AC:U82664]









[OR:Escherichia coli]


SPX0110
110
2771
514
1542
1502
3.70E-258
[LN:D69813]
188









[AC:D69813]









[PN:ABC transporter (ATP-binding protein) homolog yfmM]









[GN:yfmM]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Bacillus subtilis]


SPX0111
111
2772
161
483
88
2.20E-11
[GI:7110140]
100









[LN:AF155139]









[AC:AF155139:AF019976]









[PN:VanZF]









[GN:vanZF]









[OR:Paenibacillus popilliae]


SPX0112
112
2773
362
1086
452
1.30E-135
[LN:YLON_BACSU]
137









[AC:O34617]









[GN:YLON]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 41.6 KD PROTEIN IN FMT-SPOVM INTERGENIC REGION]









[SP:O34617]


SPX0113
113
2774
177
531
152
3.20E-25
[LN:F70023]
136









[AC:F70023]









[PN:hypothetical protein yutD]









[GN:yutD]









[CL:Bacillus subtilis hypothetical protein yutD]









[OR:Bacillus subtilis]


SPX0114
114
2775
202
606
1034
4.90E-138
[GI:5758312]
152









[LN:AF162664]









[AC:AF162664]









[PN:manganese co-factored superoxide dismutase]









[GN:sodA]









[FN:removes superoxide]









[OR:Streptococcus pneumoniae]


SPX0115
115
2776
346
1038
952
2.60E-127
[GI:2765186]
92









[LN:SASODA]









[AC:Y12224]









[PN:hypothetical protein]









[OR:Streptococcus agalactiae]


SPX0116
116
2777
312
936
1616
3.20E-220
[GI:5578893]
116









[LN:SPN131985]









[AC:AJ131985]









[PN:dihydroorotate dehydrogenase]









[GN:pyrDA]









[OR:Streptococcus pneumoniae]


SPX0117
117
2778
397
1191
1399
3.90E-187
[LN:METK_STAAU]
135









[AC:P50307]









[GN:METK]









[OR:Staphylococcus aureus]









[EC:2.5.1.6]









[DE:ADENOSYLTRANSFERASE) (ADOMET SYNTHETASE)]









[SP:P50307]


SPX0118
118
2779
448
1344
972
1.00E-140
[LN:YQFR_BACSU]
130









[AC:P54475]









[GN:YQFR]









[OR:Bacillus subtilis]









[DE:PROBABLE RNA HELICASE IN CCCA-SODA INTERGENIC REGION]









[SP:P54475]


SPX0119
119
2780
272
816


NO-HIT
6


SPX0120
120
2781
88
264


NO-HIT
6


SPX0121
121
2782
727
2181
735
4.60E-182
[GI:4098489]
91









[LN:SMU78600]









[AC:U78600]









[PN:putative ptsG protein]









[OR:Streptococcus mutans]


SPX0122
122
2783
312
936
330
2.80E-63
[LN:G69627]
88









[AC:G69627]









[PN:cell-division protein ftsX]









[GN:ftsX]









[OR:Bacillus subtilis]


SPX0123
123
2784
69
207


NO-HIT
6


SPX0124
124
2785
231
693
798
9.90E-106
[LN:D69627]
176









[AC:D69627]









[PN:cell-division ATP-binding protein ftsE]









[GN:ftsE]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Bacillus subtilis]


SPX0125
125
2786
75
225
94
1.10E-07
[LN:A71007]
95









[AC:A71007]









[PN:hypothetical protein PH1351]









[GN:PH1351]









[OR:Pyrococcus horikoshii]


SPX0126
126
2787
307
921
936
6.80E-124
[LN:RF2_BACSU]
128









[AC:P28367:O34444]









[GN:PRFB]









[OR:Bacillus subtilis]









[DE:PEPTIDE CHAIN RELEASE FACTOR 2 (RF-2)]









[SP:P28367:O34444]


SPX0127
127
2788
219
657
279
3.40E-41
[LN:H72290]
96









[AC:H72290]









[PN:conserved hypothetical protein]









[GN:TM1140]









[OR:Thermotoga maritima]


SPX0128
128
2789
237
711
711
7.60E-93
[LN:T35757]
212









[AC:T35757]









[PN:probable branched chain amino acid transport ATP-binding protein]









[GN:SC7H2.26]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Streptomyces coelicolor]


SPX0129
129
2790
67
201
109
6.60E-10
[LN:G72485]
92









[AC:G72485]









[PN:hypothetical protein APE2527]









[GN:APE2527]









[OR:Aeropyrum pernix]


SPX0130
130
2791
255
765
387
4.20E-90
“[LN:F72290]
206









[AC:F72290]









[PN:branched chain amino acid ABC transporter, ATP-binding protein]









[GN:TM1138]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Thermotoga maritima]”


SPX0131
131
2792
319
957
334
1.10E-63
[LN:E81303]
164









[AC:E81303]









[PN:probable branched-chain amino-acid ABC transport system permease protein Cj1016c [imported]]









[GN:livM:Cj1016c]









[OR:Campylobacter jejuni]


SPX0132
132
2793
293
879
325
1.30E-90
“[LN:D72290]
163









[AC:D72290]









[PN:branched chain amino acid ABC transporter, permease protein]









[GN:TM1136]









[CL:leucine transport protein livH]









[OR:Thermotoga maritima]”


SPX0133
133
2794
387
1161
193
5.70E-39
[LN:H81303]
166









[AC:H81303]









[PN:branched-chain amino-acid ABC transport system periplasmic binding protein Cj1019c [imported]]









[GN:livJ:Cj1019c]









[OR:Campylobacter jejuni]


SPX0134
134
2795
150
450


NO-HIT
6


SPX0135
135
2796
83
249
116
2.40E-11
[LN:D69874]
97









[AC:D69874]









[PN:conserved hypothetical protein ylbG]









[GN:ylbG]









[OR:Bacillus subtilis]


SPX0136
136
2797
197
591
933
8.10E-124
[LN:CLPP_STRSL]
119









[AC:P36398]









[GN:CLPP]









[OR:Streptococcus salivarius]









[EC:3.4.21.92]









[DE:(ENDOPEPTIDASE CLP)]









[SP:P36398]


SPX0137
137
2798
217
651
961
5.20E-129
[LN:UPP_STRSL]
124









[AC:P36399]









[GN:UPP]









[OR:Streptococcus salivarius]









[EC:2.4.2.9]









[DE:PYROPHOSPHORYLASE) (UPRTASE)]









[SP:P36399]


SPX0138
138
2799
54
162


O-HIT
6


SPX0139
139
2800
156
468
265
4.40E-49
[LN:CME2_BACSU]
106









[AC:P32393]









[GN:COMEB:COME2]









[OR:Bacillus subtilis]









[DE:COME OPERON PROTEIN 2]









[SP:P32393]


SPX0140
140
2801
186
558
114
1.10E-07
[LN:G70325]
102









[AC:G70325]









[PN:transcription regulator TetR/AcrR family]









[GN:acrR3]









[OR:Aquifex aeolicus]


SPX0141
141
2802
282
846
813
2.60E-107
[GI:4580621]
77









[LN:AF118389]









[AC:AF118389]









[PN:unknown]









[OR:Streptococcus suis]


SPX0142
142
2803
392
1176
330
1.60E-83
[GI:2293312]
83









[LN:AF008220]









[AC:AF008220]









[PN:YtfP]









[GN:ytfP]









[OR:Bacillus subtilis]


SPX0143
143
2804
152
456
106
6.50E-12
[LN:G70031]
121









[AC:G70031]









[PN:mutator MutT protein homolog yvcI]









[GN:yvcI]









[CL:mutT domain homology]









[OR:Bacillus subtilis]


SPX0144
144
2805
173
519
876
2.10E-115
[GI:6179679]
137









[LN:SPN239034]









[AC:AJ239034]









[PN:regulator of pmrA]









[GN:mta]









[FN:regulator of pmrA expression]









[OR:Streptococcus pneumoniae]


SPX0145
145
2806
490
1470
805
5.40E-151
[LN:F69825]
144









[AC:F69825]









[PN:sodium-dependent transporter homolog yhdH]









[GN:yhdH]









[CL:gamma-aminobutyric acid transporter]









[OR:Bacillus subtilis]


SPX0146
146
2807
315
945
1165
3.00E-155
[LN:MANA_STRMU]
118









[AC:Q59935]









[GN:PMI]









[OR:Streptococcus mutans]









[EC:5.3.1.8]









[DE:(PMI) (PHOSPHOHEXOMUTASE)]









[SP:Q59935]


SPX0147
147
2808
134
402


NO-HIT
6


SPX0148
148
2809
110
330
270
1.80E-43
[LN:JE0396]
121









[AC:JE0396]









[PN:phospho-beta-galactosidase II]









[CL:Agrobacterium beta-glucosidase]









[OR:Lactobacillus gasseri]


SPX0149
149
2810
89
267


NO-HIT
6


SPX0150
150
2811
218
654
154
1.00E-20
[GI:722339]
100









[LN:AXU22323]









[AC:U22323]









[PN:unknown]









[OR:Acetobacter xylinus]









[SR:Acetobacter xylinum]


SPX0151
151
2812
116
348


NO-HIT
6


SPX0152
152
2813
592
1776
3033
0
“[LN:POXB_STRPN]
141









[AC:Q54970]









[GN:SPXB]









[OR:Streptococcus pneumoniae]









[EC:1.2.3.3]









[DE:PYRUVATE OXIDASE, (PYRUVIC OXIDASE) (POX)]









[SP:Q54970]”


SPX0153
153
2814
67
201
149
2.30E-14
[GI:1513069]
147









[LN:LMU15554]









[AC:U15554]









[PN:P-type adenosine triphosphatase]









[GN:ctpA]









[FN:involved in cation transport]









[OR:Listeria monocytogenes]


SPX0154
154
2815
733
2199
648
8.80E-202
[GI:1513069]
147









[LN:LMU15554]









[AC:U15554]









[PN:P-type adenosine triphosphatase]









[GN:ctpA]









[FN:involved in cation transport]









[OR:Listeria monocytogenes]


SPX0155
155
2816
85
255
107
2.40E-09
[LN:H72624]
92









[AC:H72624]









[PN:hypothetical protein APE1456]









[GN:APE1456]









[OR:Aeropyrum pernix]


SPX0156
156
2817
61
183


NO-HIT
6


SPX0157
157
2818
124
372
70
6.10E-06
“[LN:H69267]
183









[AC:H69267]









[PN:cytochrome-c oxidase, chain II AF0144]









[CL:cytochrome-c oxidase chain II:cytochrome-c oxidase chain II homology]









[OR:Archaeoglobus fulgidus]









[EC:1.9.3.1]”


SPX0158
158
2819
142
426
240
1.00E-28
[LN:COPY_ENTHR]
118









[AC:Q47839]









[GN:COPY]









[OR:Enterococcus hirae]









[DE:COPAB ATPASES METAL-FIST TYPE REPRESSOR]









[SP:Q47839]


SPX0159
159
2820
269
807
308
4.00E-99
[GI:6707002]
96









[LN:AF109218]









[AC:AF109218:U96108]









[PN:ThiD]









[GN:thiD]









[OR:Staphylococcus carnosus]


SPX0160
160
2821
211
633
245
8.10E-55
[LN:D75087]
210









[AC:D75087]









[PN:thiamin phosphate pyrophosphorylase (thie) PAB1645]









[GN:PAB1645]









[CL:probable thiamin-phosphate pyrophosphorylase:thiamin-phosphate pyrophosphorylase homology]









[OR:Pyrococcus abyssi]


SPX0161
161
2822
269
807
228
2.70E-27
[LN:THIM_ECOLI]
144









[AC:P76423]









[GN:THIM]









[OR:Escherichia coli]









[EC:2.7.1.50]









[DE:HYDROXYETHYLTHIAZOLE KINASE) (THZ KINASE) (TH KINASE)]









[SP:P76423]


SPX0162
162
2823
175
525


NO-HIT
6


SPX0163
163
2824
231
693
384
2.00E-48
[LN:TENA_BACSU]
108









[AC:P25052]









[GN:TENA]









[OR:Bacillus subtilis]









[DE:TRANSCRIPTIONAL ACTIVATOR TENA]









[SP:P25052]


SPX0164
164
2825
217
651
112
1.10E-13
[GI:1296823]
78









[LN:LHPEPIGN]









[AC:Z56283]









[GN:orf2]









[OR:Lactobacillus helveticus]


SPX0165
165
2826
462
1386
279
4.50E-59
[GI:1296822]
78









[LN:LHPEPIGN]









[AC:Z56283]









[GN:orf1]









[OR:Lactobacillus helveticus]


SPX0166
166
2827
187
561
203
2.20E-27
[LN:A69859]
87









[AC:A69859]









[PN:hypothetical protein ykoE]









[GN:ykoE]









[OR:Bacillus subtilis]


SPX0167
167
2828
75
225


NO-HIT
6


SPX0168
168
2829
69
207


NO-HIT
6


SPX0169
169
2830
210
630
520
4.10E-72
[GI:6707004]
96









[LN:AF109218]









[AC:AF109218:U96108]









[PN:ThiE]









[GN:thiE]









[OR:Staphylococcus carnosus]


SPX0170
170
2831
268
804
523
4.60E-67
[GI:6707003]
96









[LN:AF109218]









[AC:AF109218:U96108]









[PN:ThiM]









[GN:thiM]









[OR:Staphylococcus carnosus]


SPX0171
171
2832
137
411
114
2.00E-08
[LN:H71057]
95









[AC:H71057]









[PN:hypothetical protein PH1158]









[GN:PH1158]









[OR:Pyrococcus horikoshii]


SPX0172
172
2833
82
246


NO-HIT
6


SPX0173
173
2834
75
225
203
1.90E-23
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX0174
174
2835
223
669
127
6.60E-15
“[LN:PT18_YEAST]
141









[AC:P25362]









[GN:PET18:HIT2:YCR020C:YCR20C]









[OR:Saccharomyces cerevisiae]









[SR:,Baker′s yeast]









[DE:PET18 PROTEIN]









[SP:P25362]”


SPX0175
175
2836
379
1137
1379
5.20E-216
[GI:2239174]
116









[LN:SILCT]









[AC:Y07622]









[PN:lactate oxidase]









[GN:lctO]









[FN:lactate utilisation]









[OR:Streptococcus iniae]


SPX0176
176
2837
497
1491
1157
1.60E-228
“[LN:SYK_BACSU]
144









[AC:P37477]









[GN:LYSS]









[OR:Bacillus subtilis]









[EC:6.1.1.6]









[DE:LYSYL-TRNA SYNTHETASE, (LYSINE--TRNA LIGASE) (LYSRS)]









[SP:P37477]”


SPX0177
177
2838
227
681
351
2.10E-70
“[LN:D71849]
195









[AC:D71849]









[PN:amino acid ABC transporter, permease protein]









[GN:jhp1096]









[CL:histidine permease protein M]









[OR:Helicobacter pylori]









[SR:strain J99, , strain J99]









[SR:strain J99, ]”


SPX0178
178
2839
127
381
279
2.10E-35
“[LN:B64666]
133









[AC:B64666]









[PN:glutamine ABC transporter, permease protein]









[CL:histidine permease protein M]









[OR:Helicobacter pylori]”


SPX0179
179
2840
96
288
249
4.10E-30
“[LN:B64666]
133









[AC:B64666]









[PN:glutamine ABC transporter, permease protein]









[CL:histidine permease protein M]









[OR:Helicobacter pylori]”


SPX0180
180
2841
71
213
92
5.90E-05
[GI:4163988]
114









[LN:AF082511]









[AC:AF082511]









[PN:putative ATP-binding protein MglA]









[GN:mglA]









[OR:Treponema denticola]


SPX0181
181
2842
169
507
531
5.00E-70
[LN:H81391]
131









[AC:H81391]









[PN:amino-acid ABC transporter ATP-binding protein Cj0469 [imported]]









[GN:Cj0469]









[OR:Campylobacter jejuni]


SPX0182
182
2843
67
201
72
3.30E-07
[LN:G72510]
92









[AC:G72510]









[PN:hypothetical protein APE2061]









[GN:APE2061]









[OR:Aeropyrum pernix]


SPX0183
183
2844
81
243
132
5.50E-12
[GI:4204972]
111









[LN:LLU60994]









[AC:U60994]









[FN:transport systems for basic amino acids and]









[OR:Leuconostoc lactis]


SPX0184
184
2845
185
555
531
1.40E-67
[LN:C81373]
153









[AC:C81373]









[PN:probable amino-acid transporter periplasmic solute-binding protein Cj0982c [imported]]









[GN:Cj0982c]









[OR:Campylobacter jejuni]


SPX0185
185
2846
216
648
353
6.60E-51
[LN:YYBJ_BACSU]
95









[AC:P37494]









[GN:YYBJ]









[OR:Bacillus subtilis]









[DE:INTERGENIC REGION]









[SP:P37494]


SPX0186
186
2847
235
705


NO-HIT
6


SPX0187
187
2848
68
204


NO-HIT
6


SPX0188
188
2849
269
807


NO-HIT
6


SPX0189
189
2850
255
765


NO-HIT
6


SPX0190
190
2851
117
351


NO-HIT
6


SPX0191
191
2852
211
633
1057
1.30E-140
[GI:4009484]
124









[LN:AF068902]









[AC:AF068902]









[PN:orotate phosphoribosyltransferase PyrE]









[GN:pyrE]









[OR:Streptococcus pneumoniae]


SPX0192
192
2853
234
702
1173
1.80E-157
[GI:4009483]
117









[LN:AF068902]









[AC:AF068902]









[PN:orotidine-5′-decarboxylase PyrF]









[GN:pyrF]









[OR:Streptococcus pneumoniae]


SPX0193
193
2854
67
201


NO-HIT
6


SPX0194
194
2855
400
1200
1946
3.00E-251
[GI:4009482]
114









[LN:AF068902]









[AC:AF068902]









[PN:cell division protein DivIB]









[GN:divIB]









[OR:Streptococcus pneumoniae]


SPX0195
195
2856
148
444
110
2.20E-07
“[GI:6473880]
180









[LN:AB027890]









[AC:AB027890]









[PN:Hypothetical protein]









[GN:SPBC3D5.14C]









[OR:Schizosaccharomyces pombe]









[SR:Schizosaccharomyces pombe (strain:968 h90) DNA, clone:TA46]]


SPX0196
196
2857
353
1059
1780
1.40E-242
[GI:4009481]
131









[LN:AF068902]









[AC:AF068902]









[PN:undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc]









[GN:murG]









[OR:Streptococcus pneumoniae]


SPX0197
197
2858
451
1353
2206
1.20E-297
[GI:4009480]
120









[LN:AF068902]









[AC:AF068902]









[PN:D-glutamic acid adding enzyme MurD]









[GN:murD]









[OR:Streptococcus pneumoniae]


SPX0198
198
2859
214
642
1062
1.20E-142
[GI:4009479]
83









[LN:AF068902]









[AC:AF068902]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX0199
199
2860
674
2022
2263
0
[GI:4009478]
83









[LN:AF068902]









[AC:AF068902]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX0200
200
2861
135
405
86
1.80E-05
[GI:7576923]
109









[LN:AF242367]









[AC:AF242367]









[PN:lactococcin 972]









[GN:lclA]









[OR:Lactococcus lactis subsp. lactis]


SPX0201
201
2862
73
219


NO-HIT
6


SPX0202
202
2863
85
255
89
2.50E-05
[LN:T20916]
98









[AC:T20916]









[PN:hypothetical protein F14F8.3]









[GN:F14F8.3]









[OR:Caenorhabditis elegans]


SPX0203
203
2864
621
1863
1706
0
[LN:TYPA_BACSU]
115









[AC:O07631]









[GN:TYPA]









[OR:Bacillus subtilis]









[DE:GTP-BINDING PROTEIN TYPA/BIPA HOMOLOG]









[SP:O07631]


SPX0204
204
2865
242
726
154
3.00E-34
[GI:7328274]
103









[LN:SAY14816]









[AC:Y14816]









[PN:hypothetical protein]









[GN:ORF231]









[OR:Staphylococcus aureus]


SPX0205
205
2866
66
198


NO-HIT
6


SPX0206
206
2867
127
381
174
3.80E-28
[LN:YQHL_BACSU]
141









[AC:P54510]









[GN:YQHL]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 14.6 KD PROTEIN IN GCVT-SPOIIIAA INTERGENIC REGION]









[SP:P54510]


SPX0207
207
2868
74
222
158
1.80E-17
[LN:T44786]
87









[AC:T44786]









[PN:hypothetical protein 1 [imported]]









[OR:Bacillus megaterium]


SPX0208
208
2869
303
909
1241
5.30E-168
[LN:T44638]
172









[AC:T44638]









[PN:capsular polysaccharide biosynthesis protein cpsY [imported]]









[GN:cpsY]









[CL:probable transcription regulator lsyR]









[OR:Streptococcus agalactiae]


SPX0209
209
2870
252
756
476
5.30E-66
[LN:YQJQ_BACSU]
103









[AC:P54554]









[GN:YQJQ]









[OR:Bacillus subtilis]









[EC:1.-.-.-]









[DE:(EC 1.-.-.-)]









[SP:P54554]


SPX0210
210
2871
310
930
368
9.50E-98
[LN:YQJK_BACSU]
137









[AC:P54548]









[GN:YQJK]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 34.0 KD PROTEIN IN GLNQ-ANSR INTERGENIC REGION]









[SP:P54548]


SPX0211
211
2872
208
624


NO-HIT
6


SPX0212
212
2873
413
1239
792
1.40E-103
[LN:B69888]
187









[AC:B69888]









[PN:GTP-binding protein proteinase modulator homolog ynbA]









[GN:ynbA]









[CL:GTP-binding protein hflX:translation elongation factor Tu homology]









[OR:Bacillus subtilis]


SPX0213
213
2874
312
936
317
7.10E-70
[LN:G69657]
159









[AC:G69657]









[PN:tRNA isopentenylpyrophosphate transferase miaA]









[GN:miaA]









[CL:delta(2)-isopentenylpyrophosphate transferase]









[OR:Bacillus subtilis]


SPX0214
214
2875
63
189


NO-HIT
6


SPX0215
215
2876
66
198
129
6.10E-12
“[LN:TYSY_LACLA]
160









[AC:P19368]









[GN:THYA]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:2.1.1.45]









[DE:THYMIDYLATE SYNTHASE, (TS)]









[SP:P19368]]


SPX0216
216
2877
221
663
318
1.20E-39
[GI:7328278]
103









[LN:SAY14816]









[AC:Y14816]









[PN:hypothetical protein]









[GN:ORF242]









[OR:Staphylococcus aureus]


SPX0217
217
2878
212
636
691
4.80E-91
[LN:B69997]
130









[AC:B69997]









[PN:conserved hypothetical protein ytmQ]









[GN:ytmQ]









[CL:hypothetical protein HI0340]









[OR:Bacillus subtilis]


SPX0218
218
2879
89
267


NO-HIT
6


SPX0219
219
2880
103
309
215
6.90E-25
[LN:YLXS_BACSU]
137









[AC:P32726]









[GN:YLXS]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 17.6 KD PROTEIN IN NUSA 5′REGION (P15A) (ORF1)]









[SP:P32726]


SPX0220
220
2881
379
1137
715
6.00E-122
[GI:2634032]
111









[LN:BSUB0009]









[AC:Z99112:AL009126]









[GN:nusA]









[FN:transcription termination]









[OR:Bacillus subtilis]


SPX0221
221
2882
98
294
220
1.70E-25
[LN:YLXR_BACSU]
144









[AC:P32728]









[GN:YLXR]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 10.4 KD PROTEIN IN NUSA-INFB INTERGENIC REGION (ORF3)]









[SP:P32728]


SPX0222
222
2883
100
300
259
3.80E-31
“[LN:YLXQ_ENTFC]
144









[AC:P55768]









[OR:Enterococcus faecium]









[SR:,Streptococcus faecium]









[DE:PROBABLE RIBOSOMAL PROTEIN IN INFB 5′REGION]









[SP:P55768]]


SPX0223
223
2884
165
495


NO-HIT
6


SPX0224
224
2885
931
2793
2768
0
[GI:3947714]
142









[LN:SAAJ3164]









[AC:AJ003164]









[PN:initiation factor IF2]









[GN:infB]









[FN:translation initiation factor]









[OR:Streptococcus agalactiae]


SPX0225
225
2886
82
246


NO-HIT
6


SPX0226
226
2887
117
351
478
2.00E-61
[GI:3947715]
136









[LN:SAAJ3164]









[AC:AJ003164]









[PN:ribosome binding factor A]









[GN:rbfA]









[FN:ribosome maturation]









[OR:Streptococcus agalactiae]


SPX0227
227
2888
260
780
217
3.30E-40
[LN:T35040]
110









[AC:T35040]









[PN:hypothetical protein SC4G2.05 SC4G2.05]









[GN:SC4G2.05]









[OR:Streptomyces coelicolor]


SPX0228
228
2889
84
252


NO-HIT
6


SPX0229
229
2890
74
222


NO-HIT
6


SPX0230
230
2891
65
195
202
2.70E-24
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX0231
231
2892
78
234
102
4.60E-08
[LN:A69271]
140









[AC:A69271]









[PN:hypothetical protein AF0169]









[CL:Archaeoglobus fulgidus hypothetical protein AF0169]









[OR:Archaeoglobus fulgidus]


SPX0232
232
2893
445
1335
123
1.30E-41
[LN:B69271]
84









[AC:B69271]









[PN:hypothetical protein AF0170]









[OR:Archaeoglobus fulgidus]


SPX0233
233
2894
85
255


NO-HIT
6


SPX0234
234
2895
132
396


NO-HIT
6


SPX0235
235
2896
69
207


NO-HIT
6


SPX0236
236
2897
150
450


NO-HIT
6


SPX0237
237
2898
186
558
148
2.10E-18
[LN:YP20_BACLI]
106









[AC:P05332]









[GN:P20]









[OR:Bacillus licheniformis]









[DE:HYPOTHETICAL P20 PROTEIN]









[SP:P05332]


SPX0238
238
2899
321
963


NO-HIT
6


SPX0239
239
2900
884
2652
1594
0
“[LN:SYV_BACSU]
144









[AC:Q05873]









[GN:VALS]









[OR:Bacillus subtilis]









[EC:6.1.1.9]









[DE:VALYL-TRNA SYNTHETASE, (VALINE--TRNA LIGASE) (VALRS)]









[SP:Q05873]]


SPX0240
240
2901
252
756
642
7.80E-85
“[LN:B71947]
145









[AC:B71947]









[PN:hypothetical protein jhp0330]









[GN:jhp0330]









[OR:Helicobacter pylori]









[SR:strain J99, , strain J99]









[SR:strain J99, ]]


SPX0241
241
2902
268
804
91
1.80E-05
“[LN:Y4LH_RHISN]
128









[AC:P55548]









[GN:Y4LH]









[OR:Rhizobium sp]









[SR:,strain NGR234]









[DE:HYPOTHETICAL 22.4 KD PROTEIN Y4LH]









[SP:P55548]]


SPX0242
242
2903
95
285
387
3.10E-49
[GI:1490399]
90









[LN:SPPARCETP]









[AC:Z67739]









[PN:DNA transposase]









[OR:Streptococcus pneumoniae]


SPX0243
243
2904
102
306
323
2.70E-40
[GI:1490399]
90









[LN:SPPARCETP]









[AC:Z67739]









[PN:DNA transposase]









[OR:Streptococcus pneumoniae]


SPX0244
244
2905
91
273
315
2.50E-39
[LN:A33595]
107









[AC:A33595:A30868]









[PN:probable transposase]









[CL:transposase IS3]









[OR:Streptococcus agalactiae]


SPX0245
245
2906
92
276
135
3.80E-13
[LN:B30868]
81









[AC:B30868]









[PN:hypothetical protein 1]









[OR:Streptococcus agalactiae]


SPX0246
246
2907
422
1266


NO-HIT
6


SPX0247
247
2908
399
1197
109
9.90E-10
[GI:6689196]
109









[LN:SCE20]









[AC:AL136058]









[PN:putative helicase]









[GN:SCE20.37]









[OR:Streptomyces coelicolor A3(2)]


SPX0248
248
2909
98
294


NO-HIT
6


SPX0249
249
2910
280
840
489
2.30E-81
[LN:LICT_BACSU]
116









[AC:P39805]









[GN:LICT:N15A]









[OR:Bacillus subtilis]









[DE:TRANSCRIPTION ANTITERMINATOR LICT]









[SP:P39805]


SPX0250
250
2911
613
1839
534
8.10E-147
“[LN:PTBA_BACSU]
149









[AC:P40739:Q45661]









[GN:BGLP:N17C]









[OR:Bacillus subtilis]









[EC:2.7.1.69]









[DE:ENZYME II, ABC COMPONENT), (EII-BGL)]









[SP:P40739:Q45661]]


SPX0251
251
2912
472
1416
1046
3.70E-228
“[LN:ABGA_CLOLO]
127









[AC:Q46130]









[GN:ABGA]









[OR:Clostridium longisporum]









[EC:3.2.1.86]









[DE:6-PHOSPHO-BETA-GLUCOSIDASE,]









[SP:Q46130]]


SPX0252
252
2913
349
1047
656
3.10E-156
[LN:SYFA_BACSU]
139









[AC:P17921:P94539]









[GN:PHES]









[OR:Bacillus subtilis]









[EC:6.1.1.20]









[DE:-TRNA LIGASE ALPHA CHAIN) (PHERS)]









[SP:P17921:P94539]


SPX0253
253
2914
331
993


NO-HIT
6


SPX0254
254
2915
170
510
333
1.80E-41
“[LN:YPIP_LACDL]
141









[AC:P46543]









[OR:Lactobacillus delbrueckii]









[SR:,subsplactis]









[DE:HYPOTHETICAL 19.8 KD PROTEIN IN PEPI 3′REGION]









[SP:P46543]]


SPX0255
255
2916
801
2403
312
2.20E-132
“[LN:SYFB_SYNY3]
154









[AC:P74296]









[GN:PHET:SLL1553]









[OR:Synechocystis sp]









[SR:,strain PCC 6803]









[EC:6.1.1.20]









[DE:TRNA LIGASE BETA CHAIN) (PHERS)]









[SP:P74296]]


SPX0256
256
2917
296
888


NO-HIT
6


SPX0257
257
2918
149
447
437
4.90E-55
[GI:517210]
65









[LN:SPU11799]









[AC:U11799]









[OR:Streptococcus pyogenes]


SPX0258
258
2919
89
267
245
2.00E-28
[LN:Y659_HAEIN]
112









[AC:P44030]









[GN:HI0659]









[OR:Haemophilus influenzae]









[DE:HYPOTHETICAL PROTEIN HI0659]









[SP:P44030]


SPX0259
259
2920
99
297


NO-HIT
6


SPX0260
260
2921
750
2250
1309
6.60E-297
“[LN:C81326]
175









[AC:C81326]









[PN:5-methyltetrahydropteroyltriglutamate-- homocystei methyltransferase, Cj1201 [imported]]









[GN:metE:Cj1201]









[OR:Campylobacter jejuni]









[EC:2.1.1.14]]


SPX0261
261
2922
289
867
261
3.90E-77
“[LN:D81326]
147









[AC:D81326]









[PN:5,10-methylenetetrahydrofolate reductase, Cj1202 [imported]]









[GN:metF:Cj1202]









[OR:Campylobacter jejuni]









[EC:1.7.99.5]]


SPX0262
262
2923
90
270


NO-HIT
6


SPX0263
263
2924
738
2214
1323
3.80E-298
[LN:PNPA_BACSU]
151









[AC:P50849]









[GN:PNPA:COMR]









[OR:Bacillus subtilis]









[EC:2.7.7.8]









[DE:PHOSPHORYLASE) (PNPASE) (VEGETATIVE PROTEIN 15) (VEG15)]









[SP:P50849]


SPX0264
264
2925
206
618
493
1.20E-63
[GI:6899995]
110









[LN:CST130879]









[AC:AJ130879]









[PN:serine acetyltransferase]









[GN:cysE]









[OR:Clostridium sticklandii]


SPX0265
265
2926
295
885
113
3.80E-07
[LN:E69786]
190









[AC:E69786]









[PN:ribosomal-protein-alanine N-acetyltransfer homolog ydiD]









[GN:ydiD]









[CL:Escherichia coli ribosomal-protein-alanine N-acetyltransferase rimI]









[OR:Bacillus subtilis]


SPX0266
266
2927
152
456


NO-HIT
6


SPX0267
267
2928
448
1344
570
9.00E-167
[GI:6899996]
112









[LN:CST130879]









[AC:AJ130879]









[PN:cysteinyl tRNA synthetase]









[GN:cysRS]









[OR:Clostridium sticklandii]


SPX0268
268
2929
129
387
316
6.30E-39
[LN:C69742]
97









[AC:C69742]









[PN:conserved hypothetical protein yazC]









[GN:yazC]









[OR:Bacillus subtilis]


SPX0269
269
2930
295
885
224
3.10E-30
[LN:LRPR_STREQ]
105









[AC:Q54087]









[GN:LRP]









[OR:Streptococcus equisimilis]









[DE:LEUCINE RICH PROTEIN]









[SP:Q54087]


SPX0270
270
2931
88
264


NO-HIT
6


SPX0271
271
2932
200
600


NO-HIT
6


SPX0272
272
2933
52
156
87
3.30E-06
[LN:D75542]
90









[AC:D75542]









[PN:hypothetical protein]









[GN:DR0254]









[OR:Deinococcus radiodurans]


SPX0273
273
2934
82
246
247
1.10E-29
[LN:F81737]
131









[AC:F81737]









[PN:hypothetical protein TC0129 [imported]]









[GN:TC0129]









[OR:Chlamydia muridarum:Chlamydia trachomatis MoPn]


SPX0274
274
2935
78
234
143
4.90E-15
[LN:F71245]
95









[AC:F71245]









[PN:hypothetical protein PHS004]









[GN:PHS004]









[OR:Pyrococcus horikoshii]


SPX0275
275
2936
72
216


NO-HIT
6


SPX0276
276
2937
63
189
68
2.40E-07
[LN:C64571]
134









[AC:C64571]









[PN:hypothetical protein HP0411]









[CL:Helicobacter pylori hypothetical protein HP0411]









[OR:Helicobacter pylori]


SPX0277
277
2938
312
936
194
2.60E-36
“[GI:773349]
142









[LN:BSU20445]









[AC:U20445]









[PN:BirA protein]









[GN:birA]









[FN:biotin protein ligase, biotin operon repressor]









[OR:Bacillus subtilis]]


SPX0278
278
2939
287
861
255
1.70E-56
[LN:MSMR_STRMU]
110









[AC:Q00753]









[GN:MSMR]









[OR:Streptococcus mutans]









[DE:MSM OPERON REGULATORY PROTEIN]









[SP:Q00753]


SPX0279
279
2940
721
2163
2528
0
“[LN:AGAL_STRMU]
128









[AC:P27756]









[GN:AGA]









[OR:Streptococcus mutans]









[EC:3.2.1.22]









[DE:ALPHA-GALACTOSIDASE, (MELIBIASE)]









[SP:P27756]]


SPX0280
280
2941
420
1260
1106
2.40E-180
[LN:MSME_STRMU]
121









[AC:Q00749]









[GN:MSME]









[OR:Streptococcus mutans]









[DE:MULTIPLE SUGAR-BINDING PROTEIN PRECURSOR]









[SP:Q00749]


SPX0281
281
2942
82
246


NO-HIT
6


SPX0282
282
2943
289
867
1188
1.40E-166
[LN:MSMF_STRMU]
142









[AC:Q00750]









[GN:MSMF]









[OR:Streptococcus mutans]









[DE:MULTIPLE SUGAR-BINDING TRANSPORT SYSTEM PERMEASE PROTEIN MSMF]









[SP:Q00750]


SPX0283
283
2944
278
834
1174
3.40E-164
[LN:MSMG_STRMU]
142









[AC:Q00751]









[GN:MSMG]









[OR:Streptococcus mutans]









[DE:MULTIPLE SUGAR-BINDING TRANSPORT SYSTEM PERMEASE PROTEIN MSMG]









[SP:Q00751]


SPX0284
284
2945
482
1446
2154
6.70E-294
“[LN:A27626]
110









[AC:A27626]









[PN:sucrose phosphorylase,]









[CL:gtfA protein]









[OR:Streptococcus mutans]









[EC:2.4.1.7]]


SPX0285
285
2946
398
1194


NO-HIT
6


SPX0286
286
2947
134
402


NO-HIT
6


SPX0287
287
2948
662
1986
3341
0
[LN:AMIA_STRPN]
142









[AC:P18791:P18792]









[GN:AMIA]









[OR:Streptococcus pneumoniae]









[DE:OLIGOPEPTIDE-BINDING PROTEIN AMIA PRECURSOR]









[SP:P18791:P18792]


SPX0288
288
2949
499
1497
2538
0
[LN:AMIC_STRPN]
129









[AC:P18793]









[GN:AMIC]









[OR:Streptococcus pneumoniae]









[DE:OLIGOPEPTIDE TRANSPORT PERMEASE PROTEIN AMIC]









[SP:P18793]


SPX0289
289
2950
309
927
1564
1.10E-217
[LN:AMID_STRPN]
129









[AC:P18794]









[GN:AMID]









[OR:Streptococcus pneumoniae]









[DE:OLIGOPEPTIDE TRANSPORT PERMEASE PROTEIN AMID]









[SP:P18794]


SPX0290
290
2951
356
1068
1806
2.10E-245
[LN:AMIE_STRPN]
132









[AC:P18765]









[GN:AMIE]









[OR:Streptococcus pneumoniae]









[DE:OLIGOPEPTIDE TRANSPORT ATP-BINDING PROTEIN AMIE]









[SP:P18765]


SPX0291
291
2952
113
339


NO-HIT
6


SPX0292
292
2953
309
927
1534
5.40E-208
[LN:AMIF_STRPN]
132









[AC:P18766]









[GN:AMIF]









[OR:Streptococcus pneumoniae]









[DE:OLIGOPEPTIDE TRANSPORT ATP-BINDING PROTEIN AMIF]









[SP:P18766]


SPX0293
293
2954
419
1257
2039
1.30E-284
[GI:2804700]
87









[LN:AF030361]









[AC:AF030361]









[PN:transposase]









[OR:Streptococcus pneumoniae]


SPX0294
294
2955
96
288
274
1.10E-34
[GI:663279]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX0295
295
2956
173
519
840
6.50E-114
[GI:663278]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX0296
296
2957
237
711
471
2.40E-60
[LN:TRER_BACSU]
120









[AC:P39796]









[GN:TRER]









[OR:Bacillus subtilis]









[DE:TREHALOSE OPERON TRANSCRIPTIONAL REPRESSOR]









[SP:P39796]


SPX0297
297
2958
656
1968
383
7.20E-135
[LN:PTTB_ECOLI]
114









[AC:P36672]









[GN:TREB]









[OR:Escherichia coli]









[EC:2.7.1.69]









[DE:(EC 2.7.1.69) (EII-TRE)]









[SP:P36672]


SPX0298
298
2959
542
1626
1617
2.00E-272
[GI:2208998]
102









[LN:SSU35633]









[AC:U35633]









[PN:dextran glucosidase DexS]









[GN:dexS]









[OR:Streptococcus suis]


SPX0299
299
2960
60
180
125
2.30E-12
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX0300
300
2961
84
252
104
4.40E-09
[GI:6899236]
116









[LN:AE002123]









[AC:AE002123:AF222894]









[PN:conserved hypothetical]









[GN:UU265]









[OR:Ureaplasma urealyticum]


SPX0301
301
2962
265
795
476
2.60E-84
[GI:2462097]
95









[LN:BCBCTLGLR]









[AC:Y10927]









[PN:glutamate racemase]









[GN:bcglr]









[OR:Bacillus cereus]


SPX0302
302
2963
297
891
273
9.10E-35
[LN:C69986]
165









[AC:C69986]









[PN:conserved hypothetical protein ysnA]









[GN:ysnA]









[CL:Methanococcus jannaschii conserved hypothetical protein MJ0226]









[OR:Bacillus subtilis]


SPX0303
303
2964
74
222
158
1.60E-15
[LN:YGGV_ECOLI]
143









[AC:P52061]









[GN:YGGV]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 21.0 KD PROTEIN IN GSHB-ANSB INTERGENIC REGION (O197)]









[SP:P52061]


SPX0304
304
2965
174
522
229
8.10E-27
[LN:YSNB_BACSU]
136









[AC:P94559]









[GN:YSNB]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 19.2 KD PROTEIN IN RPH-ILVB INTERGENIC REGION]









[SP:P94559]


SPX0305
305
2966
154
462
75
8.30E-08
[LN:A69866]
136









[AC:A69866]









[PN:hypothetical protein ykuL]









[GN:ykuL]









[CL:Bacillus subtilis hypothetical protein ykuL]









[OR:Bacillus subtilis]


SPX0306
306
2967
247
741
61
0.0006
[LN:A75153]
164









[AC:A75153]









[PN:integrase/recombinase xerd PAB0255]









[GN:xerD-like:PAB0255]









[CL:probable site-specific integrase/recombinase XerC]









[OR:Pyrococcus abyssi]


SPX0307
307
2968
243
729
233
1.60E-40
[LN:YPUG_BACSU]
145









[AC:P35154]









[GN:YPUG]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 29.6 KD PROTEIN IN RIBT-DACB INTERGENIC REGION (ORFX7)]









[SP:P35154]


SPX0308
308
2969
190
570
216
2.00E-28
[LN:Y214_MYCPN]
106









[AC:P75477]









[OR:Mycoplasma pneumoniae]









[DE:HYPOTHETICAL PROTEIN MG214 HOMOLOG]









[SP:P75477]


SPX0309
309
2970
241
723
660
5.60E-86
[LN:RLUB_BACSU]
138









[AC:P35159]









[GN:RLUB]









[OR:Bacillus subtilis]









[EC:4.2.1.70]









[DE:(PSEUDOURIDYLATE SYNTHASE) (URACIL HYDROLYASE)]









[SP:P35159]


SPX0310
310
2971
81
243
166
1.10E-32
[LN:G72251]
139









[AC:G72251]









[PN:conserved hypothetical protein]









[GN:TM1462]









[CL:conserved hypothetical protein HI1000]









[OR:Thermotoga maritima]


SPX0311
311
2972
175
525


NO-HIT
6


SPX0312
312
2973
322
966
218
2.70E-57
[LN:E69763]
146









[AC:E69763]









[PN:probable ferrichrome ABC transporter yclQ]









[GN:yclQ]









[CL:iron(III) dicitrate transport protein]









[OR:Bacillus subtilis]


SPX0313
313
2974
251
753
702
2.90E-92
[LN:D69763]
194









[AC:D69763]









[PN:ferrichrome ABC transporter (ATP-binding p) homolog yclP]









[GN:yclP]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Bacillus subtilis]


SPX0314
314
2975
67
201
89
6.60E-07
[LN:G72510]
92









[AC:G72510]









[PN:hypothetical protein APE2061]









[GN:APE2061]









[OR:Aeropyrum pernix]


SPX0315
315
2976
319
957
474
8.60E-64
[LN:C69763]
146









[AC:C69763]









[PN:ferrichrome ABC transporter (permease) homolog yclO]









[GN:yclO]









[CL:ferrichrome ABC transporter]









[OR:Bacillus subtilis]


SPX0316
316
2977
320
960
625
2.80E-84
[LN:B69763]
153









[AC:B69763]









[PN:ferrichrome ABC transporter (permease) homolog yclN]









[GN:yclN]









[CL:vitamin B12 transport protein btuC]









[OR:Bacillus subtilis]


SPX0317
317
2978
136
408
288
3.50E-36
[GI:6707010]
98









[LN:AF109295]









[AC:AF109295:AF022796]









[PN:GalE]









[GN:galE]









[OR:Staphylococcus carnosus]


SPX0318
318
2979
81
243
164
6.20E-18
[GI:3703059]
105









[LN:AF082009]









[AC:AF082009]









[PN:UDP-galactose-4-epimerase]









[GN:galE]









[OR:Lactococcus lactis]


SPX0319
319
2980
354
1062
388
8.30E-143
“[LN:PEPA_LACLC]
162









[AC:Q48677]









[GN:PEPA]









[OR:Lactococcus lactis]









[SR:,subspcremoris:Streptococcus cremoris]









[EC:3.4.11.7]









[DE:GLUTAMYL-AMINOPEPTIDASE,]









[SP:Q48677]]


SPX0320
320
2981
99
297


NO-HIT
6


SPX0321
321
2982
63
189


NO-HIT
6


SPX0322
322
2983
148
444
87
0.00059
[GI:2791904]
78









[LN:SSK3MECA1]









[AC:Y13052]









[GN:ORF145]









[OR:Staphylococcus sciuri]


SPX0323
323
2984
255
765


NO-HIT
6


SPX0324
324
2985
243
729
1211
8.40E-163
[GI:5579394]
117









[LN:AF162655]









[AC:AF162655]









[PN:choline transporter]









[GN:proV]









[FN:ATPase]









[OR:Streptococcus pneumoniae]


SPX0325
325
2986
29
87


NO-HIT
6


SPX0326
326
2987
311
933
1434
2.40E-200
[LN:T44634]
100









[AC:T44634]









[PN:choline transporter [imported]]









[GN:proWX]









[OR:Streptococcus pneumoniae]


SPX0327
327
2988
210
630
1042
3.30E-137
[LN:T44634]
100









[AC:T44634]









[PN:choline transporter [imported]]









[GN:proWX]









[OR:Streptococcus pneumoniae]


SPX0328
328
2989
270
810
125
1.90E-15
[LN:YA7B_HAEIN]
130









[AC:Q57425:P96338]









[GN:HI1077.1]









[OR:Haemophilus influenzae]









[DE:HYPOTHETICAL PROTEIN HI1077.1]









[SP:Q57425:P96338]


SPX0329
329
2990
179
537
150
8.10E-17
[GI:5881867]
139









[LN:SC5G9]









[AC:AL117385]









[PN:putative tetR-family transcriptional regulator]









[GN:SC5G9.19c]









[OR:Streptomyces coelicolor A3(2)]


SPX0330
330
2991
300
900
202
5.60E-39
[GI:1944409]
151









[LN:D87026]









[AC:D87026:D28136]









[PN:membrane protein]









[OR:Bacillus stearothermophilus]









[SR:Bacillus stearothermophilus (strain:TRBE14) DNA]


SPX0331
331
2992
118
354
282
3.60E-34
[LN:B69970]
144









[AC:B69970]









[PN:transcription regulator MerR family homolog yraB]









[GN:yraB]









[CL:transcription repressor glnR]









[OR:Bacillus subtilis]


SPX0332
332
2993
346
1038
403
3.80E-82
[LN:T44975]
146









[AC:T44975]









[PN:dehydrogenase [imported]]









[CL:alcohol dehydrogenase:long-chain alcohol dehydrogenase homology]









[OR:Haloferax volcanii]


SPX0333
333
2994
336
1008
729
4.00E-144
[GI:4097439]
90









[LN:STU61402]









[AC:U61402]









[PN:GalR]









[GN:galR]









[OR:Streptococcus thermophilus]


SPX0334
334
2995
393
1179
1674
3.10E-227
[GI:4097440]
125









[LN:STU61402]









[AC:U61402]









[PN:galactokinase]









[GN:galK]









[FN:galactose metabolism]









[OR:Streptococcus thermophilus]


SPX0335
335
2996
494
1482
1612
1.90E-230
[GI:4097441]
139









[LN:STU61402]









[AC:U61402]









[PN:gal-1-P uridylyltransferase]









[GN:galT]









[FN:galactose metabolism]









[OR:Streptococcus thermophilus]


SPX0336
336
2997
135
405
467
1.10E-60
[GI:1196924]
81









[LN:STRDPN2A]









[AC:M14339]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX0337
337
2998
296
888
1461
6.00E-199
[LN:MT21_STRPN]
137









[AC:P04043]









[GN:DPNM]









[OR:Streptococcus pneumoniae]









[EC:2.1.1.72]









[DE:METHYLTRANSFERASE DPNII 1) (M.DPNII 1)]









[SP:P04043]


SPX0338
338
2999
257
771
1366
2.60E-183
[LN:MT22_STRPN]
137









[AC:P09358]









[GN:DPNA]









[OR:Streptococcus pneumoniae]









[EC:2.1.1.72]









[DE:METHYLTRANSFERASE DPNII 2) (M.DPNII 2)]









[SP:P09358]


SPX0339
339
3000
289
867
1492
5.50E-202
[LN:T2D2_STRPN]
108









[AC:P09357]









[GN:DPNB]









[OR:Streptococcus pneumoniae]









[EC:3.1.21.4]









[DE:(R.DPNII)]









[SP:P09357]


SPX0340
340
3001
119
357
462
1.20E-61
[GI:6978345]
81









[LN:STRDPN2A]









[AC:M14339]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX0341
341
3002
283
849
436
8.70E-87
[LN:YUNK_BACSU]
136









[AC:O32140]









[GN:YUNK]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 44.9 KD PROTEIN IN HOM-MRGA INTERGENIC REGION]









[SP:O32140]


SPX0342
342
3003
194
582
786
3.40E-105
[GI:7160242]
120









[LN:SPN272465]









[AC:AJ272465]









[PN:xanthine phosphoribosyltransferase]









[GN:xpt]









[OR:Streptococcus pneumoniae]


SPX0343
343
3004
58
174
79
7.70E-11
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX0344
344
3005
80
240
113
5.90E-10
[LN:C75408]
90









[AC:C75408]









[PN:hypothetical protein]









[GN:DR1341]









[OR:Deinococcus radiodurans]


SPX0345
345
3006
276
828
1432
8.60E-192
“[LN:EXOA_STRPN]
122









[AC:P21998]









[GN:EXOA]









[OR:Streptococcus pneumoniae]









[EC:3.1.11.2]









[DE:EXODEOXYRIBONUCLEASE,]









[SP:P21998]]


SPX0346
346
3007
76
228


NO-HIT
6


SPX0347
347
3008
90
270


NO-HIT
6


SPX0348
348
3009
177
531
132
9.60E-19
[LN:F69972]
128









[AC:F69972]









[PN:probable membrane protein yrbG]









[GN:yrbG]









[CL:probable membrane protein ycaP]









[OR:Bacillus subtilis]


SPX0349
349
3010
79
237
129
5.90E-21
[GI:1914870]
81









[LN:SPZ82001]









[AC:Z82001]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX0350
350
3011
582
1746
685
1.90E-170
[LN:A69829]
188









[AC:A69829]









[PN:ABC transporter (ATP-binding protein) homolog yheI]









[GN:yheI]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Bacillus subtilis]


SPX0351
351
3012
294
882
364
6.80E-49
[LN:H69828]
188









[AC:H69828]









[PN:ABC transporter (ATP-binding protein) homolog yheH]









[GN:yheH]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Bacillus subtilis]


SPX0352
352
3013
69
207
82
0.00022
[LN:H69828]
188









[AC:H69828]









[PN:ABC transporter (ATP-binding protein) homolog yheH]









[GN:yheH]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Bacillus subtilis]


SPX0353
353
3014
264
792
383
3.90E-79
[LN:H69828]
188









[AC:H69828]









[PN:ABC transporter (ATP-binding protein) homolog yheH]









[GN:yheH]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Bacillus subtilis]


SPX0354
354
3015
232
696
632
1.10E-83
[GI:6601354]
115









[LN:AF164515]









[AC:AF164515]









[PN:putative glycosyltransferase Cps7F]









[GN:cps7F]









[OR:Streptococcus suis]


SPX0355
355
3016
409
1227
973
4.70E-214
[GI:6601355]
86









[LN:AF164515]









[AC:AF164515]









[PN:Cps7G]









[GN:cps7G]









[OR:Streptococcus suis]


SPX0356
356
3017
63
189


NO-HIT
6


SPX0357
357
3018
89
267


NO-HIT
6


SPX0358
358
3019
709
2127
107
4.60E-08
[GI:2952545]
109









[LN:AF051898]









[AC:AF051898]









[PN:coronin binding protein]









[GN:DB10]









[OR:Dictyostelium discoideum]


SPX0359
359
3020
82
246


NO-HIT
6


SPX0360
360
3021
69
207


NO-HIT
6


SPX0361
361
3022
95
285


NO-HIT
6


SPX0362
362
3023
96
288
289
6.60E-34
[GI:43589]
103









[LN:HILIC3]









[AC:X57315]









[PN:UDP-galactose-4-epimerase]









[GN:galE]









[OR:Haemophilus influenzae]


SPX0363
363
3024
66
198


NO-HIT
6


SPX0364
364
3025
220
660


NO-HIT
6


SPX0365
365
3026
356
1068
286
2.20E-30
“[LN:Y4FP_RHISN]
162









[AC:P55454]









[GN:Y4FP]









[OR:Rhizobium sp]









[SR:,strain NGR234]









[DE:PROBABLE ABC TRANSPORTER PERIPLASMIC BINDING PROTEIN Y4FP PRECURSOR]









[SP:P55454]]


SPX0366
366
3027
337
1011
395
3.30E-90
“[LN:A70180]
237









[AC:A70180]









[PN:spermidine/putrescine ABC transporter, ATP-binding protein (potA) homolog]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Borrelia burgdorferi]









[SR:, Lyme disease spirochete]









”””


SPX0367
367
3028
564
1692
433
1.50E-93
“[LN:Y4FN_RHISN]
141









[AC:P55452]









[GN:Y4FN]









[OR:Rhizobium sp]









[SR:,strain NGR234]









[DE:PROBABLE ABC TRANSPORTER PERMEASE PROTEIN Y4FN]









[SP:P55452]”


SPX0368
368
3029
237
711
192
4.80E-28
[LN:Y647_HAEIN]
126









[AC:Q57424:O05028]









[GN:HI0647]









[OR:Haemophilus influenzae]









[DE:HYPOTHETICAL PROTEIN HI0647]









[SP:Q57424:O05028]


SPX0369
369
3030
103
309


NO-HIT
6


SPX0370
370
3031
334
1002
144
3.70E-25
[LN:CCPA_BACME]
145









[AC:P46828]









[GN:CCPA]









[OR:Bacillus megaterium]









[DE:GLUCOSE-RESISTANCE AMYLASE REGULATOR (CATABOLITE CONTROL PROTEIN)]









[SP:P46828]


SPX0371
371
3032
66
198


NO-HIT
6


SPX0372
372
3033
69
207


NO-HIT
6


SPX0373
373
3034
488
1464
1100
2.50E-173
“[LN:TRPE_LACLA]
168









[AC:Q02001]









[GN:TRPE]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:4.1.3.27]









[DE:ANTHRANILATE SYNTHASE COMPONENT I,]









[SP:Q02001]”


SPX0374
374
3035
67
201
108
6.30E-10
[LN:C72489]
92









[AC:C72489]









[PN:hypothetical protein APE2554]









[GN:APE2554]









[OR:Aeropyrum pernix]


SPX0375
375
3036
189
567
440
8.80E-75
“[LN:TRPG_LACLA]
146









[AC:Q02003]









[GN:TRPG]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:4.1.3.27]









[DE:TRANSFERASE)]









[SP:Q02003]”


SPX0376
376
3037
335
1005
1008
9.70E-134
“[LN:TRPD_LACLA]
173









[AC:Q02000]









[GN:TRPD]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:2.4.2.18]









[DE:ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE,]









[SP:Q02000]”


SPX0377
377
3038
256
768
446
6.20E-107
“[LN:TRPC_LACLA]
178









[AC:Q01999]









[GN:TRPC]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:4.1.1.48]









[DE:INDOLE-3-GLYCEROL PHOSPHATE SYNTHASE, (IGPS)]









[SP:Q01999]”


SPX0378
378
3039
210
630
225
3.50E-49
“[LN:TRPF_LACLA]
185









[AC:Q02002]









[GN:TRPF]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:5.3.1.24]









[DE:N-(5′-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE, (PRAI)]









[SP:Q02002]”


SPX0379
379
3040
408
1224
930
9.00E-225
“[LN:TRPB_LACLA]
165









[AC:Q01998]









[GN:TRPB]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:4.2.1.20]









[DE:TRYPTOPHAN SYNTHASE BETA CHAIN,]









[SP:Q01998]”


SPX0380
380
3041
278
834
1137
5.00E-153
[GI:5231181]
117









[LN:AF157817]









[AC:AF157817]









[PN:tryptophan synthase alpha chain]









[GN:trpA]









[OR:Streptococcus pneumoniae]


SPX0381
381
3042
68
204


NO-HIT
6


SPX0382
382
3043
244
732


NO-HIT
6


SPX0383
383
3044
384
1152
92
2.70E-13
[LN:H70940]
116









[AC:H70940]









[PN:probable helix-turn-helix motif at aa 18-39]









[GN:Rv2017]









[OR:Mycobacterium tuberculosis]


SPX0384
384
3045
220
660
109
1.00E-14
[LN:B72220]
124









[AC:B72220]









[PN:type IV prepilin peptidase]









[GN:TM1696]









[CL:type IV prepilin peptidase]









[OR:Thermotoga maritima]


SPX0385
385
3046
149
447
92
0.00011
[LN:E72312]
169









[AC:E72312]









[PN:conserved hypothetical protein]









[GN:TM0968]









[CL:Escherichia coli ribosomal-protein-alanine N-acetyltransferase rimJ]









[OR:Thermotoga maritima]


SPX0386
386
3047
104
312
138
1.30E-12
“[GI:6332767]
194









[LN:AB033763]









[AC:AB033763:AB014419:AB014429:AB014439]









[PN:hypothetical protein]









[OR:Staphylococcus aureus]









[SR:Staphylococcus aureus (strain:NCTC10442) DNA, clone_lib:Lambda das]”


SPX0387
387
3048
68
204
98
8.10E-08
[GI:2772940]
116









[LN:AF034574]









[AC:AF034574]









[PN:putative cruciform DNA binding protein]









[GN:Gv1]









[OR:Glomus versiforme]


SPX0388
388
3049
203
609
515
8.70E-64
[GI:727436]
61









[LN:LLU23376]









[AC:U23376]









[OR:Lactococcus lactis]


SPX0389
389
3050
191
573


NO-HIT
6


SPX0390
390
3051
513
1539
193
6.90E-35
“[GI:6782400]
171









[LN:STC133440]









[AC:AJ133440]









[PN:multigene regulator protein Mgc, putative]









[GN:mgc]









[FN:gene regulatory function, putative]









[OR:Streptococcus dysgalactiae]”


SPX0391
391
3052
334
1002
185
3.80E-46
[LN:SCRR_STRMU]
137









[AC:Q54430]









[GN:SCRR]









[OR:Streptococcus mutans]









[DE:SUCROSE OPERON REPRESSOR (SCR OPERON REGULATORY PROTEIN)]









[SP:Q54430]


SPX0392
392
3053
315
945
376
2.50E-89
[LN:A69653]
125









[AC:A69653]









[PN:transmembrane lipoprotein lplB]









[GN:lplB]









[CL:inner membrane protein ugpA]









[OR:Bacillus subtilis]


SPX0393
393
3054
306
918
450
1.20E-73
[LN:LPLC_BACSU]
90









[AC:P39129]









[GN:LPLC]









[OR:Bacillus subtilis]









[DE:LPLC PROTEIN]









[SP:P39129]


SPX0394
394
3055
539
1617
167
2.90E-15
[GI:4056657]
136









[LN:AF098273]









[AC:AF098273]









[PN:peripheral protein]









[GN:glucuronic acid catabolism operon]









[OR:Bacillus stearothermophilus]


SPX0395
395
3056
141
423


NO-HIT
6


SPX0396
396
3057
440
1320
305
2.30E-76
“[LN:RAFD_ECOLI]
125









[AC:P16553]









[GN:RAFD]









[OR:Escherichia coli]









[EC:3.2.1.26]









[DE:RAFFINOSE INVERTASE, (INVERTASE)]









[SP:P16553]”


SPX0397
397
3058
424
1272
722
7.10E-167
[LN:D69981]
163









[AC:D69981]









[PN:conserved hypothetical protein yrvN]









[GN:yrvN]









[CL:Haemophilus influenzae conserved hypothetical protein HI1590]









[OR:Bacillus subtilis]


SPX0398
398
3059
74
222


NO-HIT
6


SPX0399
399
3060
60
180


NO-HIT
6


SPX0400
400
3061
84
252


NO-HIT
6


SPX0401
401
3062
151
453
92
4.90E-09
[LN:T13557]
146









[AC:T13557]









[PN:hypothetical protein 17]









[CL:Archaeoglobus fulgidus conserved hypothetical protein AF1072]









[OR:Bacillus phage phi-105]


SPX0402
402
3063
157
471


NO-HIT
6


SPX0403
403
3064
363
1089


NO-HIT
6


SPX0404
404
3065
345
1035
130
8.00E-15
[GI:758793]
72









[LN:ECU23723]









[AC:U23723]









[FN:unknown]









[OR:Escherichia coli]


SPX0405
405
3066
748
2244
68
0.00048
[GI:758794]
72









[LN:ECU23723]









[AC:U23723]









[FN:unknown]









[OR:Escherichia coli]


SPX0406
406
3067
340
1020


NO-HIT
6


SPX0407
407
3068
317
951
395
1.40E-81
“[LN:T43740]
215









[AC:T43740]









[PN:probable ribosomal protein L11 methyltransferase, [imported]









:hypothetical protein 35]









[CL:ribosomal protein L11 methyltransferase:bioC homology]









[OR:Listeria monocytogenes]









[EC:2.1.1.-]”


SPX0408
408
3069
248
744
461
1.90E-64
[LN:T43741]
104









[AC:T43741]









[PN:conserved hypothetical protein orf29 [imported]]









[OR:Listeria monocytogenes]


SPX0409
409
3070
599
1797
300
2.10E-57
“[LN:PEPF_BACSU]
123









[AC:O31605]









[GN:YJBG]









[OR:Bacillus subtilis]









[EC:3.4.24.-]









[DE:OLIGOENDOPEPTIDASE F HOMOLOG,]









[SP:O31605]”


SPX0410
410
3071
226
678
312
1.80E-58
[LN:D69780]
87









[AC:D69780]









[PN:hypothetical protein ydfF]









[GN:ydfF]









[OR:Bacillus subtilis]


SPX0411
411
3072
217
651
394
1.40E-54
[LN:G69803]
188









[AC:G69803]









[PN:ABC transporter (ATP-binding protein) homolog yfiL]









[GN:yfiL]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Bacillus subtilis]


SPX0412
412
3073
255
765
346
4.20E-44
“[LN:NODJ_RHILV]
126









[AC:P06755]









[GN:NODJ]









[OR:Rhizobium leguminosarum]









[SR:,biovar viciae]









[DE:NODULATION PROTEIN J]









[SP:P06755]”


SPX0413
413
3074
264
792


NO-HIT
6


SPX0414
414
3075
210
630
257
3.90E-39
“[LN:A69428]
130









[AC:A69428]









[PN:glycerol uptake facilitator, MIP channel (glpF) homolog]









[CL:nodulin-26]









[OR:Archaeoglobus fulgidus]”


SPX0415
415
3076
60
180


NO-HIT
6


SPX0416
416
3077
191
573
467
1.10E-60
[LN:D69868]
128









[AC:D69868]









[PN:conserved hypothetical protein ykvM]









[GN:ykvM]









[CL:hypothetical protein ykvM]









[OR:Bacillus subtilis]


SPX0417
417
3078
105
315
193
1.80E-43
[GI:5640117]
129









[LN:LMO133006]









[AC:AJ133006]









[PN:thioredoxin]









[GN:trxA]









[FN:thiol:disulfide interchange]









[OR:Listeria monocytogenes]


SPX0418
418
3079
101
303


NO-HIT
6


SPX0419
419
3080
67
201


NO-HIT
6


SPX0420
420
3081
75
225


NO-HIT
6


SPX0421
421
3082
318
954
433
2.70E-56
[LN:YQJA_BACSU]
137









[AC:P54538]









[GN:YQJA]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 37.1 KD PROTEIN IN BMRU-ANSR INTERGENIC REGION]









[SP:P54538]


SPX0422
422
3083
287
861
745
1.50E-100
[LN:YGJU_HAEIN]
114









[AC:P45246]









[GN:HI1545]









[OR:Haemophilus influenzae]









[DE:HYPOTHETICAL SYMPORTER HI1545]









[SP:P45246]


SPX0423
423
3084
75
225
153
4.00E-15
[LN:YGJU_ECOLI]
143









[AC:P42602]









[GN:YGJU]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 43.5 KD PROTEIN IN EBGC-UXAA INTERGENIC REGION (O414)]









[SP:P42602]


SPX0424
424
3085
140
420
163
2.90E-17
“[GI:2828366]
128









[LN:AB010789]









[AC:AB010789]









[OR:Lactococcus lactis]









[SR:Lactococcus lactis (sub_species:lactis, strain:01-7) DNA]”


SPX0425
425
3086
66
198
102
1.80E-07
[LN:A69867]
174









[AC:A69867]









[PN:conserved hypothetical protein ykuT]









[GN:ykuT]









[CL:Escherichia coli hypothetical 30.9K protein (sbm-fba intergenic region)]









[OR:Bacillus subtilis]


SPX0426
426
3087
59
177


NO-HIT
6


SPX0427
427
3088
303
909
270
1.70E-35
[GI:5123526]
112









[LN:AF036485]









[AC:AF036485:AF036486:AF036487:U93364]









[PN:hypothetical protein]









[OR:Plasmid pNZ4000]


SPX0428
428
3089
176
528
326
9.70E-41
[LN:YQEG_BACSU]
137









[AC:P54452]









[GN:YQEG]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 20.1 KD PROTEIN IN NUCB-AROD INTERGENIC REGION]









[SP:P54452]


SPX0429
429
3090
369
1107
1037
1.30E-164
[LN:YQEH_BACSU]
137









[AC:P54453]









[GN:YQEH]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 41.0 KD PROTEIN IN NUCB-AROD INTERGENIC REGION]









[SP:P54453]


SPX0430
430
3091
104
312
211
5.20E-24
[LN:YQEI_BACSU]
138









[AC:P54454]









[GN:YQEI]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 10.8 KD PROTEIN IN AROD-COMER INTERGENIC REGION]









[SP:P54454]


SPX0431
431
3092
205
615
491
1.30E-63
[LN:YQEJ_BACSU]
138









[AC:P54455]









[GN:YQEJ]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 22.2 KD PROTEIN IN AROD-COMER INTERGENIC REGION]









[SP:P54455]


SPX0432
432
3093
198
594
375
2.90E-47
[LN:YQEK_BACSU]
138









[AC:P54456]









[GN:YQEK]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 21.3 KD PROTEIN IN AROD-COMER INTERGENIC REGION]









[SP:P54456]


SPX0433
433
3094
167
501
110
4.90E-10
[GI:7160132]
119









[LN:SC5C11]









[AC:AL158060]









[PN:putative isochorismatase.]









[GN:SC5C11.12]









[OR:Streptomyces coelicolor A3(2)]


SPX0434
434
3095
118
354
267
7.00E-32
[LN:YQEL_BACSU]
138









[AC:P54457]









[GN:YQEL]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 13.3 KD PROTEIN IN AROD-COMER INTERGENIC REGION]









[SP:P54457]


SPX0435
435
3096
247
741
287
4.60E-55
[LN:YQEM_BACSU]
138









[AC:P54458]









[GN:YQEM]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 28.3 KD PROTEIN IN AROD-COMER INTERGENIC REGION]









[SP:P54458]


SPX0436
436
3097
188
564


NO-HIT
6


SPX0437
437
3098
366
1098
222
9.30E-38
[LN:B69875]
97









[AC:B69875]









[PN:conserved hypothetical protein ylbM]









[GN:ylbM]









[OR:Bacillus subtilis]


SPX0438
438
3099
63
189


NO-HIT
6


SPX0439
439
3100
916
2748
86
1.00E-10
[GI:1890605]
77









[LN:RMEXPGNS]









[AC:Z79692]









[PN:ORF25]









[OR:Sinorhizobium meliloti]


SPX0440
440
3101
537
1611
1547
2.30E-211
[GI:6984124]
81









[LN:AF228345]









[AC:AF228345]









[PN:unknown]









[OR:Listeria monocytogenes]


SPX0441
441
3102
209
627
614
1.40E-80
[LN:B69878]
139









[AC:B69878]









[PN:guanylate kinase homolog yloD]









[GN:yloD]









[CL:guanylate kinase:guanylate kinase homology]









[OR:Bacillus subtilis]


SPX0442
442
3103
105
315
91
1.00E-09
[LN:C69878]
87









[AC:C69878]









[PN:hypothetical protein yloH]









[GN:yloH]









[OR:Bacillus subtilis]


SPX0443
443
3104
799
2397
953
2.70E-237
[LN:PRIA_BACSU]
136









[AC:P94461:O34941]









[GN:PRIA]









[OR:Bacillus subtilis]









[DE:PRIMOSOMAL PROTEIN N′(REPLICATION FACTOR Y)]









[SP:P94461:O34941]


SPX0444
444
3105
312
936
434
1.70E-64
[GI:1772500]
105









[LN:BSPRIADFS]









[AC:Y10304]









[PN:Met-tRNAi formyl transferase]









[GN:fmt]









[OR:Bacillus subtilis]


SPX0445
445
3106
176
528
248
1.40E-39
[GI:1772501]
71









[LN:BSPRIADFS]









[AC:Y10304]









[GN:sun]









[OR:Bacillus subtilis]


SPX0446
446
3107
139
417
130
1.30E-09
[GI:4210751]
93









[LN:LLA132604]









[AC:AJ132604]









[PN:sunL protein]









[GN:sunL]









[OR:Lactococcus lactis]


SPX0447
447
3108
233
699
606
2.70E-80
[GI:4210751]
93









[LN:LLA132604]









[AC:AJ132604]









[PN:sunL protein]









[GN:sunL]









[OR:Lactococcus lactis]


SPX0448
448
3109
247
741
371
1.50E-85
[GI:4210752]
134









[LN:LLA132604]









[AC:AJ132604]









[PN:pppL protein]









[GN:pppL]









[FN:putative phosphoprotein phosphatase]









[OR:Lactococcus lactis]


SPX0449
449
3110
660
1980
985
1.70E-128
[GI:4210753]
91









[LN:LLA132604]









[AC:AJ132604]









[PN:hypothetical protein]









[OR:Lactococcus lactis]


SPX0450
450
3111
68
204


NO-HIT
6


SPX0451
451
3112
74
222


NO-HIT
6


SPX0452
452
3113
170
510
125
1.80E-09
[LN:YJJP_ECOLI]
143









[AC:P39402]









[GN:YJJP]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 30.5 KD PROTEIN IN DNAT-BGLJ INTERGENIC REGION (F277)]









[SP:P39402]


SPX0453
453
3114
112
336
94
4.60E-07
[LN:G81321]
121









[AC:G81321]









[PN:probable integral membrane protein Cj1165c [imported]]









[GN:Cj1165c]









[OR:Campylobacter jejuni]


SPX0454
454
3115
67
201
217
3.80E-24
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX0455
455
3116
130
390
362
7.00E-46
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX0456
456
3117
96
288


NO-HIT
6


SPX0457
457
3118
391
1173
775
1.30E-101
[GI:4096796]
67









[LN:SCU40157]









[AC:U40157]









[OR:Staphylococcus carnosus]


SPX0458
458
3119
425
1275
354
8.70E-92
[LN:MVAA_PSEMV]
106









[AC:P13702]









[GN:MVAA]









[OR:Pseudomonas mevalonii]









[EC:1.1.1.88]









[DE:REDUCTASE)]









[SP:P13702]


SPX0459
459
3120
322
966
1108
1.00E-150
[LN:SCRR_STRMU]
137









[AC:Q54430]









[GN:SCRR]









[OR:Streptococcus mutans]









[DE:SUCROSE OPERON REPRESSOR (SCR OPERON REGULATORY PROTEIN)]









[SP:Q54430]


SPX0460
460
3121
485
1455
1691
3.60E-229
“[LN:S68598]
189









[AC:S68598]









[PN:sucrose-6-phosphate hydrolase ScrB]









[GN:scrB]









[CL:sucrose-6-phosphate hydrolase]









[OR:Streptococcus sobrinus]









[SR:strain 6715, , strain 6715]









[SR:strain 6715, ]”


SPX0461
461
3122
77
231


NO-HIT
6


SPX0462
462
3123
66
198


NO-HIT
6


SPX0463
463
3124
628
1884
717
6.70E-255
“[LN:S68599]
177









[AC:S68599]









[PN:phosphotransferase system enzyme II,, sucrose-specific:sucrose-specific enzyme II:sucrose-specific enzyme II]









[GN:scrA]









[OR:Streptococcus sobrinus]”


SPX0464
464
3125
296
888
701
3.80E-158
“[LN:SCRK_STRMU]
109









[AC:Q07211]









[GN:SCRK]









[OR:Streptococcus mutans]









[EC:2.7.1.4]









[DE:FRUCTOKINASE,]









[SP:Q07211]”


SPX0465
465
3126
71
213


NO-HIT
6


SPX0466
466
3127
200
600
103
2.90E-07
[LN:YDJZ_ECOLI]
136









[AC:P76221]









[GN:YDJZ]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 26.2 KD PROTEIN IN XTHA-GDHA INTERGENIC REGION]









[SP:P76221]


SPX0467
467
3128
75
225
200
1.30E-21
[GI:517210]
65









[LN:SPU11799]









[AC:U11799]









[OR:Streptococcus pyogenes]


SPX0468
468
3129
84
252


NO-HIT
6


SPX0469
469
3130
76
228
187
3.50E-21
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX0470
470
3131
298
894
460
1.20E-78
[GI:3688825]
81









[LN:AF084104]









[AC:AF084104]









[PN:NatA]









[GN:natA]









[OR:Bacillus firmus]


SPX0471
471
3132
400
1200
200
4.70E-36
[GI:1150487]
89









[LN:LSLASAMPT]









[AC:Z54312]









[PN:unknown]









[GN:orf414]









[OR:Lactobacillus sakei]


SPX0472
472
3133
56
168


NO-HIT
6


SPX0473
473
3134
283
849


NO-HIT
6


SPX0474
474
3135
241
723
460
1.50E-58
“[LN:G71842]
238









[AC:G71842]









[PN:probable ABC transporter, ATP-binding protein]









[GN:jhp1141]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Helicobacter pylori]









[SR:strain J99, , strain J99]









[SR:strain J99, ]”


SPX0475
475
3136
70
210
95
4.40E-07
[LN:E72756]
92









[AC:E72756]









[PN:hypothetical protein APE0042]









[GN:APE0042]









[OR:Aeropyrum pernix]


SPX0476
476
3137
122
366
256
3.70E-30
[GI:5822822]
129









[LN:AB024564]









[AC:AB024564]









[PN:YHCF]









[GN:yhcF]









[OR:Bacillus halodurans]









[SR:Bacillus halodurans (strain:C-125) DNA]


SPX0477
477
3138
158
474
405
8.00E-51
[LN:E72221]
139









[AC:E72221]









[PN:conserved hypothetical protein]









[GN:TM1707]









[CL:conserved hypothetical protein HI0943]









[OR:Thermotoga maritima]


SPX0478
478
3139
390
1170


NO-HIT
6


SPX0479
479
3140
299
897
300
2.40E-58
[LN:DNAI_BACSU]
101









[AC:P06567]









[GN:DNAI]









[OR:Bacillus subtilis]









[DE:PRIMOSOMAL PROTEIN DNAI]









[SP:P06567]


SPX0480
480
3141
238
714
239
3.90E-35
“[LN:CHRR_PSESP]
110









[AC:P96977]









[GN:CHRR]









[OR:Pseudomonas sp]









[SR:,strain G-1]









[DE:CR(VI) REDUCTASE]









[SP:P96977]”


SPX0481
481
3142
437
1311
1986
1.10E-270
“[GI:6681650]
174









[LN:AB016077]









[AC:AB016077]









[PN:phosphoglycerate dehydrogenase]









[GN:pgdA]









[OR:Streptococcus mutans]









[SR:Streptococcus mutans (strain:MT8148) DNA, clone:pYT570]”


SPX0482
482
3143
115
345


NO-HIT
6


SPX0483
483
3144
118
354


NO-HIT
6


SPX0484
484
3145
64
192


NO-HIT
6


SPX0485
485
3146
284
852
103
3.00E-11
[GI:4102023]
134









[LN:AF007761]









[AC:AF007761]









[PN:MutR]









[GN:mutR]









[FN:positive transcriptional regulator of mutA]









[OR:Streptococcus mutans]


SPX0486
486
3147
131
393


NO-HIT
6


SPX0487
487
3148
264
792


NO-HIT
6


SPX0488
488
3149
226
678


NO-HIT
6


SPX0489
489
3150
211
633
282
3.20E-42
[LN:YYBJ_BACSU]
95









[AC:P37494]









[GN:YYBJ]









[OR:Bacillus subtilis]









[DE:INTERGENIC REGION]









[SP:P37494]


SPX0490
490
3151
96
288


NO-HIT
6


SPX0491
491
3152
838
2514
989
0
[LN:SECA_LISMO]
118









[AC:P47847]









[GN:SECA]









[OR:Listeria monocytogenes]









[DE:PREPROTEIN TRANSLOCASE SECA SUBUNIT]









[SP:P47847]


SPX0492
492
3153
344
1032
156
7.30E-47
[GI:7380801]
136









[LN:NMA7Z2491]









[AC:AL162758:AL157959]









[PN:phospho-2-dehydr-3-deoxyheptonate aldolase]









[GN:aroG]









[OR:Neisseria meningitidis]


SPX0493
493
3154
215
645
178
3.50E-34
[LN:AROF_ECOLI]
157









[AC:P00888]









[GN:AROF]









[OR:Escherichia coli]









[EC:4.1.2.15]









[DE:SYNTHETASE) (3-DEOXY-D-ARABINO-HEPTULOSONATE 7-PHOSPHATE SYNTHASE)]









[SP:P00888]


SPX0494
494
3155
111
333


NO-HIT
6


SPX0495
495
3156
89
267
132
2.60E-14
[GI:7380801]
136









[LN:NMA7Z2491]









[AC:AL162758:AL157959]









[PN:phospho-2-dehydr-3-deoxyheptonate aldolase]









[GN:aroG]









[OR:Neisseria meningitidis]


SPX0496
496
3157
121
363
177
1.70E-30
“[LN:H69772]
137









[AC:H69772]









[PN:holo-[acyl-carrier-protein]









synthase,]









[GN:ydcB]









[CL:holo-ACP synthase]









[OR:Bacillus subtilis]









[EC:2.7.8.7]”


SPX0497
497
3158
368
1104
1852
1.10E-252
[GI:5759209]
101









[LN:AF171873]









[AC:AF171873]









[PN:alanine racemase]









[GN:alr]









[OR:Streptococcus pneumoniae]


SPX0498
498
3159
672
2016
3357
0
“[LN:RECG_STRPN]
137









[AC:Q54900]









[GN:RECG:MMSA]









[OR:Streptococcus pneumoniae]









[EC:3.6.1.-]









[DE:ATP-DEPENDENT DNA HELICASE RECG,]









[SP:Q54900]”


SPX0499
499
3160
89
267
263
2.70E-32
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX0500
500
3161
68
204


NO-HIT
6


SPX0501
501
3162
327
981
447
1.40E-92
[GI:2353697]
117









[LN:AF001926]









[AC:AF001926]









[PN:xylan esterase 1]









[GN:axe1]









[OR:Thermoanaerobacterium sp. ′JW/SL YS485′]


SPX0502
502
3163
206
618
355
1.20E-44
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX0503
503
3164
168
504
172
1.10E-15
[GI:4101572]
122









[LN:AF004842]









[AC:AF004842]









[PN:major royal jelly protein MRJP5]









[GN:MRJP5]









[OR:Apis mellifera]









[SR:honeybee]


SPX0504
504
3165
76
228
371
3.40E-50
[LN:T30286]
89









[AC:T30286:S26297]









[PN:hypothetical protein 76]









[OR:Streptococcus pneumoniae]


SPX0505
505
3166
938
2814
4378
0
“[LN:NANA_STRPN]
155









[AC:Q59959:Q54722]









[GN:NANA]









[OR:Streptococcus pneumoniae]









[EC:3.2.1.18]









[DE:SIALIDASE A PRECURSOR, (NEURAMINIDASE A)]









[SP:Q59959:Q54722]”


SPX0506
506
3167
72
216


NO-HIT
6


SPX0507
507
3168
151
453
773
6.10E-103
[GI:1163111]
68









[LN:SPU43526]









[AC:U43526]









[OR:Streptococcus pneumoniae]


SPX0508
508
3169
446
1338
2307
0
[GI:1163112]
68









[LN:SPU43526]









[AC:U43526]









[OR:Streptococcus pneumoniae]


SPX0509
509
3170
295
885
1542
2.00E-218
[GI:1163113]
68









[LN:SPU43526]









[AC:U43526]









[OR:Streptococcus pneumoniae]


SPX0510
510
3171
278
834
1375
3.80E-192
[GI:1163114]
68









[LN:SPU43526]









[AC:U43526]









[OR:Streptococcus pneumoniae]


SPX0511
511
3172
254
762
1250
1.40E-167
“[LN:NANB_STRPN]
141









[AC:Q54727]









[GN:NANB]









[OR:Streptococcus pneumoniae]









[EC:3.2.1.18]









[DE:SIALIDASE B PRECURSOR, (NEURAMINIDASE B)]









[SP:Q54727]”


SPX0512
512
3173
126
378
333
1.60E-40
[GI:517210]
65









[LN:SPU11799]









[AC:U11799]









[OR:Streptococcus pyogenes]


SPX0513
513
3174
211
633
762
7.90E-101
[GI:517210]
65









[LN:SPU11799]









[AC:U11799]









[OR:Streptococcus pyogenes]


SPX0514
514
3175
467
1401
2363
0
“[LN:NANB_STRPN]
141









[AC:Q54727]









[GN:NANB]









[OR:Streptococcus pneumoniae]









[EC:3.2.1.18]









[DE:SIALIDASE B PRECURSOR, (NEURAMINIDASE B)]









[SP:Q54727]”


SPX0515
515
3176
368
1104
1838
1.30E-249
[LN:YJHC_STRPN]
131









[AC:Q54728]









[OR:Streptococcus pneumoniae]









[DE:HYPOTHETICAL PROTEIN IN NANB 3′REGION (ORF-5) (FRAGMENT)]









[SP:Q54728]


SPX0516
516
3177
130
390


NO-HIT
6


SPX0517
517
3178
233
699
331
1.90E-64
“[LN:C70180]
125









[AC:C70180]









[PN:conserved hypothetical protein BB0644]









[OR:Borrelia burgdorferi]









[SR:, Lyme disease spirochete]”


SPX0518
518
3179
506
1518
839
2.60E-178
“[LN:D70180]
167









[AC:D70180]









[PN:phosphotransferase system enzyme II,, glucose-specific, factor II]









[OR:Borrelia burgdorferi]









[SR:, Lyme disease spirochete]









[EC:2.7.1.69]”


SPX0519
519
3180
443
1329
110
1.90E-09
[GI:6137033]
132









[LN:SCF11]









[AC:AL132662]









[PN:putative sugar transporter sugar binding]









[GN:SCF11.11]









[OR:Streptomyces coelicolor A3(2)]


SPX0520
520
3181
296
888
211
1.60E-50
“[LN:E72357]
140









[AC:E72357]









[PN:sugar ABC transporter, permease protein]









[GN:TM0596]









[CL:inner membrane protein malF]









[OR:Thermotoga maritima]”


SPX0521
521
3182
280
840
434
1.10E-65
“[LN:F72379]
143









[AC:F72379]









[PN:sugar ABC transporter, permease protein]









[GN:TM0430]









[CL:maltose transport protein malG]









[OR:Thermotoga maritima]”


SPX0522
522
3183
151
453
109
2.60E-13
[LN:YJGK_ECOLI]
144









[AC:P39335]









[GN:YJGK]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 17.3 KD PROTEIN IN PYRL-ARGI INTERGENIC REGION (O153B)]









[SP:P39335]


SPX0523
523
3184
118
354


NO-HIT
6


SPX0524
524
3185
66
198


NO-HIT
6


SPX0525
525
3186
215
645


NO-HIT
6


SPX0526
526
3187
220
660
830
1.30E-109
[GI:2385360]
100









[LN:CTSIALIDA]









[AC:Y08695]









[PN:putative acylneuraminate lyase]









[OR:Clostridium tertium]


SPX0527
527
3188
100
300
68
0.00016
[GI:42131]
55









[LN:ECNPL]









[AC:X03345]









[OR:Escherichia coli]


SPX0528
528
3189
295
885
423
2.50E-53
[LN:YNGA_CLOPE]
129









[AC:P26832]









[OR:Clostridium perfringens]









[DE:HYPOTHETICAL PROTEIN IN NAGH 5′REGION (ORFA) (FRAGMENT)]









[SP:P26832]


SPX0529
529
3190
283
849
170
2.10E-25
[LN:Y143_HAEIN]
112









[AC:P44540]









[GN:HI0143]









[OR:Haemophilus influenzae]









[DE:HYPOTHETICAL PROTEIN HI0143]









[SP:P44540]


SPX0530
530
3191
681
2043
3365
0
[GI:4009463]
116









[LN:AF068901]









[AC:AF068901]









[PN:penicillin-binding protein 2b]









[GN:pbp2b]









[OR:Streptococcus pneumoniae]


SPX0531
531
3192
119
357
524
5.00E-69
[GI:49383]
143









[LN:SPPBP2BH]









[AC:Z21808]









[PN:internal region of the penicillin-binding]









[FN:penicillin-resistantance]









[OR:Streptococcus pneumoniae]


SPX0532
532
3193
171
513
625
4.80E-83
[GI:4009464]
90









[LN:AF068901]









[AC:AF068901]









[PN:RecM]









[GN:recM]









[OR:Streptococcus pneumoniae]


SPX0533
533
3194
348
1044
1766
1.30E-239
[GI:4009465]
103









[LN:AF068901]









[AC:AF068901]









[PN:D-Ala-D-Ala ligase]









[GN:ddl]









[OR:Streptococcus pneumoniae]


SPX0534
534
3195
458
1374
2278
0
[GI:4009466]
111









[LN:AF068901]









[AC:AF068901]









[PN:D-Ala-D-Ala adding enzyme]









[GN:murF]









[OR:Streptococcus pneumoniae]


SPX0535
535
3196
449
1347
403
3.50E-76
[GI:5822769]
109









[LN:AB024553]









[AC:AB024553]









[OR:Bacillus halodurans]









[SR:Bacillus halodurans (strain:C-125) DNA]


SPX0536
536
3197
192
576
954
1.80E-127
[GI:4009467]
90









[LN:AF068901]









[AC:AF068901]









[PN:MutT]









[GN:mutT]









[OR:Streptococcus pneumoniae]


SPX0537
537
3198
199
597
1003
1.80E-140
[GI:4009468]
83









[LN:AF068901]









[AC:AF068901]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX0538
538
3199
87
261


NO-HIT
6


SPX0539
539
3200
458
1374
2266
0
[GI:4009469]
112









[LN:AF068901]









[AC:AF068901]









[PN:cell division protein FtsA]









[GN:ftsA]









[OR:Streptococcus pneumoniae]


SPX0540
540
3201
419
1257
2094
4.10E-280
[GI:4009470]
112









[LN:AF068901]









[AC:AF068901]









[PN:cell division protein FtsZ]









[GN:ftsZ]









[OR:Streptococcus pneumoniae]


SPX0541
541
3202
79
237
178
2.40E-19
[LN:A71218]
95









[AC:A71218]









[PN:hypothetical protein PH0004]









[GN:PH0004]









[OR:Pyrococcus horikoshii]


SPX0542
542
3203
224
672
1101
6.20E-148
[GI:4009471]
90









[LN:AF068901]









[AC:AF068901]









[PN:YlmE]









[GN:ylmE]









[OR:Streptococcus pneumoniae]


SPX0543
543
3204
180
540
920
1.10E-122
[GI:4009472]
90









[LN:AF068901]









[AC:AF068901]









[PN:YlmF]









[GN:ylmF]









[OR:Streptococcus pneumoniae]


SPX0544
544
3205
88
264
431
1.50E-58
[GI:4009473]
90









[LN:AF068901]









[AC:AF068901]









[PN:YlmG]









[GN:ylmG]









[OR:Streptococcus pneumoniae]


SPX0545
545
3206
262
786
1318
2.10E-179
[GI:4009474]
90









[LN:AF068901]









[AC:AF068901]









[PN:YlmH]









[GN:ylmH]









[OR:Streptococcus pneumoniae]


SPX0546
546
3207
263
789
1297
1.90E-171
[GI:4009475]
116









[LN:AF068901]









[AC:AF068901]









[PN:cell division protein DivIVA]









[GN:divIVA]









[OR:Streptococcus pneumoniae]


SPX0547
547
3208
931
2793
4840
0
[GI:4009476]
112









[LN:AF068901]









[AC:AF068901]









[PN:isoleucine-tRNA synthetase]









[GN:ileS]









[OR:Streptococcus pneumoniae]


SPX0548
548
3209
62
186
82
0.00016
“[LN:A56034]
120









[AC:A56034]









[PN:insulin activator factor]









[CL:human insulin activator factor]









[OR:Homo sapiens]









[SR:, man]”


SPX0549
549
3210
87
261
192
2.20E-20
“[LN:A56034]
120









[AC:A56034]









[PN:insulin activator factor]









[CL:human insulin activator factor]









[OR:Homo sapiens]









[SR:, man]”


SPX0550
550
3211
63
189


NO-HIT
6


SPX0551
551
3212
72
216


NO-HIT
6


SPX0552
552
3213
231
693
1201
1.00E-160
[GI:5578891]
107









[LN:SPN131985]









[AC:AJ131985]









[PN:phosphoglyceromutase]









[GN:gpmA]









[OR:Streptococcus pneumoniae]


SPX0553
553
3214
804
2412
232
2.70E-95
[GI:5912520]
124









[LN:SCF12]









[AC:AL117669]









[PN:putative large secreted protein]









[GN:SCF12.20c]









[OR:Streptomyces coelicolor A3(2)]


SPX0554
554
3215
237
711
642
7.20E-84
“[LN:B69477]
179









[AC:B69477]









[PN:ABC transporter, ATP-binding protein homolog]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Archaeoglobus fulgidus]”


SPX0555
555
3216
925
2775
106
1.10E-16
[LN:C69477]
84









[AC:C69477]









[PN:hypothetical protein AF1820]









[OR:Archaeoglobus fulgidus]


SPX0556
556
3217
173
519
878
1.10E-117
[GI:4193357]
137









[LN:AF055088]









[AC:AF055088:AF055087]









[PN:putative hydrophobic transmembrane protein]









[GN:psaD]









[OR:Streptococcus pneumoniae]


SPX0557
557
3218
310
930
1579
2.30E-209
[GI:3258602]
150









[LN:SPU40786]









[AC:U40786]









[PN:surface antigen A variant precursor]









[GN:psaA]









[FN:putative fimbrial adhesin]









[OR:Streptococcus pneumoniae]


SPX0558
558
3219
283
849
1171
8.00E-165
[LN:P29K_STRGC]
127









[AC:P42361]









[OR:Streptococcus gordonii challis]









[DE:29 KD MEMBRANE PROTEIN IN PSAA 5′REGION (ORF1)]









[SP:P42361]


SPX0559
559
3220
252
756
1208
2.80E-164
[GI:4193356]
115









[LN:AF055088]









[AC:AF055088:AF055087]









[PN:ATP-binding cassette]









[GN:psaB]









[OR:Streptococcus pneumoniae]


SPX0560
560
3221
651
1953
1477
0
[GI:5139244]
104









[LN:AF116532]









[AC:AF116532]









[PN:endopeptidase O]









[GN:pepO]









[OR:Streptococcus parasanguinis]


SPX0561
561
3222
210
630
181
2.90E-36
[LN:YQGX_BACSU]
138









[AC:P54501]









[GN:YQGX]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 23.2 KD PROTEIN IN SODA-COMGA INTERGENIC REGION]









[SP:P54501]


SPX0562
562
3223
67
201
131
2.00E-13
[GI:1914870]
81









[LN:SPZ82001]









[AC:Z82001]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX0563
563
3224
81
243


NO-HIT
6


SPX0564
564
3225
741
2223
1601
0
[LN:RELA_STREQ]
111









[AC:Q54089]









[GN:RELA:REL]









[OR:Streptococcus equisimilis]









[EC:2.7.6.5]









[DE:PROTEIN)]









[SP:Q54089]


SPX0565
565
3226
81
243
70
0.0001
[LN:Q3ECS7]
163









[AC:A30374:Q90796]









[PN:hypothetical 77K protein (spoT 3′region)]









[CL:Escherichia coli hypothetical 77K protein (spoT 3′region)]









[OR:Escherichia coli]


SPX0566
566
3227
148
444
585
2.40E-76
[LN:S39974]
123









[AC:S39974]









[PN:hypothetical protein]









[CL:conserved hypothetical protein HI0670]









[OR:Streptococcus equisimilis]


SPX0567
567
3228
76
228


NO-HIT
6


SPX0568
568
3229
141
423


NO-HIT
6


SPX0569
569
3230
236
708


NO-HIT
6


SPX0570
570
3231
140
420
433
7.90E-56
[GI:6694218]
105









[LN:AF182402]









[AC:AF182402]









[PN:metalloregulator RmtA]









[GN:rmtA]









[OR:Streptococcus gordonii]


SPX0571
571
3232
80
240
307
4.00E-38
[GI:6694218]
105









[LN:AF182402]









[AC:AF182402]









[PN:metalloregulator RmtA]









[GN:rmtA]









[OR:Streptococcus gordonii]


SPX0572
572
3233
281
843
125
2.00E-13
[LN:G75297]
167









[AC:G75297]









[PN:conserved hypothetical protein]









[GN:DR2233]









[CL:probable phosphoesterase MJ0912:phosphoesterase core homology]









[OR:Deinococcus radiodurans]


SPX0573
573
3234
65
195


NO-HIT
6


SPX0574
574
3235
105
315
142
7.90E-15
[LN:D70063]
87









[AC:D70063]









[PN:hypothetical protein ywnA]









[GN:ywnA]









[OR:Bacillus subtilis]


SPX0575
575
3236
73
219
129
2.40E-12
[LN:D70063]
87









[AC:D70063]









[PN:hypothetical protein ywnA]









[GN:ywnA]









[OR:Bacillus subtilis]


SPX0576
576
3237
101
303


NO-HIT
6


SPX0577
577
3238
358
1074


NO-HIT
6


SPX0578
578
3239
226
678
1146
1.70E-157
[GI:5830520]
104









[LN:SPAJ6391]









[AC:AJ006391]









[PN:response regulator]









[GN:rr01]









[OR:Streptococcus pneumoniae]


SPX0579
579
3240
325
975
1628
3.20E-226
[GI:5830521]
102









[LN:SPAJ6391]









[AC:AJ006391]









[PN:histidine kinase]









[GN:hk01]









[OR:Streptococcus pneumoniae]


SPX0580
580
3241
661
1983
1149
2.20E-274
[LN:SYT1_BACSU]
118









[AC:P18255:P06570]









[GN:THRS:THRSV]









[OR:Bacillus subtilis]









[EC:6.1.1.3]









[DE:(THRRS)]









[SP:P18255:P06570]


SPX0581
581
3242
130
390


NO-HIT
6


SPX0582
582
3243
97
291


NO-HIT
6


SPX0583
583
3244
70
210


NO-HIT
6


SPX0584
584
3245
210
630
371
1.30E-60
[LN:E70063]
87









[AC:E70063]









[PN:hypothetical protein ywnB]









[GN:ywnB]









[OR:Bacillus subtilis]


SPX0585
585
3246
90
270
311
1.10E-38
[LN:F69700]
214









[AC:F69700:S11365:S70690]









[PN:ribosomal protein S15 (rpsO):ribosomal protein BS18]









[GN:rpsO]









[CL:Escherichia coli ribosomal protein S15:eubacterial ribosomal protein S15 homology]









[OR:Bacillus subtilis]


SPX0586
586
3247
75
225


NO-HIT
6


SPX0587
587
3248
159
477
243
1.30E-38
[GI:1916729]
94









[LN:AF134905]









[AC:AF134905:U76550]









[PN:CadD]









[GN:cadD]









[OR:Staphylococcus aureus]


SPX0588
588
3249
250
750
165
1.10E-23
[LN:E69826]
117









[AC:E69826]









[PN:1-acylglycerol-3-phosphate O-acyltransfera homolog yhdO]









[GN:yhdO]









[OR:Bacillus subtilis]


SPX0589
589
3250
779
2337
414
1.80E-126
“[LN:CTPE_MYCTU]
160









[AC:O08365]









[GN:CTPE:RV0908:MTCY21C12.02]









[OR:Mycobacterium tuberculosis]









[EC:3.6.1.-]









[DE:PROBABLE CATION-TRANSPORTING ATPASE E,]









[SP:O08365]”


SPX0590
590
3251
77
231


NO-HIT
6


SPX0591
591
3252
488
1464
122
9.60E-23
[GI:1480429]
88









[LN:BSU18943]









[AC:U18943:X99465]









[GN:MtlR]









[OR:Bacillus stearothermophilus]


SPX0592
592
3253
143
429
60
0.00018
[GI:2317740]
108









[LN:AF013987]









[AC:AF013987]









[PN:nitrogen regulatory IIA protein]









[GN:ptsN]









[OR:Vibrio cholerae]


SPX0593
593
3254
151
453
223
5.60E-24
“[LN:HRSA_ECOLI]
106









[AC:P54745]









[GN:HRSA]









[OR:Escherichia coli]









[EC:2.7.1.69]









[DE:HRSA PROTEIN,]









[SP:P54745]”


SPX0594
594
3255
104
312
236
1.30E-27
“[LN:PTWB_ECOLI]
110









[AC:P32673]









[GN:FRWB]









[OR:Escherichia coli]









[EC:2.7.1.69]









[DE:II, B COMPONENT),]









[SP:P32673]”


SPX0595
595
3256
369
1107
398
8.00E-60
“[LN:PTFB_XANCP]
141









[AC:P23355]









[GN:FRUA]









[OR:Xanthomonas campestris]









[SR:,pvcampestris]









[EC:2.7.1.69]









[DE:(EC 2.7.1.69) (EII-FRU)]









[SP:P23355]”


SPX0596
596
3257
232
696
560
6.50E-74
“[LN:ALSE_ECOLI]
127









[AC:P32719]









[GN:ALSE]









[OR:Escherichia coli]









[EC:5.1.3.-]









[DE:D-ALLULOSE-6-PHOSPHATE 3-EPIMERASE,]









[SP:P32719]”


SPX0597
597
3258
657
1971
1371
2.00E-292
“[LN:TKT_STRPN]
127









[AC:P22976]









[GN:RECP]









[OR:Streptococcus pneumoniae]









[EC:2.2.1.1]









[DE:PROBABLE TRANSKETOLASE, (TK)]









[SP:P22976]”


SPX0598
598
3259
191
573
422
2.30E-53
[LN:B30868]
81









[AC:B30868]









[PN:hypothetical protein 1]









[OR:Streptococcus agalactiae]


SPX0599
599
3260
191
573
422
2.30E-53
[LN:B30868]
81









[AC:B30868]









[PN:hypothetical protein 1]









[OR:Streptococcus agalactiae]


SPX0600
600
3261
278
834
587
1.60E-140
[LN:A33595]
107









[AC:A33595:A30868]









[PN:probable transposase]









[CL:transposase IS3]









[OR:Streptococcus agalactiae]


SPX0601
601
3262
177
531


NO-HIT
6


SPX0602
602
3263
139
417
138
1.40E-10
[LN:T35180]
160









[AC:T35180]









[PN:hypothetical protein SC5A7.31]









[GN:SC5A7.31]









[CL:Streptomyces coelicolor hypothetical protein SC5A7.31]









[OR:Streptomyces coelicolor]


SPX0603
603
3264
226
678
612
1.10E-79
[GI:1813343]
114









[LN:D78182]









[AC:D78182]









[GN:ORF3]









[OR:Streptococcus mutans]









[SR:Streptococcus mutans (strain:Xc) DNA]


SPX0604
604
3265
266
798
344
5.40E-120
[GI:1813344]
114









[LN:D78182]









[AC:D78182]









[GN:ORF4]









[OR:Streptococcus mutans]









[SR:Streptococcus mutans (strain:Xc) DNA]


SPX0605
605
3266
368
1104
335
4.50E-71
[LN:YURR_BACSU]
143









[AC:O32159]









[GN:YURR]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 39.4 KD OXIDOREDUCTASE IN HOM-MRGA INTERGENIC REGION]









[SP:O32159]


SPX0606
606
3267
64
192


NO-HIT
6


SPX0607
607
3268
340
1020
1167
7.10E-156
[LN:GALE_BACSU]
113









[AC:P55180]









[GN:GALE]









[OR:Bacillus subtilis]









[EC:5.1.3.2]









[DE:GALACTOSE 4-EPIMERASE)]









[SP:P55180]


SPX0608
608
3269
318
954
441
7.80E-87
[LN:CSBB_BACSU]
90









[AC:Q45539]









[GN:CSBB]









[OR:Bacillus subtilis]









[DE:CSBB PROTEIN]









[SP:Q45539]


SPX0609
609
3270
222
666


NO-HIT
6


SPX0610
610
3271
69
207
55
0.00029
“[LN:FER_MOOTH]
117









[AC:P00203]









[OR:Moorella thermoacetica]









[SR:,Clostridium thermoaceticum]









[DE:FERREDOXIN]









[SP:P00203]”


SPX0611
611
3272
159
477


NO-HIT
6


SPX0612
612
3273
224
672
413
6.00E-74
[LN:KCY_BACSU]
107









[AC:P38493]









[GN:CMK:JOFC]









[OR:Bacillus subtilis]









[EC:2.7.4.14]









[DE:(CMP KINASE)]









[SP:P38493]


SPX0613
613
3274
113
339
432
5.60E-55
[LN:PHNA_ECOLI]
89









[AC:P16680]









[GN:PHNA]









[OR:Escherichia coli]









[DE:PHNA PROTEIN]









[SP:P16680]


SPX0614
614
3275
210
630


NO-HIT
6


SPX0615
615
3276
76
228
192
3.60E-23
[GI:1914870]
81









[LN:SPZ82001]









[AC:Z82001]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX0616
616
3277
384
1152
68
6.80E-05
[LN:C81266]
108









[AC:C81266]









[PN:probable efflux protein Cj1687 [imported]]









[GN:Cj1687]









[OR:Campylobacter jejuni]


SPX0617
617
3278
250
750
309
4.30E-69
[LN:TRUA_BACSU]
141









[AC:P70973]









[GN:TRUA]









[OR:Bacillus subtilis]









[EC:4.2.1.70]









[DE:I) (PSEUDOURIDINE SYNTHASE I) (URACIL HYDROLYASE)]









[SP:P70973]


SPX0618
618
3279
258
774
155
3.70E-39
[LN:THID_BACSU]
113









[AC:P39610]









[GN:THID:IPA-52R]









[OR:Bacillus subtilis]









[EC:2.7.4.7]









[DE:(HMP-P KINASE)]









[SP:P39610]


SPX0619
619
3280
154
462
69
5.80E-12
[LN:G75153]
93









[AC:G75153]









[PN:hypothetical protein PAB2090]









[GN:PAB2090]









[OR:Pyrococcus abyssi]


SPX0620
620
3281
191
573
422
2.30E-53
[LN:B30868]
81









[AC:B30868]









[PN:hypothetical protein 1]









[OR:Streptococcus agalactiae]


SPX0621
621
3282
91
273
288
2.30E-35
[LN:A33595]
107









[AC:A33595:A30868]









[PN:probable transposase]









[CL:transposase IS3]









[OR:Streptococcus agalactiae]


SPX0622
622
3283
198
594
583
9.30E-95
[LN:A33595]
107









[AC:A33595:A30868]









[PN:probable transposase]









[CL:transposase IS3]









[OR:Streptococcus agalactiae]


SPX0623
623
3284
159
477


NO-HIT
6


SPX0624
624
3285
361
1083
1016
1.20E-136
[GI:2323341]
103









[LN:AF014460]









[AC:AF014460]









[PN:PepQ]









[FN:hydrolysis of Leu-Pro]









[OR:Streptococcus mutans]


SPX0625
625
3286
261
783
147
5.10E-36
[LN:T31439]
91









[AC:T31439]









[PN:probable cobyric acid synthase CobQ]









[OR:Heliobacillus mobilis]


SPX0626
626
3287
448
1344
137
1.30E-46
[LN:T31440]
110









[AC:T31440]









[PN:UDP-N-acetylmuramyl tripeptide synthetase homolog murC]









[OR:Heliobacillus mobilis]


SPX0627
627
3288
439
1317
797
4.80E-136
[LN:YKGC_ECOLI]
94









[AC:P77212]









[GN:YKGC]









[OR:Escherichia coli]









[DE:INTERGENIC REGION]









[SP:P77212]


SPX0628
628
3289
291
873
711
3.70E-137
[GI:7107009]
96









[LN:AF168363]









[AC:AF168363]









[PN:oxalate:formate antiporter]









[OR:Lactococcus lactis]


SPX0629
629
3290
82
246
193
5.00E-21
[GI:7107009]
96









[LN:AF168363]









[AC:AF168363]









[PN:oxalate:formate antiporter]









[OR:Lactococcus lactis]


SPX0630
630
3291
525
1575
1329
1.80E-184
[GI:4409804]
116









[LN:AF091502]









[AC:AF091502]









[PN:autoaggregation-mediating protein]









[GN:aggH]









[OR:Lactobacillus reuteri]


SPX0631
631
3292
263
789
547
3.10E-74
[LN:CODY_BACSU]
126









[AC:P39779]









[GN:CODY]









[OR:Bacillus subtilis]









[DE:CODY PROTEIN (VEGETATIVE PROTEIN 286B) (VEG286B)]









[SP:P39779]


SPX0632
632
3293
69
207
174
1.30E-18
[LN:C70008]
136









[AC:C70008]









[PN:pyrazinamidase/nicotinamidase homolog yueJ]









[GN:yueJ]









[CL:hypothetical protein b1011]









[OR:Bacillus subtilis]


SPX0633
633
3294
152
456
253
1.50E-30
[LN:C70008]
136









[AC:C70008]









[PN:pyrazinamidase/nicotinamidase homolog yueJ]









[GN:yueJ]









[CL:hypothetical protein b1011]









[OR:Bacillus subtilis]


SPX0634
634
3295
78
234
328
1.70E-40
[GI:600072]
96









[LN:SEDEXB]









[AC:X72832]









[PN:ABC transporter]









[GN:abc]









[OR:Streptococcus equisimilis]


SPX0635
635
3296
52
156
113
2.50E-10
[LN:E72756]
92









[AC:E72756]









[PN:hypothetical protein APE0042]









[GN:APE0042]









[OR:Aeropyrum pernix]


SPX0636
636
3297
285
855
731
1.70E-136
[LN:MSMK_STRMU]
138









[AC:Q00752]









[GN:MSMK]









[OR:Streptococcus mutans]









[DE:MULTIPLE SUGAR-BINDING TRANSPORT ATP-BINDING PROTEIN MSMK]









[SP:Q00752]


SPX0637
637
3298
253
759
485
3.90E-95
[LN:Y095_HAEIN]
126









[AC:Q57060:O05007]









[GN:HI0095]









[OR:Haemophilus influenzae]









[DE:HYPOTHETICAL PROTEIN HI0095]









[SP:Q57060:O05007]


SPX0638
638
3299
177
531
603
2.90E-79
“[LN:B69587]
194









[AC:B69587]









[PN:adenine phosphoribosyltransferase,:AMP pyrophosphorylase:transphosphoribosidase]









[GN:apt]









[CL:adenine phosphoribosyltransferase]









[OR:Bacillus subtilis]









[EC:2.4.2.7]”


SPX0639
639
3300
315
945
567
6.90E-116
[LN:C72324]
134









[AC:C72324]









[PN:homoserine O-succinyltransferase]









[GN:TM0881]









[CL:homoserine succinyltransferase]









[OR:Thermotoga maritima]


SPX0640
640
3301
226
678
357
5.50E-90
[GI:1813342]
114









[LN:D78182]









[AC:D78182]









[GN:ORF2]









[OR:Streptococcus mutans]









[SR:Streptococcus mutans (strain:Xc) DNA]


SPX0641
641
3302
125
375


NO-HIT
6


SPX0642
642
3303
253
759
864
1.30E-113
“[LN:TPIS_LACDE]
159









[AC:O32757]









[GN:TPIA:TPI]









[OR:Lactobacillus delbrueckii]









[SR:,subspbulgaricus]









[EC:5.3.1.1]









[DE:TRIOSEPHOSPHATE ISOMERASE, (TIM)]









[SP:O32757]”


SPX0643
643
3304
502
1506
2728
0
“[GI:4218526]
153









[LN:SPAJ9639]









[AC:AJ009639]









[PN:1,4-beta-N-acetylmuramidase]









[GN:lytC]









[FN:lysis of cell wall peptidoglycan]









[OR:Streptococcus pneumoniae]”


SPX0644
644
3305
173
519
800
2.60E-105
[GI:3513547]
83









[LN:AF055720]









[AC:AF055720]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX0645
645
3306
213
639


NO-HIT
6


SPX0646
646
3307
169
507
882
2.00E-118
[GI:2196662]
135









[LN:HSZ84379]









[AC:Z84379]









[PN:dihydrofolate reductase]









[GN:dfr]









[FN:trimethoprim resistance]









[OR:Streptococcus pneumoniae]


SPX0647
647
3308
69
207


NO-HIT
6


SPX0648
648
3309
411
1233
1251
4.80E-206
[GI:7546983]
93









[LN:AF236863]









[AC:AF236863]









[PN:protease ClpX]









[GN:clpX]









[OR:Lactococcus lactis]


SPX0649
649
3310
196
588
807
9.70E-107
[GI:7546984]
102









[LN:AF236863]









[AC:AF236863]









[PN:hypothetical GTP-binding protein]









[OR:Lactococcus lactis]


SPX0650
650
3311
127
381
392
2.30E-49
“[LN:ALDR_LACLA]
143









[AC:O34133]









[GN:ALDR]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[DE:PUTATIVE REGULATOR ALDR]









[SP:O34133]”


SPX0651
651
3312
297
891
337
2.00E-91
[GI:7328270]
91









[LN:SAY14324]









[AC:Y14324]









[PN:hypothetical protein]









[OR:Staphylococcus aureus]


SPX0652
652
3313
326
978
268
1.30E-62
[LN:YVCK_BACSU]
136









[AC:O06974]









[GN:YVCK]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 34.7 KD PROTEIN IN CRH-TRXB INTERGENIC REGION]









[SP:O06974]


SPX0653
653
3314
304
912
424
5.50E-81
[GI:7328272]
65









[LN:SAY14324]









[AC:Y14324]









[OR:Staphylococcus aureus]


SPX0654
654
3315
323
969
422
5.00E-99
[LN:B70015]
154









[AC:B70015]









[PN:thioredoxin reductase homolog yumC]









[GN:yumC]









[CL:thioredoxin reductase:thioredoxin reductase homology]









[OR:Bacillus subtilis]


SPX0655
655
3316
272
816
419
8.50E-81
[LN:H69744]
128









[AC:H69744]









[PN:conserved hypothetical protein ybbP]









[GN:ybbP]









[CL:hypothetical protein ybbP]









[OR:Bacillus subtilis]


SPX0656
656
3317
260
780
104
2.70E-10
[LN:A69745]
87









[AC:A69745]









[PN:hypothetical protein ybbR]









[GN:ybbR]









[OR:Bacillus subtilis]


SPX0657
657
3318
64
192


NO-HIT
6


SPX0658
658
3319
451
1353
655
2.00E-180
[GI:3892895]
107









[LN:SAARGFEMD]









[AC:Y15477]









[PN:phosphoglucosamine-mutase]









[GN:glmM]









[OR:Staphylococcus aureus]


SPX0659
659
3320
121
363


NO-HIT
6


SPX0660
660
3321
283
849
239
6.50E-25
[LN:DEGV_BACSU]
90









[AC:P32436]









[GN:DEGV]









[OR:Bacillus subtilis]









[DE:DEGV PROTEIN]









[SP:P32436]


SPX0661
661
3322
256
768
614
6.50E-89
“[LN:DAPB_BACSU]
124









[AC:P42976]









[GN:DAPB]









[OR:Bacillus subtilis]









[EC:1.3.1.26]









[DE:DIHYDRODIPICOLINATE REDUCTASE,]









[SP:P42976]”


SPX0662
662
3323
400
1200
601
8.40E-92
“[LN:PAPS_BACSU]
119









[AC:P42977]









[GN:PAPS]









[OR:Bacillus subtilis]









[EC:2.7.7.19]









[DE:POLY(A) POLYMERASE, (PAP)]









[SP:P42977]”


SPX0663
663
3324
624
1872
669
1.80E-162
[LN:A69814]
188









[AC:A69814]









[PN:ABC transporter (ATP-binding protein) homolog yfmR]









[GN:yfmR]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Bacillus subtilis]


SPX0664
664
3325
144
432


NO-HIT
6


SPX0665
665
3326
394
1182
629
1.90E-82
[LN:YEAB_BACSU]
158









[AC:P46348:O05001]









[GN:YEAB]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 31.8 KD PROTEIN IN GABP-GUAA INTERGENIC REGION (ORFX)]









[SP:P46348:O05001]


SPX0666
666
3327
899
2697
601
1.20E-189
“[LN:S77052]
218









[AC:S77052]









[PN:cation-transporting ATPase, pacL-1:protein sll0672:protein sll0672]









[GN:pacL-1]









[CL:Na+/K+-transporting ATPase alpha chain:ATPase nucleotide-binding domain homology]









[OR:Synechocystis sp.]”


SPX0667
667
3328
97
291


NO-HIT
6


SPX0668
668
3329
83
249
73
0.00016
[LN:H72624]
92









[AC:H72624]









[PN:hypothetical protein APE1456]









[GN:APE1456]









[OR:Aeropyrum pernix]


SPX0669
669
3330
264
792
713
2.30E-105
[LN:YGHU_ECOLI]
135









[AC:Q46845]









[GN:YGHU]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 34.2 KD PROTEIN IN GSP-HYBG INTERGENIC REGION]









[SP:Q46845]


SPX0670
670
3331
152
456
368
3.30E-46
“[LN:DEF_CLOBE]
136









[AC:O08450]









[GN:DEF:FMS]









[OR:Clostridium beijerinckii]









[SR:,Clostridium MP]









[EC:3.5.1.31]









[DE:DEFORMYLASE)]









[SP:O08450]”


SPX0671
671
3332
532
1596


NO-HIT
6


SPX0672
672
3333
60
180


NO-HIT
6


SPX0673
673
3334
243
729
473
1.20E-60
[GI:4580623]
77









[LN:AF118389]









[AC:AF118389]









[PN:unknown]









[OR:Streptococcus suis]


SPX0674
674
3335
210
630
111
2.10E-12
[GI:6562870]
116









[LN:SCM1]









[AC:AL133422]









[PN:putative secreted protein.]









[GN:SCM1.21]









[OR:Streptomyces coelicolor A3(2)]


SPX0675
675
3336
163
489
68
0.00021
[LN:YPMB_BACSU]
137









[AC:P54396]









[GN:YPMB]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 17.9 KD PROTEIN IN DING-ASPB INTERGENIC REGION]









[SP:P54396]


SPX0676
676
3337
396
1188
1400
2.80E-187
[GI:6465901]
106









[LN:AF035157]









[AC:AF035157]









[PN:aspartate aminotransferase]









[GN:aspC]









[OR:Lactococcus lactis]


SPX0677
677
3338
124
372
178
1.90E-27
[LN:T03486]
87









[AC:T03486]









[PN:conserved hypothetical protein]









[OR:Rhodobacter capsulatus]


SPX0678
678
3339
448
1344
703
1.60E-180
[LN:SYN_BACSU]
98









[AC:P39772]









[GN:ASNS]









[OR:Bacillus subtilis]









[EC:6.1.1.22]









[DE:(ASNRS)]









[SP:P39772]


SPX0679
679
3340
129
387


NO-HIT
6


SPX0680
680
3341
97
291
236
7.30E-39
[LN:RS6_BACSU]
107









[AC:P21468]









[GN:RPSF]









[OR:Bacillus subtilis]









[DE:30S RIBOSOMAL PROTEIN S6 (BS9)]









[SP:P21468]


SPX0681
681
3342
157
471
481
5.20E-71
[GI:6716352]
136









[LN:AF145054]









[AC:AF145054:AF001793:AF118440:U89246]









[PN:ORF9]









[GN:orf9]









[OR:Streptococcus thermophilus bacteriophage 7201]


SPX0682
682
3343
87
261
134
1.30E-13
[LN:RS18_BACST]
120









[AC:P10806]









[GN:RPSR]









[OR:Bacillus stearothermophilus]









[DE:30S RIBOSOMAL PROTEIN S18 (BS21)]









[SP:P10806]


SPX0683
683
3344
112
336


NO-HIT
6


SPX0684
684
3345
467
1401
270
7.50E-47
[GI:4678225]
137









[LN:AC007135]









[AC:AC007135:AE002093]









[PN:cyclophilin-like protein]









[GN:At2g36130]









[OR:Arabidopsis thaliana]









[SR:thale cress]


SPX0685
685
3346
84
252
172
6.10E-19
[LN:YABR_BACSU]
140









[AC:P37560]









[GN:YABR]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 14.2 KD PROTEIN IN DIVIC-SPOIIE INTERGENIC REGION]









[SP:P37560]


SPX0686
686
3347
87
261
96
1.40E-15
[LN:YABB_BACSU]
137









[AC:P37543]









[GN:YABB]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 28.3 KD PROTEIN IN XPAC-ABRB INTERGENIC REGION]









[SP:P37543]


SPX0687
687
3348
67
201
109
3.00E-09
[LN:YABB_BACSU]
137









[AC:P37543]









[GN:YABB]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 28.3 KD PROTEIN IN XPAC-ABRB INTERGENIC REGION]









[SP:P37543]


SPX0688
688
3349
129
387
267
1.40E-39
[LN:YABB_BACSU]
137









[AC:P37543]









[GN:YABB]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 28.3 KD PROTEIN IN XPAC-ABRB INTERGENIC REGION]









[SP:P37543]


SPX0689
689
3350
93
279
224
1.50E-26
[LN:A69742]
127









[AC:A69742]









[PN:conserved hypothetical protein yazA]









[GN:yazA]









[CL:hypothetical protein 312]









[OR:Bacillus subtilis]


SPX0690
690
3351
60
180
143
5.60E-14
[GI:1743856]
115









[LN:SGU57759]









[AC:U57759]









[PN:intrageneric coaggregation-relevant adhesin]









[OR:Streptococcus gordonii]


SPX0691
691
3352
222
666
955
2.60E-126
[GI:1743856]
115









[LN:SGU57759]









[AC:U57759]









[PN:intrageneric coaggregation-relevant adhesin]









[OR:Streptococcus gordonii]


SPX0692
692
3353
171
513


NO-HIT
6


SPX0693
693
3354
105
315
140
1.80E-21
[GI:2952534]
79









[LN:AF051356]









[AC:AF051356]









[PN:unknown]









[OR:Streptococcus mutans]


SPX0694
694
3355
95
285


NO-HIT
6


SPX0695
695
3356
65
195
74
0.00038
[GI:2772940]
116









[LN:AF034574]









[AC:AF034574]









[PN:putative cruciform DNA binding protein]









[GN:Gv1]









[OR:Glomus versiforme]


SPX0696
696
3357
504
1512
172
1.50E-35
[LN:MURE_BACSU]
122









[AC:Q03523]









[GN:MURE]









[OR:Bacillus subtilis]









[EC:6.3.2.13]









[DE:DIAMINOPIMELATE-ADDING ENZYME)]









[SP:Q03523]


SPX0697
697
3358
192
576
172
9.40E-16
[LN:MURE_BACSU]
122









[AC:Q03523]









[GN:MURE]









[OR:Bacillus subtilis]









[EC:6.3.2.13]









[DE:DIAMINOPIMELATE-ADDING ENZYME)]









[SP:Q03523]


SPX0698
698
3359
541
1623
187
2.90E-75
[LN:G69992]
95









[AC:G69992]









[PN:spore cortex protein homolog ytgP]









[GN:ytgP]









[OR:Bacillus subtilis]


SPX0699
699
3360
653
1959
3335
0
[LN:ALIB_STRPN]
128









[AC:Q51933]









[GN:ALIB]









[OR:Streptococcus pneumoniae]









[DE:OLIGOPEPTIDE-BINDING PROTEIN ALIB PRECURSOR]









[SP:Q51933]


SPX0700
700
3361
185
555
282
2.00E-38
[GI:1125685]
104









[LN:SADNAS55]









[AC:X87104]









[GN:mdr]









[FN:multiple grug resistance]









[OR:Staphylococcus aureus]


SPX0701
701
3362
180
540
179
9.60E-18
[LN:S58356]
166









[AC:S66651:S58356]









[PN:pepT protein]









[GN:pepT]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Staphylococcus epidermidis]


SPX0702
702
3363
182
546
444
4.80E-55
[GI:1262136]
116









[LN:SAPBP4GEN]









[AC:X91786]









[PN:ATP-binding cassette transporter A]









[GN:abcA]









[OR:Staphylococcus aureus]


SPX0703
703
3364
365
1095
681
2.80E-123
[LN:A69847]
143









[AC:A69847]









[PN:cystathionine gamma-synthase homolog yjcI]









[GN:yjcI]









[CL:O-succinylhomoserine (thiol)-lyase]









[OR:Bacillus subtilis]


SPX0704
704
3365
389
1167
582
1.60E-99
“[LN:PATB_BACSU]
121









[AC:Q08432]









[GN:PATB]









[OR:Bacillus subtilis]









[EC:2.6.1.-]









[DE:PUTATIVE AMINOTRANSFERASE B,]









[SP:Q08432]”


SPX0705
705
3366
1033
3099
552
1.00E-129
[GI:1769947]
68









[LN:BCX98455]









[AC:X98455]









[GN:SNF]









[OR:Bacillus cereus]


SPX0706
706
3367
206
618


NO-HIT
6


SPX0707
707
3368
445
1335
491
2.00E-154
[LN:MURC_BACSU]
127









[AC:P40778]









[GN:MURC]









[OR:Bacillus subtilis]









[EC:6.3.2.8]









[DE:ACETYLMURANOYL-L-ALANINE SYNTHETASE)]









[SP:P40778]


SPX0708
708
3369
155
465


NO-HIT
6


SPX0709
709
3370
119
357
56
7.70E-05
“[LN:A64491]
192









[AC:A64491]









[PN:N-terminal acetyltransferase complex, subunit ARD1 homolog]









[CL:Escherichia coli ribosomal-protein-alanine N-acetyltransferase rimI]









[OR:Methanococcus jannaschii]”


SPX0710
710
3371
71
213


NO-HIT
6


SPX0711
711
3372
502
1506
185
2.10E-43
[LN:E69979]
110









[AC:E69979]









[PN:folate metabolism homolog yrrL]









[GN:yrrL]









[CL:yceG protein]









[OR:Bacillus subtilis]


SPX0712
712
3373
161
483
271
3.60E-55
[LN:GREA_BACSU]
121









[AC:P80240]









[GN:GREA]









[OR:Bacillus subtilis]









[DE:GREA) (GENERAL STRESS PROTEIN 20M) (GSP20M)]









[SP:P80240]


SPX0713
713
3374
61
183
121
2.50E-12
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX0714
714
3375
163
489
152
1.50E-24
[LN:S31638]
77









[AC:S31638]









[PN:hypothetical protein]









[OR:Lactobacillus curvatus]


SPX0715
715
3376
66
198


NO-HIT
6


SPX0716
716
3377
70
210
89
0.0001
[GI:4966270]
81









[LN:CELK09H11]









[AC:U97002]









[GN:K09H11.1]









[OR:Caenorhabditis elegans]


SPX0717
717
3378
148
444
419
7.50E-56
[GI:517210]
65









[LN:SPU11799]









[AC:U11799]









[OR:Streptococcus pyogenes]


SPX0718
718
3379
164
492
484
1.40E-63
[GI:517210]
65









[LN:SPU11799]









[AC:U11799]









[OR:Streptococcus pyogenes]


SPX0719
719
3380
67
201
331
3.00E-44
“[LN:S49404]
185









[AC:S49404:S38206]









[PN:H+-transporting ATP synthase, chain c]









[GN:atpC]









[CL:H+-transporting ATP synthase lipid-binding protein]









[OR:Streptococcus pneumoniae]









[EC:3.6.1.34]”


SPX0720
720
3381
239
717
1205
5.00E-168
“[LN:ATP6_STRPN]
139









[AC:Q59954]









[GN:ATPB:ATPA]









[OR:Streptococcus pneumoniae]









[EC:3.6.1.34]









[DE:ATP SYNTHASE A CHAIN, (PROTEIN 6)]









[SP:Q59954]”


SPX0721
721
3382
165
495
769
2.90E-100
“[LN:ATPF_STRPN]
153









[AC:Q59952:Q59955]









[GN:ATPF:ATPB]









[OR:Streptococcus pneumoniae]









[EC:3.6.1.34]









[DE:ATP SYNTHASE B CHAIN, (SUBUNIT I)]









[SP:Q59952:Q59955]”


SPX0722
722
3383
179
537
509
8.40E-66
[GI:4100654]
126









[LN:AF001955]









[AC:AF001955]









[PN:proton-translocating ATPase delta subunit]









[GN:uncH]









[OR:Streptococcus sanguinis]


SPX0723
723
3384
502
1506
2347
0
[GI:4100655]
126









[LN:AF001955]









[AC:AF001955]









[PN:proton-translocating ATPase alpha subunit]









[GN:uncA]









[OR:Streptococcus sanguinis]


SPX0724
724
3385
293
879
1011
1.70E-169
[GI:4100656]
116









[LN:AF001955]









[AC:AF001955]









[PN:proton-translocating ATPase gamma subunit]









[OR:Streptococcus sanguinis]


SPX0725
725
3386
469
1407
2287
0
[GI:4100657]
125









[LN:AF001955]









[AC:AF001955]









[PN:proton-translocating ATPase beta subunit]









[GN:uncD]









[OR:Streptococcus sanguinis]


SPX0726
726
3387
140
420
581
1.40E-76
[GI:4100658]
128









[LN:AF001955]









[AC:AF001955]









[PN:proton-translocating ATPase epsilon subunit]









[GN:uncC]









[OR:Streptococcus sanguinis]


SPX0727
727
3388
251
753
175
2.70E-42
[GI:6746427]
90









[LN:AF179847]









[AC:AF179847]









[PN:putative transposase]









[OR:Lactococcus lactis]


SPX0728
728
3389
65
195


NO-HIT
6


SPX0729
729
3390
182
546
107
1.20E-15
[GI:3849798]
118









[LN:U91581]









[AC:U91581:U04057]









[PN:putative transposase]









[GN:tpase]









[OR:Lactococcus lactis subsp. lactis]


SPX0730
730
3391
338
1014
444
1.50E-117
[GI:3242228]
73









[LN:LLCADHE]









[AC:AJ001007]









[GN:orfB]









[OR:Lactococcus lactis]


SPX0731
731
3392
78
234


NO-HIT
6


SPX0732
732
3393
389
1167
1141
1.60E-158
[GI:4098497]
95









[LN:SMU78604]









[AC:U78604]









[PN:putative membrane protein]









[OR:Streptococcus mutans]


SPX0733
733
3394
410
1230
457
6.20E-71
“[GI:473901]
128









[LN:LACALS]









[AC:L16975]









[OR:Lactococcus lactis]









[SR:Lactococcus lactis (strain DSM 20384, sub_species lactis) DNA]”


SPX0734
734
3395
214
642
351
1.70E-45
“[LN:A72357]
146









[AC:A72357]









[PN:amino acid ABC transporter, permease protein]









[GN:TM0592]









[CL:histidine permease protein M]









[OR:Thermotoga maritima]”


SPX0735
735
3396
210
630
367
2.90E-65
[GI:1649037]
116









[LN:STU73111]









[AC:U73111]









[PN:glutamine transport ATP-binding protein GLNQ]









[OR:Salmonella typhimurium]


SPX0736
736
3397
279
837
1411
4.70E-188
[GI:5929889]
90









[LN:AF165218]









[AC:AF165218]









[PN:AatB]









[GN:aatB]









[OR:Streptococcus pneumoniae]


SPX0737
737
3398
116
348
578
1.80E-76
[GI:5929888]
88









[LN:AF165218]









[AC:AF165218]









[PN:Bta]









[GN:bta]









[OR:Streptococcus pneumoniae]


SPX0738
738
3399
573
1719
2903
0
[GI:5929887]
88









[LN:AF165218]









[AC:AF165218]









[PN:Pgm]









[GN:pgm]









[OR:Streptococcus pneumoniae]


SPX0739
739
3400
109
327
129
8.30E-12
[GI:4200438]
96









[LN:AF026471]









[AC:AF026471]









[PN:putative transposase]









[OR:Streptococcus pneumoniae]


SPX0740
740
3401
100
300
245
5.10E-30
[GI:5019553]
97









[LN:SPN239004]









[AC:AJ239004]









[PN:putative transposase]









[OR:Streptococcus pneumoniae]


SPX0741
741
3402
95
285


NO-HIT
6


SPX0742
742
3403
85
255


NO-HIT
6


SPX0743
743
3404
71
213


NO-HIT
6


SPX0744
744
3405
371
1113


NO-HIT
6


SPX0745
745
3406
174
522
72
1.10E-05
“[LN:I38170]
87









[AC:I38170]









[PN:gene hr44 protein]









[GN:hr44]









[OR:Homo sapiens]









[SR:, man]”


SPX0746
746
3407
290
870
335
2.40E-72
[LN:B72254]
135









[AC:B72254]









[PN:glycerol uptake facilitator protein]









[GN:TM1429]









[CL:glycerol facilitator protein]









[OR:Thermotoga maritima]


SPX0747
747
3408
399
1197
2022
6.40E-273
[LN:EFTU_STROR]
108









[AC:P33170]









[GN:TUF]









[OR:Streptococcus oralis]









[DE:ELONGATION FACTOR TU (EF-TU)]









[SP:P33170]


SPX0748
748
3409
128
384
104
1.80E-06
[LN:H71023]
95









[AC:H71023]









[PN:hypothetical protein PH1485]









[GN:PH1485]









[OR:Pyrococcus horikoshii]


SPX0749
749
3410
138
414
99
6.40E-06
[LN:S31840]
82









[AC:S31840]









[PN:probable transposase]









[OR:Bacillus stearothermophilus]


SPX0750
750
3411
62
186


NO-HIT
6


SPX0751
751
3412
218
654
163
3.90E-21
[GI:722339]
100









[LN:AXU22323]









[AC:U22323]









[PN:unknown]









[OR:Acetobacter xylinus]









[SR:Acetobacter xylinum]


SPX0752
752
3413
361
1083
272
2.20E-72
[LN:C69813]
153









[AC:C69813]









[PN:RNA helicase homolog yfmL]









[GN:yfmL]









[CL:unassigned DEAD/H box helicases:DEAD/H box helicase homology]









[OR:Bacillus subtilis]


SPX0753
753
3414
354
1062
197
3.10E-44
[LN:YGJR_ECOLI]
164









[AC:P42599:P42600:P76661]









[GN:YGJR]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 36.2 KD PROTEIN IN EBGC-UXAA INTERGENIC REGION]









[SP:P42599:P42600:P76661]


SPX0754
754
3415
62
186
77
0.00028
“[LN:S67482]
152









[AC:S67482:S52150]









[PN:serine O-acetyltransferase,, cytosolic:serine acetyltransferase:serine acetyltransferase]









[OR:Arabidopsis thaliana]”


SPX0755
755
3416
126
378


NO-HIT
6


SPX0756
756
3417
481
1443
485
5.60E-59
“[LN:G69849]
118









[AC:G69849]









[PN:endo-1,4-beta-xylanase homolog yjeA]









[GN:yjeA]









[CL:nodB homology]









[OR:Bacillus subtilis]”


SPX0757
757
3418
256
768
357
5.70E-83
[LN:C70040]
129









[AC:C70040]









[PN:plant-metabolite dehydrogenase homolog yvgN]









[GN:yvgN]









[CL:aldehyde reductase]









[OR:Bacillus subtilis]


SPX0758
758
3419
77
231


NO-HIT
6


SPX0759
759
3420
254
762


NO-HIT
6


SPX0760
760
3421
306
918
1187
3.50E-159
[LN:SYGA_BACSU]
112









[AC:P54380]









[GN:GLYQ]









[OR:Bacillus subtilis]









[EC:6.1.1.14]









[DE:ALPHA CHAIN) (GLYRS)]









[SP:P54380]


SPX0761
761
3422
679
2037
1334
6.50E-179
[LN:SYGB_BACSU]
111









[AC:P54381]









[GN:GLYS]









[OR:Bacillus subtilis]









[EC:6.1.1.14]









[DE:BETA CHAIN) (GLYRS)]









[SP:P54381]


SPX0762
762
3423
86
258
218
1.20E-24
[LN:E69894]
87









[AC:E69894]









[PN:hypothetical protein ynzC]









[GN:ynzC]









[OR:Bacillus subtilis]


SPX0763
763
3424
415
1245
97
5.10E-08
[LN:YIEF_ECOLI]
136









[AC:P31465]









[GN:YIEF]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 20.4 KD PROTEIN IN TNAB-BGLB INTERGENIC REGION]









[SP:P31465]


SPX0764
764
3425
79
237


NO-HIT
6


SPX0765
765
3426
202
606
110
2.80E-13
[LN:YIEF_ECOLI]
136









[AC:P31465]









[GN:YIEF]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 20.4 KD PROTEIN IN TNAB-BGLB INTERGENIC REGION]









[SP:P31465]


SPX0766
766
3427
308
924
172
3.10E-41
[LN:APBE_TREPA]
134









[AC:O83774]









[GN:APBE:TP0796]









[OR:Treponema pallidum]









[DE:THIAMINE BIOSYNTHESIS LIPOPROTEIN APBE PRECURSOR]









[SP:O83774]


SPX0767
767
3428
91
273


NO-HIT
6


SPX0768
768
3429
460
1380
2342
0
[GI:4416519]
88









[LN:AF014458]









[AC:AF014458]









[PN:NADH oxidase]









[OR:Streptococcus pneumoniae]


SPX0769
769
3430
298
894
1411
3.40E-191
[LN:YG47_HAEIN]
112









[AC:P45293]









[GN:HI1647]









[OR:Haemophilus influenzae]









[DE:HYPOTHETICAL PROTEIN HI1647]









[SP:P45293]


SPX0770
770
3431
78
234
125
3.00E-12
[LN:F71007]
150









[AC:F71007]









[PN:hypothetical protein PH1356]









[GN:PH1356]









[CL:Pyrococcus horikoshii hypothetical protein PH1356]









[OR:Pyrococcus horikoshii]


SPX0771
771
3432
63
189
157
1.20E-15
[LN:F72782]
92









[AC:F72782]









[PN:hypothetical protein APE0247]









[GN:APE0247]









[OR:Aeropyrum pernix]


SPX0772
772
3433
52
156
159
4.30E-16
[LN:F72782]
92









[AC:F72782]









[PN:hypothetical protein APE0247]









[GN:APE0247]









[OR:Aeropyrum pernix]


SPX0773
773
3434
194
582
720
2.40E-95
[LN:YG48_HAEIN]
112









[AC:P45294]









[GN:HI1648]









[OR:Haemophilus influenzae]









[DE:HYPOTHETICAL PROTEIN HI1648]









[SP:P45294]


SPX0774
774
3435
216
648
183
5.00E-34
[LN:YA37_TREPA]
108









[AC:O84000]









[GN:TP1037]









[OR:Treponema pallidum]









[DE:HYPOTHETICAL PROTEIN TP1037]









[SP:O84000]


SPX0775
775
3436
151
453


NO-HIT
6


SPX0776
776
3437
165
495
94
2.80E-12
[LN:G81269]
111









[AC:G81269]









[PN:probable acetyltransferase Cj1715 [imported]]









[GN:Cj1715]









[OR:Campylobacter jejuni]


SPX0777
777
3438
177
531
167
1.80E-29
[GI:3694956]
119









[LN:AF091508]









[AC:AF091508]









[PN:O-6-methylguanine DNA methyltransferase]









[GN:ogt]









[OR:Salmonella muenster]


SPX0778
778
3439
119
357
272
2.10E-32
[LN:B70021]
124









[AC:B70021]









[PN:arsenate reductase homolog yusI]









[GN:yusI]









[CL:hypothetical protein yjbD]









[OR:Bacillus subtilis]


SPX0779
779
3440
126
378


NO-HIT
6


SPX0780
780
3441
267
801
284
2.10E-54
[LN:YXEN_BACSU]
100









[AC:P54953]









[GN:YXEN:LP9F]









[OR:Bacillus subtilis]









[DE:INTERGENIC REGION]









[SP:P54953]


SPX0781
781
3442
248
744
468
5.80E-82
[GI:666983]
102









[LN:BSPAAT]









[AC:X77636]









[PN:putative ATP binding subunit]









[GN:ORF3]









[OR:Bacillus subtilis]


SPX0782
782
3443
79
237


NO-HIT
6


SPX0783
783
3444
74
222


NO-HIT
6


SPX0784
784
3445
266
798
542
4.60E-98
“[LN:TRXB_LISMO]
120









[AC:O32823]









[GN:TRXB]









[OR:Listeria monocytogenes]









[EC:1.6.4.5]









[DE:THIOREDOXIN REDUCTASE,]









[SP:O32823]”


SPX0785
785
3446
254
762
322
1.30E-58
“[LN:YACO_BACSU]
139









[AC:Q06753]









[GN:YACO]









[OR:Bacillus subtilis]









[EC:2.1.1.-]









[DE:HYPOTHETICAL TRNA/RRNA METHYLTRANSFERASE YACO,]









[SP:Q06753]”


SPX0786
786
3447
204
612
394
4.10E-93
“[GI:806487]
140









[LN:LACLPAGAP]









[AC:L36907]









[FN:unknown]









[OR:Lactococcus lactis]









[SR:Lactococcus lactis (individual_isolate LM0230, sub_specie]”


SPX0787
787
3448
84
252


NO-HIT
6


SPX0788
788
3449
161
483
136
6.00E-14
[LN:H70069]
116









[AC:H70069:JC7099]









[PN:poly-gamma-glutamic synthesis PgsA protein]









[GN:ywtB:pgsA]









[OR:Bacillus subtilis]


SPX0789
789
3450
126
378


NO-HIT
6


SPX0790
790
3451
276
828
242
8.80E-42
[LN:F64819]
158









[AC:F64819]









[PN:hypothetical protein b0822]









[CL:Methanobacterium thermoautotrophicum conserved hypothetical protein MTH1071]









[OR:Escherichia coli]


SPX0791
791
3452
212
636


NO-HIT
6


SPX0792
792
3453
242
726
1196
1.80E-160
[GI:5001711]
109









[LN:AF112358]









[AC:AF112358]









[PN:C3-degrading proteinase]









[GN:cppA]









[OR:Streptococcus pneumoniae]


SPX0793
793
3454
312
936
117
4.00E-22
[GI:6469268]
121









[LN:SCC75A]









[AC:AL133220]









[PN:possible secreted esterase]









[GN:SCC75A.29c]









[OR:Streptomyces coelicolor A3(2)]


SPX0794
794
3455
299
897
487
1.00E-64
[LN:YICL_ECOLI]
136









[AC:P31437]









[GN:YICL]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 33.1 KD PROTEIN IN SELC-NLPA INTERGENIC REGION]









[SP:P31437]


SPX0795
795
3456
233
699
294
7.80E-49
[LN:D70044]
144









[AC:D70044]









[PN:transcription regulator GntR family homolog yvoA]









[GN:yvoA]









[CL:transcription regulator GntR]









[OR:Bacillus subtilis]


SPX0796
796
3457
521
1563
1721
3.40E-294
[GI:4321715]
92









[LN:AF058326]









[AC:AF058326]









[PN:GMP synthase]









[GN:guaA]









[OR:Lactococcus lactis]


SPX0797
797
3458
62
186


NO-HIT
6


SPX0798
798
3459
96
288
204
2.90E-23
“[LN:JC1151]
89









[AC:JC1151]









[PN:hypothetical protein, 20.3K]









[OR:Agrobacterium tumefaciens]”


SPX0799
799
3460
65
195


NO-HIT
6


SPX0800
800
3461
130
390
91
0.00062
“[GI:5824139]
137









[LN:POL245436]









[AC:AJ245436:J04618:J04619:S50571:X52935:X65936]









[PN:hypothetical protein, 57.8 kD]









[OR:Pseudomonas putida]”


SPX0801
801
3462
143
429
84
9.20E-08
“[GI:6009407]
140









[LN:AB024946]









[AC:AB024946]









[GN:orf31]









[OR:Escherichia coli]









[SR:Escherichia coli (sub_species:enteropathogenic, strain:B171]”


SPX0802
802
3463
150
450
94
3.20E-15
“[LN:Y4HP_RHISN]
128









[AC:P50360]









[GN:Y4HP]









[OR:Rhizobium sp]









[SR:,strain NGR234]









[DE:HYPOTHETICAL 61.7 KD PROTEIN Y4HP]









[SP:P50360]”


SPX0803
803
3464
78
234
87
0.00033
“[GI:5824139]
137









[LN:POL245436]









[AC:AJ245436:J04618:J04619:S50571:X52935:X65936]









[PN:hypothetical protein, 57.8 kD]









[OR:Pseudomonas putida]”


SPX0804
804
3465
455
1365
253
2.70E-62
“[LN:D69159]
217









[AC:D69159]









[PN:methyl coenzyme M reductase system, component A2 homolog]









[GN:MTH454]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Methanobacterium thermoautotrophicum]”


SPX0805
805
3466
74
222


NO-HIT
6


SPX0806
806
3467
232
696
88
1.90E-07
[LN:E72202]
96









[AC:E72202]









[PN:conserved hypothetical protein]









[GN:TM1868]









[OR:Thermotoga maritima]


SPX0807
807
3468
195
585


NO-HIT
6


SPX0808
808
3469
582
1746
554
3.00E-83
[GI:4097162]
81









[LN:PMU46488]









[AC:U46488]









[PN:NrpB]









[GN:nrpB]









[OR:Proteus mirabilis]


SPX0809
809
3470
587
1761
526
2.60E-78
[GI:4097161]
81









[LN:PMU46488]









[AC:U46488]









[PN:NrpA]









[GN:nrpA]









[OR:Proteus mirabilis]


SPX0810
810
3471
159
477
131
3.30E-12
[LN:SOXS_ECOLI]
100









[AC:P22539]









[GN:SOXS]









[OR:Escherichia coli]









[DE:REGULATORY PROTEIN SOXS]









[SP:P22539]


SPX0811
811
3472
69
207


NO-HIT
6


SPX0812
812
3473
397
1191
889
2.70E-126
[GI:2995646]
177









[LN:AF051092]









[AC:AF051092]









[PN:DNA modification methyltransferase M.XbaI]









[GN:xbaIM]









[FN:recognizes ds DNA sequence TCTAGA; thought to]









[OR:Xanthomonas campestris]


SPX0813
813
3474
63
189
128
1.30E-17
[GI:2995645]
169









[LN:AF051092]









[AC:AF051092]









[PN:restriction endonuclease R.XbaI]









[GN:xbaIR]









[FN:recognizes ds DNA sequence TCTAGA; cleaves both]









[OR:Xanthomonas campestris]


SPX0814
814
3475
61
183
199
4.80E-22
[GI:2995645]
169









[LN:AF051092]









[AC:AF051092]









[PN:restriction endonuclease R.XbaI]









[GN:xbaIR]









[FN:recognizes ds DNA sequence TCTAGA; cleaves both]









[OR:Xanthomonas campestris]


SPX0815
815
3476
71
213


NO-HIT
6


SPX0816
816
3477
429
1287
681
4.70E-147
[LN:H69979]
107









[AC:H69979]









[PN:proteinase homolog yrrO]









[GN:yrrO]









[CL:collagenase prtC]









[OR:Bacillus subtilis]


SPX0817
817
3478
243
729
251
6.20E-58
[LN:H69979]
107









[AC:H69979]









[PN:proteinase homolog yrrO]









[GN:yrrO]









[CL:collagenase prtC]









[OR:Bacillus subtilis]


SPX0818
818
3479
241
723
225
4.40E-26
[LN:YCBN_BACSU]
145









[AC:P42246]









[GN:YCBN]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 31.7 KD PROTEIN IN GLTP-CWLJ INTERGENIC REGION (ORF13)]









[SP:P42246]


SPX0819
819
3480
243
729


NO-HIT
6


SPX0820
820
3481
80
240
152
2.50E-16
[GI:1536960]
115









[LN:SOORFS]









[AC:Z79691]









[GN:yorfE]









[FN:putative transcription regulator]









[OR:Streptococcus pneumoniae]


SPX0821
821
3482
163
489


NO-HIT
6


SPX0822
822
3483
487
1461
981
1.70E-215
[LN:D70008]
111









[AC:D70008]









[PN:nicotinate phosphoribosyltransferase homolog yueK]









[GN:yueK]









[OR:Bacillus subtilis]


SPX0823
823
3484
275
825
923
1.70E-122
[LN:NADE_ECOLI]
121









[AC:P18843:P78235]









[GN:NADE:EFG:NTRL]









[OR:Escherichia coli]









[EC:6.3.5.1]









[DE:PROTEIN)]









[SP:P18843:P78235]


SPX0824
824
3485
66
198


NO-HIT
6


SPX0825
825
3486
184
552
135
1.80E-13
[GI:7635982]
117









[LN:SCE6]









[AC:AL353832]









[PN:putative acetyltransferase.]









[GN:SCE6.13]









[OR:Streptomyces coelicolor A3(2)]


SPX0826
826
3487
250
750
66
0.00023
[GI:4185565]
101









[LN:AF115379]









[AC:AF115379]









[PN:surface protein Pls]









[GN:pls]









[OR:Staphylococcus aureus]


SPX0827
827
3488
130
390
306
1.70E-36
[LN:A41971]
169









[AC:A41971:A60282:A33134]









[PN:surface protein pspA precursor:pneumococcal surface protein A]









[GN:pspA]









[CL:cpl repeat homology]









[OR:Streptococcus pneumoniae]


SPX0828
828
3489
347
1041
1229
5.30E-166
[LN:QUEA_BACSU]
128









[AC:O32054]









[GN:QUEA]









[OR:Bacillus subtilis]









[EC:5.-.-.-]









[DE:(QUEUOSINE BIOSYNTHESIS PROTEIN QUEA)]









[SP:O32054]


SPX0829
829
3490
236
708
336
3.00E-66
[LN:NAGB_BACSU]
139









[AC:O35000]









[GN:NAGB]









[OR:Bacillus subtilis]









[EC:5.3.1.10]









[DE:PHOSPHATE DEAMINASE) (GNPDA) (GLCN6P DEAMINASE)]









[SP:O35000]


SPX0830
830
3491
67
201
248
1.00E-29
[LN:T43742]
89









[AC:T43742]









[PN:ribosomal protein S21 [imported]]









[OR:Listeria monocytogenes]


SPX0831
831
3492
313
939
1224
7.60E-165
[GI:4884536]
123









[LN:AB027460]









[AC:AB027460]









[PN:Hpr kinase]









[OR:Streptococcus bovis]









[SR:Streptococcus bovis (strain:JB1) DNA]


SPX0832
832
3493
192
576
608
1.30E-84
“[LN:T11569]
169









[AC:T11569]









[PN:prolipoprotein diacylglyceryl transferase,]









[GN:lgt]









[CL:prolipoprotein diacylglyceryl transferase]









[OR:Streptococcus mutans]









[EC:2.4.99.-]”


SPX0833
833
3494
128
384
333
1.50E-41
[LN:T11570]
77









[AC:T11570]









[PN:hypothetical protein 1]









[OR:Streptococcus mutans]


SPX0834
834
3495
110
330


NO-HIT
6


SPX0835
835
3496
130
390
164
5.70E-17
[LN:T11571]
77









[AC:T11571]









[PN:hypothetical protein 2]









[OR:Streptococcus mutans]


SPX0836
836
3497
377
1131
596
4.30E-126
“[LN:B69640]
184









[AC:B69640]









[PN:coproporphyrinogen oxidase, III, oxygen-independent hemN]









[GN:hemN]









[CL:oxygen-independent coproporphyrinogen oxidase]









[OR:Bacillus subtilis]









[EC:1.3.3.3]”


SPX0837
837
3498
166
498


NO-HIT
6


SPX0838
838
3499
246
738
96
7.20E-11
[GI:4704640]
92









[LN:AF110462]









[AC:AF110462]









[PN:oleoyl-ACP thioesterase]









[OR:Elaeis guineensis]


SPX0839
839
3500
203
609
466
3.10E-59
[LN:H70023]
124









[AC:H70023]









[PN:N-acetyl-glucosamine catabolism homolog yutF]









[GN:yutF]









[CL:nagD protein]









[OR:Bacillus subtilis]


SPX0840
840
3501
217
651


NO-HIT
6


SPX0841
841
3502
108
324


NO-HIT
6


SPX0842
842
3503
134
402
447
5.60E-58
[LN:D69843]
128









[AC:D69843]









[PN:conserved hypothetical protein yjbD]









[GN:yjbD]









[CL:hypothetical protein yjbD]









[OR:Bacillus subtilis]


SPX0843
843
3504
93
279
216
2.40E-24
[LN:C69864]
87









[AC:C69864]









[PN:hypothetical protein yktA]









[GN:yktA]









[OR:Bacillus subtilis]


SPX0844
844
3505
283
849
207
1.30E-46
[LN:SUHB_BACSU]
120









[AC:Q45499]









[GN:SUHB]









[OR:Bacillus subtilis]









[DE:EXTRAGENIC SUPPRESSOR PROTEIN SUHB HOMOLOG]









[SP:Q45499]


SPX0845
845
3506
113
339


NO-HIT
6


SPX0846
846
3507
305
915
143
8.30E-21
[LN:YEBU_ECOLI]
149









[AC:P76273:O07980]









[GN:YEBU]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 53.2 KD PROTEIN IN PRC-PRPA INTERGENIC REGION]









[SP:P76273:O07980]


SPX0847
847
3508
76
228


NO-HIT
6


SPX0848
848
3509
56
168


NO-HIT
6


SPX0849
849
3510
78
234


NO-HIT
6


SPX0850
850
3511
293
879
465
1.40E-80
[LN:YQGG_BACSU]
103









[AC:P46338]









[GN:YQGG]









[OR:Bacillus subtilis]









[DE:REGION PRECURSOR (ORF108)]









[SP:P46338]


SPX0851
851
3512
306
918
403
1.00E-99
[LN:YQGH_BACSU]
92









[AC:P46339]









[GN:YQGH]









[OR:Bacillus subtilis]









[DE:REGION (ORF72)]









[SP:P46339]


SPX0852
852
3513
295
885
842
2.80E-114
[LN:YQGI_BACSU]
92









[AC:P46340]









[GN:YQGI]









[OR:Bacillus subtilis]









[DE:REGION (ORF73)]









[SP:P46340]


SPX0853
853
3514
268
804
796
1.10E-105
[LN:PSTB_METJA]
145









[AC:Q58418]









[GN:PSTB:MJ1012]









[OR:Methanococcus jannaschii]









[DE:PROBABLE PHOSPHATE TRANSPORT ATP-BINDING PROTEIN PSTB]









[SP:Q58418]


SPX0854
854
3515
253
759
763
7.10E-100
[LN:T43868]
193









[AC:T43868]









[PN:phosphate transport system peripheral membrane protein B [imported]]









[GN:pstB]









[CL:inner membrane protein malK:ATP-binding cassette homology]









[OR:Pseudomonas putida]


SPX0855
855
3516
218
654
212
3.70E-40
[GI:4530451]
90









[LN:AF118229]









[AC:AF118229]









[PN:PhoU]









[GN:phoU]









[OR:Streptococcus pneumoniae]


SPX0856
856
3517
272
816
190
2.40E-30
“[LN:B72357]
181









[AC:B72357]









[PN:amino acid ABC transporter, periplasmic amino acid-binding protein]









[GN:TM0593]









[CL:lysine-arginine-ornithine-binding protein]









[OR:Thermotoga maritima]”


SPX0857
857
3518
424
1272
778
4.20E-129
[GI:4580622]
77









[LN:AF118389]









[AC:AF118389]









[PN:unknown]









[OR:Streptococcus suis]


SPX0858
858
3519
57
171


NO-HIT
6


SPX0859
859
3520
171
513
340
3.10E-77
[GI:1524117]
108









[LN:LLALDB]









[AC:X82620]









[PN:alpha-acetolactate decarboxylase]









[GN:aldB]









[OR:Lactococcus lactis]


SPX0860
860
3521
67
201
265
2.40E-33
[GI:1808671]
129









[LN:SGCSHAG]









[AC:X65164:S52427]









[PN:putative alpha-acetolactate decarboxylase]









[GN:aldB]









[OR:Streptococcus gordonii]


SPX0861
861
3522
243
729
106
1.50E-25
[LN:A69830]
87









[AC:A69830]









[PN:hypothetical protein yhfC]









[GN:yhfC]









[OR:Bacillus subtilis]


SPX0862
862
3523
302
906
212
5.60E-55
[LN:MURB_BACSU]
150









[AC:P18579:P16669:P37581]









[GN:MURB]









[OR:Bacillus subtilis]









[EC:1.1.1.158]









[DE:ACETYLMURAMATE DEHYDROGENASE)]









[SP:P18579:P16669:P37581]


SPX0863
863
3524
379
1137
792
1.80E-114
“[LN:A70180]
237









[AC:A70180]









[PN:spermidine/putrescine ABC transporter, ATP-binding protein (potA) homolog]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Borrelia burgdorferi]









[SR:, Lyme disease spirochete]”


SPX0864
864
3525
109
327


NO-HIT
6


SPX0865
865
3526
211
633
324
4.20E-44
“[LN:H70179]
224









[AC:H70179]









[PN:spermidine/putrescine ABC transporter, permease protein (potB) homolog]









[CL:spermidine/putrescine transport system permease protein potH]









[OR:Borrelia burgdorferi]









[SR:, Lyme disease spirochete]”


SPX0866
866
3527
258
774
346
7.00E-66
“[LN:G70179]
224









[AC:G70179]









[PN:spermidine/putrescine ABC transporter, permease protein (potC) homolog]









[CL:spermidine/putrescine transport system permease protein potI]









[OR:Borrelia burgdorferi]









[SR:, Lyme disease spirochete]”


SPX0867
867
3528
226
678
173
5.20E-48
[LN:POTD_ECOLI]
143









[AC:P23861]









[GN:POTD]









[OR:Escherichia coli]









[DE:SPERMIDINE/PUTRESCINE-BINDING PERIPLASMIC PROTEIN PRECURSOR (SPBP)]









[SP:P23861]


SPX0868
868
3529
125
375
197
1.30E-20
[LN:POTD_ECOLI]
143









[AC:P23861]









[GN:POTD]









[OR:Escherichia coli]









[DE:SPERMIDINE/PUTRESCINE-BINDING PERIPLASMIC PROTEIN PRECURSOR (SPBP)]









[SP:P23861]


SPX0869
869
3530
80
240


NO-HIT
6


SPX0870
870
3531
73
219


NO-HIT
6


SPX0871
871
3532
163
489
159
4.70E-15
[LN:G70079]
136









[AC:G70079]









[PN:hypothetical protein yxjI]









[GN:yxjI]









[CL:Bacillus subtilis hypothetical protein yxjI]









[OR:Bacillus subtilis]


SPX0872
872
3533
89
267
332
2.40E-39
“[LN:SYA_BACSU]
146









[AC:O34526]









[GN:ALAS]









[OR:Bacillus subtilis]









[EC:6.1.1.7]









[DE:ALANYL-TRNA SYNTHETASE, (ALANINE--TRNA LIGASE) (ALARS)]









[SP:O34526]”


SPX0873
873
3534
787
2361
570
1.20E-202
“[LN:SYA_BACSU]
146









[AC:O34526]









[GN:ALAS]









[OR:Bacillus subtilis]









[EC:6.1.1.7]









[DE:ALANYL-TRNA SYNTHETASE, (ALANINE--TRNA LIGASE) (ALARS)]









[SP:O34526]”


SPX0874
874
3535
485
1455
1726
2.50E-257
[GI:2760119]
136









[LN:AB000830]









[AC:AB000830]









[PN:alpha-amylase precursor]









[OR:Streptococcus bovis]









[SR:Streptococcus bovis (strain:148) DNA]


SPX0875
875
3536
64
192


NO-HIT
6


SPX0876
876
3537
250
750
489
1.10E-62
“[LN:H75077]
187









[AC:H75077]









[PN:abc transporter, ATP-binding protein PAB1696]









[GN:PAB1696]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Pyrococcus abyssi]”


SPX0877
877
3538
545
1635


NO-HIT
6


SPX0878
878
3539
388
1164
468
2.20E-96
[LN:YWBD_BACSU]
144









[AC:P39587]









[GN:YWBD:IPA-19D]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 44.4 KD PROTEIN IN EPR-GALK INTERGENIC REGION]









[SP:P39587]


SPX0879
879
3540
226
678
165
6.60E-27
[GI:5919207]
100









[LN:AF184963]









[AC:AF184963]









[PN:3-dehydroquinase]









[GN:aroD]









[OR:Salmonella enteritidis]


SPX0880
880
3541
285
855
680
5.70E-89
[GI:3821433]
110









[LN:SPN232281]









[AC:AJ232281]









[PN:shikimate dehydrogenase]









[GN:aroE]









[OR:Streptococcus pneumoniae]


SPX0881
881
3542
356
1068
439
3.10E-84
“[LN:AROB_SYNY3]
148









[AC:P73997]









[GN:AROB:SLR2130]









[OR:Synechocystis sp]









[SR:,strain PCC 6803]









[EC:4.6.1.3]









[DE:3-DEHYDROQUINATE SYNTHASE,]









[SP:P73997]”


SPX0882
882
3543
389
1167
790
1.40E-142
[LN:AROC_BACSU]
138









[AC:P31104]









[GN:AROF]









[OR:Bacillus subtilis]









[EC:4.6.1.4]









[DE:PHOSPHOLYASE) (VEGETATIVE PROTEIN 216) (VEG216)]









[SP:P31104]


SPX0883
883
3544
368
1104
402
2.40E-127
“[LN:TYRA_LACLA]
165









[AC:P43901]









[GN:TYRA]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:1.3.1.12]









[DE:PREPHENATE DEHYDROGENASE, (PDH)]









[SP:P43901]”


SPX0884
884
3545
113
339
152
7.80E-16
[GI:3688819]
87









[LN:AF084104]









[AC:AF084104]









[PN:hypothetical protein]









[OR:Bacillus firmus]


SPX0885
885
3546
428
1284
2094
1.40E-284
[GI:5616525]
129









[LN:AF169483]









[AC:AF169483]









[PN:5-enolpyruvylshikimate-3-phosphate synthase]









[GN:aroA]









[OR:Streptococcus pneumoniae]


SPX0886
886
3547
159
477
262
3.60E-40
“[LN:AROK_LACLA]
156









[AC:P43906]









[GN:AROK]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:2.7.1.71]









[DE:SHIKIMATE KINASE, (SK)]









[SP:P43906]”


SPX0887
887
3548
282
846
707
3.20E-98
“[LN:PHEA_LACLA]
153









[AC:P43909]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:4.2.1.51]









[DE:PREPHENATE DEHYDRATASE, (PDT)]









[SP:P43909]”


SPX0888
888
3549
231
693
91
7.60E-09
[GI:7160813]
107









[LN:EFA276231]









[AC:AJ276231]









[PN:PSR protein]









[GN:psr]









[FN:unknown]









[OR:Enterococcus faecalis]


SPX0889
889
3550
200
600
268
9.10E-46
[GI:7160813]
107









[LN:EFA276231]









[AC:AJ276231]









[PN:PSR protein]









[GN:psr]









[FN:unknown]









[OR:Enterococcus faecalis]


SPX0890
890
3551
282
846
172
1.10E-24
[LN:LICD_HAEIN]
95









[AC:P14184]









[GN:LICD]









[OR:Haemophilus influenzae]









[DE:LICD PROTEIN]









[SP:P14184]


SPX0891
891
3552
134
402


NO-HIT
6


SPX0892
892
3553
386
1158
244
1.70E-28
[LN:F70441]
103









[AC:F70441]









[PN:capsular polysaccharide biosynthsis protein]









[GN:cap]









[OR:Aquifex aeolicus]


SPX0893
893
3554
329
987
327
4.10E-51
[GI:3320393]
111









[LN:AF030373]









[AC:AF030373]









[PN:galactosyl transferase]









[GN:cps23FU]









[OR:Streptococcus pneumoniae]


SPX0894
894
3555
478
1434
96
0.00022
[GI:5931973]
100









[LN:AF125164]









[AC:AF125164]









[PN:putative polymerase]









[GN:wzy]









[OR:Bacteroides fragilis]


SPX0895
895
3556
151
453


NO-HIT
6


SPX0896
896
3557
202
606


NO-HIT
6


SPX0897
897
3558
99
297


NO-HIT
6


SPX0898
898
3559
185
555
349
1.10E-42
[GI:5360696]
164









[LN:AB022909]









[AC:AB022909]









[PN:negative regulator of genetic competence]









[GN:mecA]









[OR:Streptococcus mutans]









[SR:Streptococcus mutans (strain:Xc) DNA]


SPX0899
899
3560
128
384


NO-HIT
6


SPX0900
900
3561
71
213
127
1.70E-11
[GI:5360696]
164









[LN:AB022909]









[AC:AB022909]









[PN:negative regulator of genetic competence]









[GN:mecA]









[OR:Streptococcus mutans]









[SR:Streptococcus mutans (strain:Xc) DNA]


SPX0901
901
3562
429
1287
1425
2.60E-191
“[LN:DHOM_LACLA]
163









[AC:P52985]









[GN:HOM]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:1.1.1.3]









[DE:HOMOSERINE DEHYDROGENASE, (HDH)]









[SP:P52985]”


SPX0902
902
3563
290
870
1439
4.70E-194
“[LN:KHSE_STRPN]
124









[AC:P72535]









[GN:THRB]









[OR:Streptococcus pneumoniae]









[EC:2.7.1.39]









[DE:HOMOSERINE KINASE, (HK)]









[SP:P72535]”


SPX0903
903
3564
142
426


NO-HIT
6


SPX0904
904
3565
75
225
192
8.30E-23
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX0905
905
3566
86
258
366
6.80E-46
[LN:PMSR_STRPN]
110









[AC:P35593]









[GN:MSRA:EXP3]









[OR:Streptococcus pneumoniae]









[DE:(EXPORTED PROTEIN 3)]









[SP:P35593]


SPX0906
906
3567
256
768
1236
9.90E-167
[LN:PMSR_STRPN]
110









[AC:P35593]









[GN:MSRA:EXP3]









[OR:Streptococcus pneumoniae]









[DE:(EXPORTED PROTEIN 3)]









[SP:P35593]


SPX0907
907
3568
103
309
123
6.70E-10
“[LN:E72396]
180









[AC:E72396]









[PN:ABC transporter, ATP-binding protein]









[GN:TM0287]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Thermotoga maritima]”


SPX0908
908
3569
488
1464
472
3.40E-92
“[LN:E72396]
180









[AC:E72396]









[PN:ABC transporter, ATP-binding protein]









[GN:TM0287]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Thermotoga maritima]”


SPX0909
909
3570
62
186


NO-HIT
6


SPX0910
910
3571
584
1752
722
7.90E-145
[LN:Y08A_MYCTU]
148









[AC:Q11047]









[GN:MTCY50.10]









[OR:Mycobacterium tuberculosis]









[DE:HYPOTHETICAL ABC TRANSPORTER ATP-BINDING PROTEIN CY50.10]









[SP:Q11047]


SPX0911
911
3572
86
258
325
5.10E-41
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX0912
912
3573
129
387
95
8.00E-06
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX0913
913
3574
64
192


NO-HIT
6


SPX0914
914
3575
74
222


NO-HIT
6


SPX0915
915
3576
69
207


NO-HIT
6


SPX0916
916
3577
65
195


NO-HIT
6


SPX0917
917
3578
99
297


NO-HIT
6


SPX0918
918
3579
295
885
447
1.10E-56
[LN:A70039]
188









[AC:A70039]









[PN:ABC transporter (ATP-binding protein) homolog yvfR]









[GN:yvfR]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Bacillus subtilis]


SPX0919
919
3580
246
738
289
1.00E-39
[GI:6759480]
90









[LN:BCE243712]









[AC:AJ243712]









[PN:YVFS protein]









[GN:yvfS]









[OR:Bacillus cereus]


SPX0920
920
3581
366
1098
1715
5.40E-238
[GI:5830547]
102









[LN:SPAJ6400]









[AC:AJ006400]









[PN:histidine kinase]









[GN:hk11]









[OR:Streptococcus pneumoniae]


SPX0921
921
3582
200
600
932
2.00E-123
[GI:5830548]
104









[LN:SPAJ6400]









[AC:AJ006400]









[PN:response regulator]









[GN:rr11]









[OR:Streptococcus pneumoniae]


SPX0922
922
3583
337
1011
1328
1.10E-176
[GI:7328454]
151









[LN:AB028599]









[AC:AB028599]









[PN:catabolite control protein A]









[GN:ccpA]









[OR:Streptococcus bovis]









[SR:Streptococcus bovis (strain:JB1) DNA]


SPX0923
923
3584
131
393
270
4.60E-32
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX0924
924
3585
113
339
89
5.70E-05
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX0925
925
3586
321
963
295
8.70E-56
[LN:G75283]
102









[AC:G75283]









[PN:L-asparaginase]









[GN:DR2353]









[CL:asparaginase]









[OR:Deinococcus radiodurans]


SPX0926
926
3587
463
1389
213
9.90E-43
[LN:C69862]
178









[AC:C69862]









[PN:conserved hypothetical protein ykrA]









[GN:ykrA]









[CL:Methanobacterium thermoautotrophicum conserved hypothetical protein MTH1071]









[OR:Bacillus subtilis]


SPX0927
927
3588
151
453
127
6.20E-14
[LN:A69220]
155









[AC:A69220]









[PN:conserved hypothetical protein MTH898]









[GN:MTH898]









[CL:Escherichia coli ybdQ protein]









[OR:Methanobacterium thermoautotrophicum]


SPX0928
928
3589
97
291


NO-HIT
6


SPX0929
929
3590
239
717
819
4.70E-109
“[LN:YFBQ_HAEIN]
133









[AC:P71348]









[GN:HI0286]









[OR:Haemophilus influenzae]









[EC:2.6.1.-]









[DE:PROBABLE AMINOTRANSFERASE HI0286,]









[SP:P71348]”


SPX0930
930
3591
111
333


NO-HIT
6


SPX0931
931
3592
125
375
385
1.70E-48
“[LN:YFBQ_HAEIN]
133









[AC:P71348]









[GN:HI0286]









[OR:Haemophilus influenzae]









[EC:2.6.1.-]









[DE:PROBABLE AMINOTRANSFERASE HI0286,]









[SP:P71348]”


SPX0932
932
3593
45
135
170
7.60E-20
[LN:RL34_BACST]
113









[AC:P23376]









[GN:RPMH]









[OR:Bacillus stearothermophilus]









[DE:50S RIBOSOMAL PROTEIN L34]









[SP:P23376]


SPX0933
933
3594
67
201


NO-HIT
6


SPX0934
934
3595
218
654
116
9.60E-07
[GI:546643]
121









[LN:S70345]









[AC:S70345]









[PN:SpaA]









[GN:SpaA]









[OR:Streptococcus sobrinus]









[SR:Streptococcus sobrinus MUCOB 263]


SPX0935
935
3596
75
225
180
6.20E-19
[LN:YABD_BACSU]
137









[AC:P37545]









[GN:YABD]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 29.2 KD PROTEIN IN METS-KSGA INTERGENIC REGION]









[SP:P37545]


SPX0936
936
3597
181
543
469
3.60E-60
[LN:YABD_BACSU]
137









[AC:P37545]









[GN:YABD]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 29.2 KD PROTEIN IN METS-KSGA INTERGENIC REGION]









[SP:P37545]


SPX0937
937
3598
187
561
235
2.70E-52
[LN:YABF_BACSU]
137









[AC:P37547]









[GN:YABF]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 20.7 KD PROTEIN IN METS-KSGA INTERGENIC REGION]









[SP:P37547]


SPX0938
938
3599
304
912


NO-HIT
6


SPX0939
939
3600
99
297
149
3.30E-15
[GI:7576923]
109









[LN:AF242367]









[AC:AF242367]









[PN:lactococcin 972]









[GN:lclA]









[OR:Lactococcus lactis subsp. lactis]


SPX0940
940
3601
269
807
65
5.50E-08
[GI:3355783]
98









[LN:LLJ002203]









[AC:AJ002203]









[PN:putative immunity]









[GN:orf2]









[OR:Lactococcus lactis]


SPX0941
941
3602
450
1350
357
1.30E-89
[GI:4009478]
83









[LN:AF068902]









[AC:AF068902]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX0942
942
3603
214
642
667
2.50E-87
[GI:4009479]
83









[LN:AF068902]









[AC:AF068902]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX0943
943
3604
103
309


NO-HIT
6


SPX0944
944
3605
169
507


NO-HIT
6


SPX0945
945
3606
291
873
781
3.80E-104
[LN:KSGA_BACSU]
111









[AC:P37468]









[GN:KSGA]









[OR:Bacillus subtilis]









[EC:2.1.1.-]









[DE:DIMETHYLTRANSFERASE)]









[SP:P37468]


SPX0946
946
3607
293
879
394
5.10E-100
[LN:A69879]
140









[AC:A69879]









[PN:conserved hypothetical protein yloQ]









[GN:yloQ]









[CL:conserved hypothetical protein HI1714]









[OR:Bacillus subtilis]


SPX0947
947
3608
301
903
460
1.20E-69
“[LN:RPE_RHOCA]
154









[AC:P51012]









[GN:CBBE]









[OR:Rhodobacter capsulatus]









[SR:,Rhodopseudomonas capsulata]









[EC:5.1.3.1]









[DE:EPIMERASE) (PPE) (R5P3E)]









[SP:P51012]”


SPX0948
948
3609
221
663
143
3.50E-18
[LN:C69879]
87









[AC:C69879]









[PN:hypothetical protein yloS]









[GN:yloS]









[OR:Bacillus subtilis]


SPX0949
949
3610
405
1215
91
5.10E-07
[LN:E81528]
140









[AC:E81528]









[PN:conserved hypothetical protein CP0874 [imported]]









[GN:CP0874]









[OR:Chlamydophila pneumoniae:Chlamydia pneumoniae]


SPX0950
950
3611
314
942
453
1.00E-88
[LN:G69818]
93









[AC:G69818]









[PN:CMP-binding factor homolog yhaM]









[GN:yhaM]









[OR:Bacillus subtilis]


SPX0951
951
3612
276
828
498
2.80E-98
[GI:2706406]
117









[LN:LLAJ642]









[AC:AJ222642]









[GN:purR]









[FN:activator of purine biosynthetic genes]









[OR:Lactococcus lactis]


SPX0952
952
3613
70
210
83
0.00046
“[LN:TABA_PSESZ]
110









[AC:P31851]









[GN:TABA]









[OR:Pseudomonas syringae]









[SR:,pvtabaci]









[DE:TABA PROTEIN]









[SP:P31851]”


SPX0953
953
3614
128
384
199
3.60E-21
“[LN:TABA_PSESZ]
110









[AC:P31851]









[GN:TABA]









[OR:Pseudomonas syringae]









[SR:,pvtabaci]









[DE:TABA PROTEIN]









[SP:P31851]”


SPX0954
954
3615
100
300


NO-HIT
6


SPX0955
955
3616
335
1005
371
8.10E-63
“[LN:TABA_PSESZ]
110









[AC:P31851]









[GN:TABA]









[OR:Pseudomonas syringae]









[SR:,pvtabaci]









[DE:TABA PROTEIN]









[SP:P31851]”


SPX0956
956
3617
265
795
1121
8.40E-152
[LN:PFLA_STRMU]
106









[AC:O68575]









[GN:ACT:PFLC]









[OR:Streptococcus mutans]









[EC:1.97.1.4]









[DE:ENZYME)]









[SP:O68575]


SPX0957
957
3618
309
927
140
6.90E-32
[GI:6117974]
98









[LN:AF139908]









[AC:AF139908]









[PN:membrane protein homolog]









[OR:Listeria monocytogenes]


SPX0958
958
3619
93
279
108
9.80E-09
[LN:T35660]
96









[AC:T35660]









[PN:probable acylphosphatase]









[GN:SC7A1.20]









[OR:Streptomyces coelicolor]


SPX0959
959
3620
253
759
217
1.10E-43
[LN:G69984]
132









[AC:G69984]









[PN:rRNA methylase homolog ysgA]









[GN:ysgA]









[CL:conserved hypothetical protein HI0860]









[OR:Bacillus subtilis]


SPX0960
960
3621
228
684
433
1.10E-57
[GI:3171165]
120









[LN:AF064763]









[AC:AF064763]









[PN:putative membrane spanning protein]









[OR:Lactococcus lactis subsp. cremoris]


SPX0961
961
3622
72
216


NO-HIT
6


SPX0962
962
3623
331
993
1387
1.70E-186
“[LN:ASNA_HAEIN]
157









[AC:P44338]









[GN:ASNA:HI0564]









[OR:Haemophilus influenzae]









[EC:6.3.1.1]









[DE:ASPARTATE--AMMONIA LIGASE, (ASPARAGINE SYNTHETASE A)]









[SP:P44338]”


SPX0963
963
3624
180
540
279
1.30E-33
[LN:E69874]
176









[AC:E69874]









[PN:conserved hypothetical protein ylbH]









[GN:ylbH]









[CL:Escherichia coli hypothetical 21.7K protein (ftsY-nikA intergenic region)]









[OR:Bacillus subtilis]


SPX0964
964
3625
123
369
184
3.00E-25
[LN:G81347]
136









[AC:G81347]









[PN:3-deoxy-D-manno-octulosonic-acid transferase Cj0767c [imported]]









[GN:kdtB:Cj0767c]









[OR:Campylobacter jejuni]


SPX0965
965
3626
239
717
184
7.20E-17
[LN:A69875]
87









[AC:A69875]









[PN:hypothetical protein ylbL]









[GN:ylbL]









[OR:Bacillus subtilis]


SPX0966
966
3627
78
234
101
1.90E-16
[LN:A69875]
87









[AC:A69875]









[PN:hypothetical protein ylbL]









[GN:ylbL]









[OR:Bacillus subtilis]


SPX0967
967
3628
95
285


NO-HIT
6


SPX0968
968
3629
428
1284
620
3.20E-133
[LN:MURA_ACICA]
124









[AC:P33986]









[GN:MURA:MURZ]









[OR:Acinetobacter calcoaceticus]









[EC:2.5.1.7]









[DE:TRANSFERASE) (EPT)]









[SP:P33986]


SPX0969
969
3630
75
225
320
4.60E-41
[LN:EPUA_STRPN]
97









[AC:Q03159]









[GN:EPUA]









[OR:Streptococcus pneumoniae]









[DE:EPUA PROTEIN]









[SP:Q03159]


SPX0970
970
3631
275
825
1392
2.50E-182
“[LN:NUCE_STRPN]
151









[AC:Q03158]









[GN:ENDA]









[OR:Streptococcus pneumoniae]









[EC:3.1.30.-]









[DE:DNA-ENTRY NUCLEASE (COMPETENCE-SPECIFIC NUCLEASE),]









[SP:Q03158]”


SPX0971
971
3632
328
984
1168
4.20E-160
[GI:2952527]
100









[LN:AF051356]









[AC:AF051356]









[PN:putative hemolysin]









[GN:hlyX]









[OR:Streptococcus mutans]


SPX0972
972
3633
95
285
266
6.50E-33
[GI:2952527]
100









[LN:AF051356]









[AC:AF051356]









[PN:putative hemolysin]









[GN:hlyX]









[OR:Streptococcus mutans]


SPX0973
973
3634
1204
3612
1921
0
[LN:T44375]
121









[AC:T44375]









[PN:rpoB protein [imported]]









[CL:DNA-directed RNA polymerase beta chain]









[OR:Bacillus halodurans]


SPX0974
974
3635
116
348


NO-HIT
6


SPX0975
975
3636
57
171


NO-HIT
6


SPX0976
976
3637
1226
3678
4009
0
[LN:RPOC_STRPY]
150









[AC:P95816]









[GN:RPOC]









[OR:Streptococcus pyogenes]









[EC:2.7.7.6]









[DE:BETA′CHAIN) (RNA POLYMERASE BETA′SUBUNIT) (FRAGMENT)]









[SP:P95816]


SPX0977
977
3638
131
393


NO-HIT
6


SPX0978
978
3639
138
414
192
4.30E-48
[GI:1655704]
121









[LN:XLNM23]









[AC:X97899]









[PN:NM23/nucleoside diphosphate kinase]









[OR:Xenopus laevis]









[SR:African clawed frog]


SPX0979
979
3640
93
279


NO-HIT
6


SPX0980
980
3641
211
633
472
1.50E-87
[GI:4009479]
83









[LN:AF068902]









[AC:AF068902]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX0981
981
3642
672
2016
277
4.50E-70
[GI:4009478]
83









[LN:AF068902]









[AC:AF068902]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX0982
982
3643
65
195


NO-HIT
6


SPX0983
983
3644
288
864
110
2.30E-09
[LN:JC6007]
152









[AC:JC6007]









[PN:transcription activator plcR]









[GN:plcR]









[CL:Bacillus thuringiensis transcription activator plcR]









[OR:Bacillus thuringiensis]


SPX0984
984
3645
137
411


NO-HIT
6


SPX0985
985
3646
159
477
166
2.20E-36
[LN:C69786]
130









[AC:C69786]









[PN:conserved hypothetical protein ydiB]









[GN:ydiB]









[CL:hypothetical protein HI0065]









[OR:Bacillus subtilis]


SPX0986
986
3647
173
519
149
7.60E-28
[LN:D72360]
96









[AC:D72360]









[PN:conserved hypothetical protein]









[GN:TM0577]









[OR:Thermotoga maritima]


SPX0987
987
3648
339
1017
182
6.50E-46
[LN:LYTR_BACSU]
105









[AC:Q02115]









[GN:LYTR]









[OR:Bacillus subtilis]









[DE:MEMBRANE-BOUND PROTEIN LYTR]









[SP:Q02115]


SPX0988
988
3649
419
1257
2015
1.70E-272
[LN:CINA_STRPN]
161









[AC:P54184:Q54853]









[GN:CINA:EXP10]









[OR:Streptococcus pneumoniae]









[DE:PUTATIVE COMPETENCE-DAMAGE PROTEIN (EXPORTED PROTEIN 10)]









[SP:P54184:Q54853]


SPX0989
989
3650
389
1167
1928
6.10E-256
[LN:RECA_STRPN]
97









[AC:P30758]









[GN:RECA]









[OR:Streptococcus pneumoniae]









[DE:RECA PROTEIN]









[SP:P30758]


SPX0990
990
3651
457
1371
2252
0
[GI:2398825]
96









[LN:SPCINREC]









[AC:Z34303]









[PN:DinF protein]









[GN:dinF]









[OR:Streptococcus pneumoniae]


SPX0991
991
3652
319
957
1786
1.50E-240
[LN:ALYS_STRPN]
160









[AC:P06653]









[GN:LYTA]









[OR:Streptococcus pneumoniae]









[EC:3.5.1.28]









[DE:HYDROLASE) (MUCOPEPTIDE AMINOHYDROLASE) (CELL WALL HYDROLASE)]









[SP:P06653]


SPX0992
992
3653
79
237


NO-HIT
6


SPX0993
993
3654
81
243


NO-HIT
6


SPX0994
994
3655
120
360


NO-HIT
6


SPX0995
995
3656
142
426


NO-HIT
6


SPX0996
996
3657
75
225


NO-HIT
6


SPX0997
997
3658
332
996
676
4.50E-129
[GI:2398827]
94









[LN:SPCINREC]









[AC:Z34303]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX0998
998
3659
82
246


NO-HIT
6


SPX0999
999
3660
90
270


NO-HIT
6


SPX1000
1000
3661
87
261


NO-HIT
6


SPX1001
1001
3662
101
303
296
7.00E-36
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX1002
1002
3663
44
132
108
5.70E-09
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX1003
1003
3664
153
459


NO-HIT
6


SPX1004
1004
3665
203
609


NO-HIT
6


SPX1005
1005
3666
137
411


NO-HIT
6


SPX1006
1006
3667
472
1416
2426
0
[LN:A28568]
110









[AC:A28568:S12829]









[PN:pneumolysin]









[CL:dipeptide transport protein]









[OR:Streptococcus pneumoniae]


SPX1007
1007
3668
239
717
915
1.30E-119
[LN:A64963]
119









[AC:A64963]









[PN:conserved hypothetical protein b1983]









[CL:hypothetical protein MG332]









[OR:Escherichia coli]


SPX1008
1008
3669
150
450
104
9.20E-07
[LN:C72329]
93









[AC:C72329]









[PN:hypothetical protein TM0816]









[GN:TM0816]









[OR:Thermotoga maritima]


SPX1009
1009
3670
291
873
309
1.20E-35
[GI:6759558]
116









[LN:SC7A8]









[AC:AL137187]









[PN:putative ABC transporter]









[GN:SC7A8.02]









[OR:Streptomyces coelicolor A3(2)]


SPX1010
1010
3671
344
1032
335
7.80E-76
[GI:6759559]
116









[LN:SC7A8]









[AC:AL137187]









[PN:putative ABC transporter]









[GN:SC7A8.03]









[OR:Streptomyces coelicolor A3(2)]


SPX1011
1011
3672
121
363


NO-HIT
6


SPX1012
1012
3673
168
504
130
2.10E-10
[LN:Y374_METJA]
114









[AC:Q57819]









[GN:MJ0374]









[OR:Methanococcus jannaschii]









[DE:HYPOTHETICAL PROTEIN MJ0374]









[SP:Q57819]


SPX1013
1013
3674
150
450


NO-HIT
6


SPX1014
1014
3675
225
675


NO-HIT
6


SPX1015
1015
3676
74
222
125
8.00E-13
[GI:1914870]
81









[LN:SPZ82001]









[AC:Z82001]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX1016
1016
3677
100
300


NO-HIT
6


SPX1017
1017
3678
106
318
276
6.70E-34
[LN:G69998]
127









[AC:G69998]









[PN:thioredoxin H1 homolog ytpP]









[GN:ytpP]









[CL:thioredoxin:thioredoxin homology]









[OR:Bacillus subtilis]


SPX1018
1018
3679
126
378


NO-HIT
6


SPX1019
1019
3680
209
627
217
5.30E-44
[LN:A69999]
172









[AC:A69999]









[PN:phenylalanyl-tRNA synthetase (beta subunit) homolog ytpR]









[GN:ytpR]









[CL:Mycoplasma genitalium hypothetical protein MG449]









[OR:Bacillus subtilis]


SPX1020
1020
3681
254
762
354
4.20E-67
[GI:2425123]
90









[LN:AF019986]









[AC:AF019986]









[PN:PksB]









[GN:pksB]









[OR:Dictyostelium discoideum]


SPX1021
1021
3682
132
396
227
1.20E-34
[GI:6716352]
136









[LN:AF145054]









[AC:AF145054:AF001793:AF118440:U89246]









[PN:ORF9]









[GN:orf9]









[OR:Streptococcus thermophilus bacteriophage 7201]


SPX1022
1022
3683
95
285
460
1.90E-58
[GI:4566772]
105









[LN:AF117741]









[AC:AF117741]









[PN:cochaperonin GroES]









[GN:groES]









[OR:Streptococcus pneumoniae]


SPX1023
1023
3684
203
609
344
8.20E-43
[GI:1196510]
143









[LN:MSGTCWPA]









[AC:M15467]









[PN:unknown protein]









[OR:Mycobacterium tuberculosis]









[SR:Mycobacterium tuberculosis (strain Erdman) DNA]


SPX1024
1024
3685
541
1623
2611
0
[GI:4566773]
103









[LN:AF117741]









[AC:AF117741]









[PN:chaperonin GroEL]









[GN:groEL]









[OR:Streptococcus pneumoniae]


SPX1025
1025
3686
70
210
70
3.30E-06
[LN:C71647]
93









[AC:C71647]









[PN:hypothetical protein RP851]









[GN:RP851]









[OR:Rickettsia prowazekii]


SPX1026
1026
3687
84
252
139
1.80E-13
[LN:F72338]
96









[AC:F72338]









[PN:conserved hypothetical protein]









[GN:TM0731]









[OR:Thermotoga maritima]


SPX1027
1027
3688
64
192


NO-HIT
6


SPX1028
1028
3689
258
774
129
6.70E-09
[LN:T33885]
149









[AC:T33885]









[PN:hypothetical protein H14E04.1]









[GN:H14E04.1]









[CL:24-sterol C-methyltransferase:bioC homology]









[OR:Caenorhabditis elegans]


SPX1029
1029
3690
113
339
133
1.50E-11
[LN:AB025228]
111









[AC:AB025228]









[GN:rgg]









[OR:Streptococcus oralis]









[SR:Streptococcus oralis (strain:ATCC10557) DNA]


SPX1030
1030
3691
116
348
90
8.90E-06
[LN:AB025228]
111









[AC:AB025228]









[GN:rgg]









[OR:Streptococcus oralis]









[SR:Streptococcus oralis (strain:ATCC10557) DNA]


SPX1031
1031
3692
178
534
294
4.90E-36
[LN:F69815]
136









[AC:F69815]









[PN:hypothetical protein ygaC]









[GN:ygaC]









[CL:Bacillus subtilis hypothetical protein ygaC]









[OR:Bacillus subtilis]


SPX1032
1032
3693
60
180


NO-HIT
6


SPX1033
1033
3694
287
861
226
3.30E-32
[LN:H69800]
87









[AC:H69800]









[PN:hypothetical protein yfhG]









[GN:yfhG]









[OR:Bacillus subtilis]


SPX1034
1034
3695
452
1356
606
1.00E-145
[LN:F69806]
129









[AC:F69806]









[PN:RNA methyltransferase homolog yfjO]









[GN:yfjO]









[CL:hypothetical protein HI0333]









[OR:Bacillus subtilis]


SPX1035
1035
3696
82
246


NO-HIT
6


SPX1036
1036
3697
50
150
82
7.60E-06
[LN:G71244]
95









[AC:G71244]









[PN:hypothetical protein PH0217]









[GN:PH0217]









[OR:Pyrococcus horikoshii]


SPX1037
1037
3698
62
186


NO-HIT
6


SPX1038
1038
3699
87
261
136
3.90E-14
[LN:G81516]
130









[AC:G81516]









[PN:hypothetical protein CP0988 [imported]]









[GN:CP0988]









[OR:Chlamydophila pneumoniae:Chlamydia pneumoniae]


SPX1039
1039
3700
76
228
190
1.00E-21
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX1040
1040
3701
79
237


NO-HIT
6


SPX1041
1041
3702
94
282
301
2.00E-35
[LN:DHAS_STRMU]
108









[AC:P10539]









[GN:ASD]









[OR:Streptococcus mutans]









[EC:1.2.1.11]









[DE:DEHYDROGENASE)]









[SP:P10539]


SPX1042
1042
3703
92
276
325
3.80E-40
[LN:DHAS_STRMU]
108









[AC:P10539]









[GN:ASD]









[OR:Streptococcus mutans]









[EC:1.2.1.11]









[DE:DEHYDROGENASE)]









[SP:P10539]


SPX1043
1043
3704
222
666
590
1.20E-108
[LN:DHAS_STRMU]
108









[AC:P10539]









[GN:ASD]









[OR:Streptococcus mutans]









[EC:1.2.1.11]









[DE:DEHYDROGENASE)]









[SP:P10539]


SPX1044
1044
3705
312
936
192
2.60E-55
“[LN:B72246]
187









[AC:B72246]









[PN:dihydrodipicolinate synthase, TM1521 [similarity]]









[GN:TM1521]









[CL:Pseudomonas 5-dehydro-4-deoxyglucarate dehydratase]









[OR:Thermotoga maritima]









[EC:4.2.1.52]”


SPX1045
1045
3706
458
1374
1312
1.10E-249
[GI:6448626]
167









[LN:SAG251564]









[AC:AJ251564]









[PN:thiophene degradation protein F]









[GN:thdF]









[FN:putative thiophene and furan oxidation gene]









[OR:Streptococcus agalactiae]


SPX1046
1046
3707
75
225
127
1.30E-12
“[LN:A43397]
153









[AC:A43397:S35225]









[PN:4-oxalocrotonate tautomerase, xylH]









[GN:xylH]









[CL:4-oxalocrotonate tautomerase]









[OR:Pseudomonas putida]









[EC:5.3.2.-]”


SPX1047
1047
3708
164
492
724
7.00E-97
“[LN:KITH_STRGC]
123









[AC:P47848]









[GN:TDK]









[OR:Streptococcus gordonii challis]









[EC:2.7.1.21]









[DE:THYMIDINE KINASE,]









[SP:P47848]”


SPX1048
1048
3709
281
843
642
2.20E-103
[LN:RF1_BACSU]
114









[AC:P45872]









[GN:PRFA]









[OR:Bacillus subtilis]









[DE:PEPTIDE CHAIN RELEASE FACTOR 1 (RF-1)]









[SP:P45872]


SPX1049
1049
3710
143
429
350
2.60E-43
[LN:RF1_BACSU]
114









[AC:P45872]









[GN:PRFA]









[OR:Bacillus subtilis]









[DE:PEPTIDE CHAIN RELEASE FACTOR 1 (RF-1)]









[SP:P45872]


SPX1050
1050
3711
280
840
183
8.00E-41
[LN:HEMK_BACSU]
98









[AC:P45873]









[GN:YWKE]









[OR:Bacillus subtilis]









[DE:HEMK PROTEIN HOMOLOG]









[SP:P45873]


SPX1051
1051
3712
201
603
244
1.80E-32
[GI:6015811]
110









[LN:SSU18930]









[AC:Y18930]









[PN:hypothetical protein]









[GN:ORF-c09_003]









[OR:Sulfolobus solfataricus]


SPX1052
1052
3713
144
432
97
1.30E-05
[LN:PHNO_ECOLI]
89









[AC:P16691]









[GN:PHNO]









[OR:Escherichia coli]









[DE:PHNO PROTEIN]









[SP:P16691]


SPX1053
1053
3714
419
1257
858
7.90E-176
[LN:GLYA_BACSU]
110









[AC:P39148]









[GN:GLYA:GLYC:IPC-34D]









[OR:Bacillus subtilis]









[EC:2.1.2.1]









[DE:(SHMT)]









[SP:P39148]


SPX1054
1054
3715
336
1008
130
3.90E-11
[GI:6899993]
109









[LN:CST130879]









[AC:AJ130879]









[PN:hypothetical protein]









[FN:unknown]









[OR:Clostridium sticklandii]


SPX1055
1055
3716
205
615
243
1.60E-27
[LN:F69900]
101









[AC:F69900]









[PN:transposon-related protein homolog yocA]









[GN:yocA]









[OR:Bacillus subtilis]


SPX1056
1056
3717
325
975
104
7.60E-08
[LN:YPUA_BACSU]
160









[AC:P31847:P37951]









[GN:YPUA]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 31.3 KD PROTEIN IN LYSA-PPIB INTERGENIC REGION (ORFX19)]









[SP:P31847:P37951]


SPX1057
1057
3718
548
1644
767
5.90E-131
[LN:E69793]
129









[AC:E69793]









[PN:RNA methyltransferase homolog yefA]









[GN:yefA]









[CL:hypothetical protein HI0333]









[OR:Bacillus subtilis]


SPX1058
1058
3719
98
294


NO-HIT
6


SPX1059
1059
3720
83
249


NO-HIT
6


SPX1060
1060
3721
65
195
81
3.20E-08
[LN:C69931]
98









[AC:C69931]









[PN:transcription regulator homolog yozG]









[GN:yozG]









[OR:Bacillus subtilis]


SPX1061
1061
3722
80
240


NO-HIT
6


SPX1062
1062
3723
345
1035
276
3.80E-70
[GI:2276374]
148









[LN:CDU02617]









[AC:U02617]









[PN:DtxR/iron regulated lipoprotein precursor]









[GN:irp1]









[FN:iron transport]









[OR:Corynebacterium diphtheriae]


SPX1063
1063
3724
212
636


NO-HIT
6


SPX1064
1064
3725
336
1008
643
1.40E-86
[LN:T44797]
161









[AC:T44797]









[PN:iron transport membrane protein irp1B [imported]]









[GN:irp1B]









[CL:vitamin B12 transport protein btuC]









[OR:Corynebacterium diphtheriae]


SPX1065
1065
3726
336
1008
484
1.10E-82
[LN:T44798]
161









[AC:T44798]









[PN:iron transport membrane protein irp1C [imported]]









[GN:irp1C]









[CL:vitamin B12 transport protein btuC]









[OR:Corynebacterium diphtheriae]


SPX1066
1066
3727
74
222


NO-HIT
6


SPX1067
1067
3728
138
414


NO-HIT
6


SPX1068
1068
3729
265
795
694
6.10E-91
[LN:G70022]
176









[AC:G70022]









[PN:iron(III) dicitrate transport permease homolog yusV]









[GN:yusV]









[CL:inner membrane protein malK:ATP-binding cassette homology]









[OR:Bacillus subtilis]


SPX1069
1069
3730
87
261
151
1.30E-14
[GI:2467226]
96









[LN:LLLPK214]









[AC:X92946:Y10522]









[PN:transposase]









[GN:tnpA]









[OR:Lactococcus lactis]


SPX1070
1070
3731
152
456
137
1.10E-10
“[LN:T4BB_BACCO]
133









[AC:Q07606]









[GN:BCGIB]









[OR:Bacillus coagulans]









[EC:3.1.21.-]









[DE:RESTRICTION ENZYME BGCI BETA SUBUNIT,]









[SP:Q07606]”


SPX1071
1071
3732
92
276


NO-HIT
6


SPX1072
1072
3733
83
249


NO-HIT
6


SPX1073
1073
3734
70
210


NO-HIT
6


SPX1074
1074
3735
560
1680
138
3.40E-35
[GI:6681569]
164









[LN:AB014436]









[AC:AB014436]









[PN:cassette chromosome recombinase B]









[GN:ccrB]









[OR:Staphylococcus aureus]









[SR:Staphylococcus aureus (strain:85/2082) DNA]


SPX1075
1075
3736
204
612


NO-HIT
6


SPX1076
1076
3737
63
189


NO-HIT
6


SPX1077
1077
3738
253
759


NO-HIT
6


SPX1078
1078
3739
285
855
70
4.40E-09
[GI:7020551]
129









[LN:AK000453]









[AC:AK000453]









[OR:Homo sapiens]









[SR:Homo sapiens signet-ring cell carcinoma cell_line:KATO III cDNA t]


SPX1079
1079
3740
295
885
192
4.90E-36
[LN:F69795]
97









[AC:F69795]









[PN:conserved hypothetical protein yerQ]









[GN:yerQ]









[OR:Bacillus subtilis]


SPX1080
1080
3741
93
279
124
1.30E-19
“[LN:JS0673]
127









[AC:JS0673]









[PN:neopullulanase,]









[CL:neopullulanase:alpha-amylase core homology]









[OR:Bacillus sp.]









[EC:3.2.1.135]”


SPX1081
1081
3742
485
1455
683
3.10E-176
“[LN:F70033]
156









[AC:F70033]









[PN:glucan 1,4-alpha-maltohydrolase homolog yvdF]









[GN:yvdF]









[CL:neopullulanase:alpha-amylase core homology]









[OR:Bacillus subtilis]”


SPX1082
1082
3743
101
303


NO-HIT
6


SPX1083
1083
3744
143
429
249
9.00E-30
[GI:6102604]
127









[LN:AF144880]









[AC:AF144880]









[PN:aminoglycoside 6′-N-acetyltransferase]









[GN:aac(6′)-Iy]









[OR:Salmonella enteritidis]


SPX1084
1084
3745
190
570


NO-HIT
6


SPX1085
1085
3746
71
213


NO-HIT
6


SPX1086
1086
3747
94
282


NO-HIT
6


SPX1087
1087
3748
65
195
184
8.80E-20
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX1088
1088
3749
410
1230
419
1.50E-74
[LN:FTSW_ENTHR]
114









[AC:Q47866]









[GN:FTSW]









[OR:Enterococcus hirae]









[DE:PROBABLE CELL DIVISION PROTEIN FTSW]









[SP:Q47866]


SPX1089
1089
3750
899
2697
418
1.60E-169
[GI:144985]
176









[LN:CORPEPC]









[AC:M25819]









[PN:phosphoenolpyruvate carboxylase]









[OR:Corynebacterium glutamicum]









[SR:Corynebacterium glutamicum (clone: pTG1200.) (tissue library: ATC]


SPX1090
1090
3751
102
306


NO-HIT
6


SPX1091
1091
3752
210
630
105
2.60E-05
[LN:H71693]
93









[AC:H71693]









[PN:hypothetical protein RP367]









[GN:RP367]









[OR:Rickettsia prowazekii]


SPX1092
1092
3753
223
669
163
6.00E-23
[LN:A71694]
93









[AC:A71694]









[PN:hypothetical protein RP368]









[GN:RP368]









[OR:Rickettsia prowazekii]


SPX1093
1093
3754
253
759
365
1.80E-45
[GI:1661179]
119









[LN:SMU75471]









[AC:U75471]









[PN:high affinity branched chain amino acid]









[GN:livG]









[OR:Streptococcus mutans]


SPX1094
1094
3755
64
192
82
2.10E-05
[LN:A71007]
95









[AC:A71007]









[PN:hypothetical protein PH1351]









[GN:PH1351]









[OR:Pyrococcus horikoshii]


SPX1095
1095
3756
592
1776
694
1.40E-161
“[LN:PRIM_LACLA]
150









[AC:Q04505]









[GN:DNAG:DNAE]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:2.7.7.-]









[DE:DNA PRIMASE,]









[SP:Q04505]”


SPX1096
1096
3757
305
915
1452
2.30E-194
[LN:RPOD_STRPN]
117









[AC:O08388]









[GN:RPOD]









[OR:Streptococcus pneumoniae]









[DE:RNA POLYMERASE SIGMA FACTOR RPOD]









[SP:O08388]


SPX1097
1097
3758
66
198
290
2.40E-35
[LN:RPOD_STRPN]
117









[AC:O08388]









[GN:RPOD]









[OR:Streptococcus pneumoniae]









[DE:RNA POLYMERASE SIGMA FACTOR RPOD]









[SP:O08388]


SPX1098
1098
3759
110
330
556
5.10E-73
[GI:2108332]
69









[LN:SPDNAGCPO]









[AC:Y11463]









[OR:Streptococcus pneumoniae]


SPX1099
1099
3760
69
207


NO-HIT
6


SPX1100
1100
3761
267
801
1357
1.40E-186
[GI:2108333]
79









[LN:SPDNAGCPO]









[AC:Y11463]









[GN:cpoA]









[OR:Streptococcus pneumoniae]


SPX1101
1101
3762
66
198
318
4.00E-38
[GI:2108333]
79









[LN:SPDNAGCPO]









[AC:Y11463]









[GN:cpoA]









[OR:Streptococcus pneumoniae]


SPX1102
1102
3763
442
1326
1475
1.70E-200
[GI:2108334]
69









[LN:SPDNAGCPO]









[AC:Y11463]









[OR:Streptococcus pneumoniae]


SPX1103
1103
3764
59
177
151
3.70E-16
[LN:B72287]
96









[AC:B72287]









[PN:conserved hypothetical protein]









[GN:TM1156]









[OR:Thermotoga maritima]


SPX1104
1104
3765
392
1176
1021
5.10E-184
[LN:OBG_BACSU]
112









[AC:P20964]









[GN:OBG]









[OR:Bacillus subtilis]









[DE:SPO0B-ASSOCIATED GTP-BINDING PROTEIN]









[SP:P20964]


SPX1105
1105
3766
420
1260
424
9.00E-142
[LN:MURA_BACSU]
140









[AC:P19670:Q03225]









[GN:MURA:MURZ]









[OR:Bacillus subtilis]









[EC:2.5.1.7]









[DE:ENOLPYRUVYL TRANSFERASE) (EPT)]









[SP:P19670:Q03225]


SPX1106
1106
3767
176
528
156
1.00E-17
[LN:C69895]
170









[AC:C69895]









[PN:conserved hypothetical protein yoaA]









[GN:yoaA]









[CL:Escherichia coli ribosomal-protein-alanine N-acetyltransferase rimJ]









[OR:Bacillus subtilis]


SPX1107
1107
3768
426
1278
425
4.20E-85
[LN:A69998]
87









[AC:A69998]









[PN:hypothetical protein ytoI]









[GN:ytoI]









[OR:Bacillus subtilis]


SPX1108
1108
3769
287
861
345
3.30E-65
“[LN:T44405]
158









[AC:T44405]









[PN:methionyl aminopeptidase, map [imported]]









[CL:Escherichia coli methionyl aminopeptidase]









[OR:Bacillus halodurans]









[EC:3.4.11.18]”


SPX1109
1109
3770
181
543
307
2.50E-38
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX1110
1110
3771
75
225
104
5.80E-08
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX1111
1111
3772
130
390
384
4.80E-49
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX1112
1112
3773
764
2292
1351
7.70E-282
[LN:E69794]
118









[AC:E69794]









[PN:ATP-dependent DNA helicase homolog yerF]









[GN:yerF]









[CL:helicase II]









[OR:Bacillus subtilis]


SPX1113
1113
3774
240
720
488
2.80E-62
[LN:RADC_BACSU]
116









[AC:Q02170]









[GN:YSXA]









[OR:Bacillus subtilis]









[DE:DNA REPAIR PROTEIN RADC HOMOLOG (ORFB)]









[SP:Q02170]


SPX1114
1114
3775
230
690
237
6.50E-27
“[LN:YDP3_LACLA]
162









[AC:P22347]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[DE:HYPOTHETICAL 18.7 KD PROTEIN IN PEPX 3′REGION (ORF3)]









[SP:P22347]”


SPX1115
1115
3776
214
642
339
2.60E-68
[LN:A69787]
87









[AC:A69787]









[PN:hypothetical protein ydiH]









[GN:ydiH]









[OR:Bacillus subtilis]


SPX1116
1116
3777
84
252


NO-HIT
6


SPX1117
1117
3778
116
348


NO-HIT
6


SPX1118
1118
3779
265
795
288
2.40E-63
[LN:E69981]
141









[AC:E69981]









[PN:iron-sulfur cofactor synthesis protein yrvO]









[GN:yrvO]









[CL:nitrogen fixation protein nifS]









[OR:Bacillus subtilis]


SPX1119
1119
3780
145
435
149
4.90E-18
[GI:2289093]
102









[LN:CAU76387]









[AC:U76387]









[PN:PRPP synthetase]









[GN:prs]









[OR:Corynebacterium ammoniagenes]


SPX1120
1120
3781
183
549
547
6.60E-75
[GI:2289093]
102









[LN:CAU76387]









[AC:U76387]









[PN:PRPP synthetase]









[GN:prs]









[OR:Corynebacterium ammoniagenes]


SPX1121
1121
3782
190
570
164
1.20E-26
[LN:C69844]
136









[AC:C69844]









[PN:hypothetical protein yjbK]









[GN:yjbK]









[CL:Bacillus subtilis hypothetical protein yjbK]









[OR:Bacillus subtilis]


SPX1122
1122
3783
168
504
338
6.80E-68
[LN:E69844]
139









[AC:E69844]









[PN:GTP pyrophosphokinase homolog yjbM]









[GN:yjbM]









[CL:GTP pyrophosphokinase related protein]









[OR:Bacillus subtilis]


SPX1123
1123
3784
71
213
90
6.20E-06
[LN:E69844]
139









[AC:E69844]









[PN:GTP pyrophosphokinase homolog yjbM]









[GN:yjbM]









[CL:GTP pyrophosphokinase related protein]









[OR:Bacillus subtilis]


SPX1124
1124
3785
263
789
309
4.70E-67
[LN:F69844]
140









[AC:F69844]









[PN:conserved hypothetical protein yjbN]









[GN:yjbN]









[CL:conserved hypothetical protein HI0072]









[OR:Bacillus subtilis]


SPX1125
1125
3786
299
897
286
3.40E-66
[LN:YJBO_BACSU]
137









[AC:O31613]









[GN:YJBO]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 31.5 KD PROTEIN IN MECA-TENA INTERGENIC REGION]









[SP:O31613]


SPX1126
1126
3787
325
975
867
5.10E-115
[LN:PTA_BACSU]
152









[AC:P39646]









[GN:PTA:IPA-88D]









[OR:Bacillus subtilis]









[EC:2.3.1.8]









[DE:(PHOSPHOTRANSACETYLASE) (VEGETATIVE PROTEIN 43) (VEG43)]









[SP:P39646]


SPX1127
1127
3788
79
237


NO-HIT
6


SPX1128
1128
3789
199
597
472
3.10E-122
[GI:663279]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX1129
1129
3790
109
327
280
2.00E-34
[GI:2804700]
87









[LN:AF030361]









[AC:AF030361]









[PN:transposase]









[OR:Streptococcus pneumoniae]


SPX1130
1130
3791
173
519
875
3.10E-119
[GI:663278]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX1131
1131
3792
108
324
190
3.90E-21
[LN:YAAK_BACSU]
137









[AC:P24281]









[GN:YAAK]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 11.8 KD PROTEIN IN DNAZ-RECR INTERGENIC REGION]









[SP:P24281]


SPX1132
1132
3793
231
693
89
1.90E-05
[LN:E69896]
87









[AC:E69896]









[PN:hypothetical protein yoaK]









[GN:yoaK]









[OR:Bacillus subtilis]


SPX1133
1133
3794
105
315
360
3.20E-44
[LN:RL21_BACSU]
110









[AC:P26908]









[GN:RPLU]









[OR:Bacillus subtilis]









[DE:50S RIBOSOMAL PROTEIN L21 (BL20)]









[SP:P26908]


SPX1134
1134
3795
147
441


NO-HIT
6


SPX1135
1135
3796
115
345
152
1.30E-22
[LN:YSXB_BACSU]
159









[AC:P26942:Q45629]









[GN:YSXB]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 12.3 KD PROTEIN IN RPLU-RPMA INTERGENIC REGION (ORF X)]









[SP:P26942:Q45629]


SPX1136
1136
3797
98
294
372
1.10E-46
[LN:RL27_BACSU]
117









[AC:P05657]









[GN:RPMA]









[OR:Bacillus subtilis]









[DE:50S RIBOSOMAL PROTEIN L27 (BL30) (BL24)]









[SP:P05657]


SPX1137
1137
3798
55
165
77
4.70E-09
[GI:1914870]
81









[LN:SPZ82001]









[AC:Z82001]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX1138
1138
3799
306
918
808
1.30E-107
[GI:2289231]
158









[LN:SAU92073]









[AC:U92073]









[PN:macrolide-efflux protein]









[GN:mreA]









[FN:resistance to 14- and 15-membered macrolides]









[OR:Streptococcus agalactiae]


SPX1139
1139
3800
283
849
531
2.80E-71
[LN:YPJC_BACSU]
142









[AC:P42978]









[GN:YPJC:JOJC]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 23.6 KD PROTEIN IN QCRC-DAPB INTERGENIC REGION]









[SP:P42978]


SPX1140
1140
3801
280
840
252
9.50E-36
[GI:671632]
86









[LN:SADIRED]









[AC:Z16422]









[PN:unknown]









[GN:ORF2]









[OR:Staphylococcus aureus]


SPX1141
1141
3802
92
276
397
9.60E-50
[GI:5209334]
112









[LN:L40356]









[AC:L40356]









[PN:histone-like DNA-binding protein]









[GN:hlpA]









[OR:Streptococcus gordonii]


SPX1142
1142
3803
634
1902
905
2.00E-202
[LN:YDIF_BACSU]
131









[AC:O05519]









[GN:YDIF]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL ABC TRANSPORTER ATP-BINDING PROTEIN YDIF]









[SP:O05519]


SPX1143
1143
3804
298
894
204
8.40E-33
[GI:4102023]
134









[LN:AF007761]









[AC:AF007761]









[PN:MutR]









[GN:mutR]









[FN:positive transcriptional regulator of mutA]









[OR:Streptococcus mutans]


SPX1144
1144
3805
393
1179
113
5.30E-22
[LN:H72265]
93









[AC:H72265]









[PN:hypothetical protein TM1336]









[GN:TM1336]









[OR:Thermotoga maritima]


SPX1145
1145
3806
656
1968
521
1.40E-217
“[LN:F69794]
140









[AC:F69794]









[PN:DNA ligase (NAD+),]









[GN:yerG]









[CL:polydeoxyribonucleotide synthase (NAD+)]









[OR:Bacillus subtilis]









[EC:6.5.1.2]”


SPX1146
1146
3807
760
2280
620
2.20E-109
[GI:3089609]
90









[LN:AF060205]









[AC:AF060205]









[PN:pullulanase]









[GN:pul]









[OR:Thermus sp. IM6501]


SPX1147
1147
3808
475
1425
1818
2.70E-245
[LN:GAPN_STRMU]
108









[AC:Q59931]









[GN:GAPN]









[OR:Streptococcus mutans]









[EC:1.2.1.9]









[DE:DEHYDROGENASE)]









[SP:Q59931]


SPX1148
1148
3809
643
1929
658
6.60E-176
“[LN:S18599]
177









[AC:S18599]









[PN:1,4-alpha-glucan branching enzyme,:glycogen branching enzyme]









[CL:1,4-alpha-glucan branching enzyme]









[OR:Bacillus stearothermophilus]









[EC:2.4.1.18]”


SPX1149
1149
3810
381
1143
187
6.00E-19
[LN:CCE277601]
105









[AC:AJ277601]









[PN:ADP-glucose pyrophosphorylase]









[GN:glgD]









[OR:Clostridium cellulolyticum]


SPX1150
1150
3811
380
1140
324
4.80E-53
[LN:GLGD_BACST]
122









[AC:O08327]









[GN:GLGD]









[OR:Bacillus stearothermophilus]









[DE:GLYCOGEN BIOSYNTHESIS PROTEIN GLGD]









[SP:O08327]


SPX1151
1151
3812
478
1434
813
6.80E-159
[LN:GLGA_BACSU]
101









[AC:P39125]









[GN:GLGA]









[OR:Bacillus subtilis]









[EC:2.4.1.21]









[DE:SYNTHASE)]









[SP:P39125]


SPX1152
1152
3813
124
372
214
7.80E-24
[LN:B69517]
97









[AC:B69517]









[PN:phosphoserine phosphatase (serB) homolog]









[OR:Archaeoglobus fulgidus]


SPX1153
1153
3814
110
330
213
6.30E-24
“[LN:A64499]
131









[AC:A64499]









[PN:phosphoserine phosphatase,]









[CL:phosphoserine phosphatase]









[OR:Methanococcus jannaschii]









[EC:3.1.3.3]”


SPX1154
1154
3815
372
1116
1670
1.30E-226
[GI:7380122]
125









[LN:NMA5Z2491]









[AC:AL162756:AL157959]









[PN:hypothetical protein NMA1473]









[GN:NMA1473]









[OR:Neisseria meningitidis]


SPX1155
1155
3816
149
447


NO-HIT
6


SPX1156
1156
3817
435
1305
2119
6.30E-286
[GI:5263171]
148









[LN:AB029313]









[AC:AB029313]









[PN:enolase]









[GN:eno]









[OR:Streptococcus intermedius]









[SR:Streptococcus intermedius (strain:ATCC 27335) DNA]


SPX1157
1157
3818
156
468
74
6.80E-09
“[LN:T45116]
113









[AC:T45116]









[PN:phosphopyruvate hydratase, [imported]]









[OR:Schizosaccharomyces pombe]









[EC:4.2.1.11]”


SPX1158
1158
3819
44
132
75
2.00E-06
[LN:B72477]
92









[AC:B72477]









[PN:hypothetical protein APE2459]









[GN:APE2459]









[OR:Aeropyrum pernix]


SPX1159
1159
3820
169
507
174
3.60E-16
[GI:6782411]
97









[LN:STH243106]









[AC:AJ243106]









[PN:integrase]









[GN:int]









[OR:Streptococcus thermophilus]


SPX1160
1160
3821
113
339
556
6.20E-74
[GI:5019553]
97









[LN:SPN239004]









[AC:AJ239004]









[PN:putative transposase]









[OR:Streptococcus pneumoniae]


SPX1161
1161
3822
116
348
573
1.80E-75
[GI:4200438]
96









[LN:AF026471]









[AC:AF026471]









[PN:putative transposase]









[OR:Streptococcus pneumoniae]


SPX1162
1162
3823
1092
3276
315
2.90E-101
[LN:T30307]
75









[AC:T30307]









[PN:rexB protein]









[GN:rexB]









[OR:Lactococcus lactis]


SPX1163
1163
3824
1217
3651
517
1.80E-246
[LN:T30308]
65









[AC:T30308]









[PN:rexA protein]









[OR:Lactococcus lactis]


SPX1164
1164
3825
79
237


NO-HIT
6


SPX1165
1165
3826
64
192
205
2.00E-24
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX1166
1166
3827
393
1179


NO-HIT
6


SPX1167
1167
3828
111
333


NO-HIT
6


SPX1168
1168
3829
1966
5898
7485
0
[GI:1213494]
149









[LN:SPU47687]









[AC:U47687]









[PN:immunoglobulin A1 protease]









[GN:iga]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae strain=R6]


SPX1169
1169
3830
76
228
138
8.00E-12
[GI:6911257]
115









[LN:AF221126]









[AC:AF221126]









[PN:putative zinc metalloprotease]









[GN:zmpB]









[OR:Streptococcus pneumoniae]


SPX1170
1170
3831
284
852
707
2.50E-96
[LN:F69880]
139









[AC:F69880]









[PN:conserved hypothetical protein ylqF]









[GN:ylqF]









[CL:conserved hypothetical protein MG442]









[OR:Bacillus subtilis]


SPX1171
1171
3832
260
780
615
3.40E-79
[LN:C69693]
101









[AC:C69693]









[PN:ribonuclease H rnh]









[GN:rnh]









[CL:ribonuclease HII]









[OR:Bacillus subtilis]


SPX1172
1172
3833
517
1551
261
1.40E-51
[LN:YADQ_ECOLI]
149









[AC:P37019:P77394]









[GN:YADQ]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 46.0 KD PROTEIN IN HEML-PFS INTERGENIC REGION]









[SP:P37019:P77394]


SPX1173
1173
3834
357
1071
1529
9.60E-206
[GI:3152920]
79









[LN:AF065141]









[AC:AF065141]









[PN:unknown]









[OR:Streptococcus mutans]


SPX1174
1174
3835
330
990
577
6.60E-108
[LN:G69830]
125









[AC:G69830]









[PN:lipoate-protein ligase homolog yhfJ]









[GN:yhfJ]









[CL:lipoate-protein ligase]









[OR:Bacillus subtilis]


SPX1175
1175
3836
568
1704
334
6.80E-104
[LN:I40794]
96









[AC:I40794]









[PN:dihydrolipoamide dehydrogenase]









[OR:Clostridium magnum]









[EC:1.8.1.4]


SPX1176
1176
3837
376
1128
366
8.20E-70
“[LN:I40793]
177









[AC:I40793]









[PN:dihydrolipoamide S-acetyltransferase,]









[CL:dihydrolipoamide acetyltransferase:lipoyl/biotin-binding homology]









[OR:Clostridium magnum]









[EC:2.3.1.12]”


SPX1177
1177
3838
331
993
550
5.00E-108
“[LN:I40791]
168









[AC:I40791]









[PN:acetoin dehydrogenase (TPP-dependent), beta chain]









[CL:pyruvate dehydrogenase (lipoamide) beta chain]









[OR:Clostridium magnum]









[EC:1.-.-.-]”


SPX1178
1178
3839
146
438


NO-HIT
6


SPX1179
1179
3840
104
312
136
6.90E-13
[LN:G72548]
92









[AC:G72548]









[PN:hypothetical protein APE1675]









[GN:APE1675]









[OR:Aeropyrum pernix]


SPX1180
1180
3841
323
969
554
6.20E-107
“[LN:I40790]
216









[AC:I40790]









[PN:acetoin dehydrogenase (TPP-dependent), alpha chain]









[CL:pyruvate dehydrogenase (lipoamide) alpha chain:thiamin pyrophosphate-binding domain homology]









[OR:Clostridium magnum]









[EC:1.-.-.-]”


SPX1181
1181
3842
454
1362
482
2.40E-117
[LN:F69906]
140









[AC:F69906]









[PN:conserved hypothetical protein yojI]









[GN:yojI]









[CL:conserved hypothetical protein HI1612]









[OR:Bacillus subtilis]


SPX1182
1182
3843
87
261


NO-HIT
6


SPX1183
1183
3844
423
1269
351
1.70E-86
“[LN:PYRC_LACLE]
125









[AC:P48795]









[GN:PYRC]









[OR:Lactobacillus leichmannii]









[EC:3.5.2.3]









[DE:DIHYDROOROTASE, (DHOASE)]









[SP:P48795]”


SPX1184
1184
3845
155
465
845
7.70E-113
“[LN:MUTX_STRPN]
144









[AC:P41354]









[GN:MUTX]









[OR:Streptococcus pneumoniae]









[EC:3.6.1.-]









[DE:(8-OXO-DGTPASE), (DGTP PYROPHOSPHOHYDROLASE)]









[SP:P41354]”


SPX1185
1185
3846
222
666
1123
8.50E-151
“[LN:UNG_STRPN]
127









[AC:P23379]









[GN:UNG]









[OR:Streptococcus pneumoniae]









[EC:3.2.2.-]









[DE:URACIL-DNA GLYCOSYLASE, (UDG)]









[SP:P23379]”


SPX1186
1186
3847
201
603


NO-HIT
6


SPX1187
1187
3848
238
714
260
5.40E-57
[LN:E69814]
153









[AC:E69814]









[PN:conserved hypothetical protein yfnB]









[GN:yfnB]









[CL:Alcaligenes eutrophus phosphoglycolate phosphatase]









[OR:Bacillus subtilis]


SPX1188
1188
3849
76
228
66
1.60E-05
[LN:H75623]
101









[AC:H75623]









[PN:conserved hypothetical protein]









[GN:DRB0052]









[OR:Deinococcus radiodurans]


SPX1189
1189
3850
852
2556
412
3.10E-104
[LN:T46758]
90









[AC:T46758]









[PN:hypothetical protein [imported]]









[OR:Streptococcus agalactiae]


SPX1190
1190
3851
830
2490
397
3.60E-100
[LN:T46758]
90









[AC:T46758]









[PN:hypothetical protein [imported]]









[OR:Streptococcus agalactiae]


SPX1191
1191
3852
411
1233
1763
4.80E-237
[GI:4958916]
169









[LN:AB027569]









[AC:AB027569]









[PN:phosphoenolpyruvate-protein phosphotransferase]









[GN:ptsI]









[OR:Streptococcus bovis]









[SR:Streptococcus bovis (strain:JB1) DNA]


SPX1192
1192
3853
46
138
144
1.50E-15
[LN:YKXH_BACSU]
132









[AC:P08876]









[GN:YKXH]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 7.4 KD PROTEIN IN PTSX OPERON (PROTEIN K)]









[SP:P08876]


SPX1193
1193
3854
88
264
402
2.30E-50
[LN:PTHP_STRMU]
138









[AC:P45596]









[GN:PTSH]









[OR:Streptococcus mutans]









[DE:PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN)]









[SP:P45596]


SPX1194
1194
3855
73
219
233
1.50E-27
“[LN:NRDH_LACLC]
154









[AC:Q48708]









[GN:NRDH]









[OR:Lactococcus lactis]









[SR:,subspcremoris:Streptococcus cremoris]









[DE:GLUTAREDOXIN-LIKE PROTEIN NRDH]









[SP:Q48708]”


SPX1195
1195
3856
720
2160
1042
2.20E-255
[GI:3077613]
125









[LN:CANRDFGEN]









[AC:Y09572]









[PN:ribonucleotide reductase subunit R1E]









[GN:nrdE]









[OR:Corynebacterium ammoniagenes]


SPX1196
1196
3857
63
189


NO-HIT
6


SPX1197
1197
3858
321
963
818
2.90E-116
[GI:3068719]
132









[LN:AF050168]









[AC:AF050168]









[PN:ribonucleoside diphosphate reductase small]









[GN:nrdF]









[OR:Corynebacterium ammoniagenes]


SPX1198
1198
3859
254
762
371
2.50E-80
“[LN:LACR_LACLA]
163









[AC:P18816]









[GN:LACR]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[DE:LACTOSE PHOSPHOTRANSFERASE SYSTEM REPRESSOR]









[SP:P18816]”


SPX1199
1199
3860
84
252


NO-HIT
6


SPX1200
1200
3861
472
1416
2452
0
“[LN:LACG_LACLA]
180









[AC:P11546]









[GN:LACG]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:3.2.1.85]









[DE:GALACTOHYDROLASE) (PGALASE) (P-BETA-GAL) (PBG)]









[SP:P11546]”


SPX1201
1201
3862
565
1695
1628
4.50E-299
“[LN:PTLB_LACLA]
157









[AC:P23531]









[GN:LACE]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:2.7.1.69]









[DE:(EC 2.7.1.69) (EII-LAC)]









[SP:P23531]”


SPX1202
1202
3863
106
318
454
2.90E-58
“[LN:PTLA_LACLA]
158









[AC:P23532]









[GN:LACF]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:2.7.1.69]









[DE:(EC 2.7.1.69) (EIII-LAC)]









[SP:P23532]”


SPX1203
1203
3864
279
837
487
1.40E-75
[LN:LACT_LACCA]
113









[AC:P24401]









[GN:LACT]









[OR:Lactobacillus casei]









[DE:TRANSCRIPTION ANTITERMINATOR LACT]









[SP:P24401]


SPX1204
1204
3865
270
810
1232
1.10E-164
“[LN:LACD_LACLA]
182









[AC:P26593]









[GN:LACD]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:4.1.2.40]









[DE:ALDOLASE) (D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE)]









[SP:P26593]”


SPX1205
1205
3866
273
819
810
9.10E-118
“[LN:LACC_LACLA]
185









[AC:P23391]









[GN:LACC]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:2.7.1.144]









[DE:TAGATOSE-6-PHOSPHATE KINASE, (PHOSPHOTAGATOKINASE)]









[SP:P23391]”


SPX1206
1206
3867
163
489


NO-HIT
6


SPX1207
1207
3868
172
516
810
5.00E-108
“[LN:LACB_LACLA]
179









[AC:P23495]









[GN:LACB]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:5.3.1.26]









[DE:GALACTOSE-6-PHOSPHATE ISOMERASE LACB SUBUNIT,]









[SP:P23495]”


SPX1208
1208
3869
142
426
612
2.90E-80
“[LN:LACA_LACLA]
179









[AC:P23494]









[GN:LACA]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:5.3.1.26]









[DE:GALACTOSE-6-PHOSPHATE ISOMERASE LACA SUBUNIT,]









[SP:P23494]”


SPX1209
1209
3870
97
291
57
0.00024
[GI:712785]
72









[LN:S74218]









[AC:S74218]









[GN:E9]









[OR:reindeer papillomavirus]


SPX1210
1210
3871
159
477
507
1.70E-65
“[LN:LAXP_LACLA]
141









[AC:P23496]









[GN:LACX]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[DE:LACX PROTEIN, PLASMID]









[SP:P23496]”””


SPX1211
1211
3872
207
621
374
1.20E-65
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX1212
1212
3873
107
321
193
4.90E-21
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX1213
1213
3874
101
303


NO-HIT
6


SPX1214
1214
3875
148
444
88
1.30E-10
“[GI:4512375]
181









[LN:AB011837]









[AC:AB011837]









[PN:phosphotransferase system (PTS)]









[GN:fruA]









[OR:Bacillus halodurans]









[SR:Bacillus halodurans (strain:C-125) DNA, clone_lib:lambda no.9]”


SPX1215
1215
3876
431
1293
2159
2.90E-302
[GI:2804700]
87









[LN:AF030361]









[AC:AF030361]









[PN:transposase]









[OR:Streptococcus pneumoniae]


SPX1216
1216
3877
63
189
120
2.10E-12
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX1217
1217
3878
417
1251
1395
2.00E-200
“[LN:THD1_LACLA]
144









[AC:Q02145]









[GN:ILVA]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:4.2.1.16]









[DE:DEAMINASE)]









[SP:Q02145]”


SPX1218
1218
3879
119
357


NO-HIT
6


SPX1219
1219
3880
78
234


NO-HIT
6


SPX1220
1220
3881
89
267


NO-HIT
6


SPX1221
1221
3882
341
1023
1329
9.50E-179
“[LN:ILVC_LACLA]
199









[AC:Q02138]









[GN:ILVC]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:1.1.1.86]









[DE:ISOMEROREDUCTASE) (ALPHA-KETO-BETA-HYDROXYLACIL REDUCTOISOMERASE)]









[SP:Q02138]”


SPX1222
1222
3883
167
501
477
4.10E-62
“[LN:ILVN_LACLA]
182









[AC:Q02140]









[GN:ILVN]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:4.1.3.18]









[DE:(ACETOHYDROXY-ACID SYNTHASE SMALL SUBUNIT) (ALS)]









[SP:Q02140]”


SPX1223
1223
3884
567
1701
1207
2.30E-266
“““[LN:ILVB_LACLA]
182









[AC:Q02137]









[GN:ILVB]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:4.1.3.18]









[DE:(ACETOHYDROXY-ACID SYNTHASE LARGE SUBUNIT) (ALS)]









[SP:Q02137]”


SPX1224
1224
3885
679
2037
565
7.80E-167
[LN:E69879]
151









[AC:E69879]









[PN:conserved hypothetical protein yloV]









[GN:yloV]









[CL:Mycoplasma genitalium hypothetical protein MG369]









[OR:Bacillus subtilis]


SPX1225
1225
3886
63
189
222
4.40E-26
[LN:RL28_BACSU]
103









[AC:P37807]









[GN:RPMB]









[OR:Bacillus subtilis]









[DE:50S RIBOSOMAL PROTEIN L28]









[SP:P37807]


SPX1226
1226
3887
82
246
123
5.10E-19
[GI:6760462]
100









[LN:AF224467]









[AC:AF224467]









[PN:putative glycosyl transferase]









[OR:Haemophilus ducreyi]


SPX1227
1227
3888
66
198
157
8.80E-16
[GI:6760462]
100









[LN:AF224467]









[AC:AF224467]









[PN:putative glycosyl transferase]









[OR:Haemophilus ducreyi]


SPX1228
1228
3889
515
1545
771
2.70E-216
[GI:3256222]
110









[LN:SAY14370]









[AC:Y14370]









[PN:peptide chain release factor 3]









[GN:RF3]









[OR:Staphylococcus aureus]


SPX1229
1229
3890
101
303
190
4.90E-21
[LN:A69795]
145









[AC:A69795]









[PN:conserved hypothetical protein yerL]









[GN:yerL]









[CL:probable glu-tRNA amidotransferase C chain]









[OR:Bacillus subtilis]


SPX1230
1230
3891
489
1467
1333
1.60E-186
[LN:B69795]
113









[AC:B69795]









[PN:amidase homolog yerM]









[GN:yerM]









[CL:indoleacetamide hydrolase]









[OR:Bacillus subtilis]


SPX1231
1231
3892
213
639
414
4.30E-94
[LN:T44293]
110









[AC:T44293]









[PN:hypothetical protein yerN [imported]]









[CL:PET112 protein]









[OR:Bacillus halodurans]


SPX1232
1232
3893
269
807
744
4.60E-97
[LN:C69795]
114









[AC:C69795]









[PN:pet112-like protein homolog yerN]









[GN:yerN]









[CL:PET112 protein]









[OR:Bacillus subtilis]


SPX1233
1233
3894
348
1044
719
1.70E-145
“[LN:H69789]
216









[AC:H69789]









[PN:L-iditol 2-dehydrogenase, homolog ydjL:sorbitol dehydrogenase homolog]









[GN:ydjL]









[CL:alcohol dehydrogenase:long-chain alcohol dehydrogenase homology]









[OR:Bacillus subtilis]









[EC:1.1.1.14]”


SPX1234
1234
3895
67
201
138
4.80E-14
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX1235
1235
3896
187
561
430
7.10E-54
[LN:EFP_BACSU]
102









[AC:P49778]









[GN:EFP]









[OR:Bacillus subtilis]









[DE:ELONGATION FACTOR P (EF-P)]









[SP:P49778]


SPX1236
1236
3897
130
390
139
8.30E-19
[LN:YQHY_BACSU]
137









[AC:P54519]









[GN:YQHY]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 14.7 KD PROTEIN IN ACCC-FOLD INTERGENIC REGION]









[SP:P54519]


SPX1237
1237
3898
141
423
105
1.00E-12
[GI:6580774]
137









[LN:AF088897]









[AC:AF088897:AF034613:AF086792:U63733]









[PN:N-utilization substance protein B]









[GN:nusB]









[OR:Zymomonas mobilis]


SPX1238
1238
3899
190
570
948
7.40E-131
[GI:663279]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX1239
1239
3900
261
783
1075
1.10E-148
[GI:2804700]
87









[LN:AF030361]









[AC:AF030361]









[PN:transposase]









[OR:Streptococcus pneumoniae]


SPX1240
1240
3901
278
834
80
9.90E-07
[LN:E69787]
87









[AC:E69787]









[PN:hypothetical protein ydiL]









[GN:ydiL]









[OR:Bacillus subtilis]


SPX1241
1241
3902
84
252


NO-HIT
6


SPX1242
1242
3903
256
768
653
4.10E-90
[GI:285621]
155









[LN:BACPK]









[AC:D13095]









[PN:undefined open reading frame]









[OR:Bacillus stearothermophilus]









[SR:Bacillus stearothermophilus (strain:NCA1503) DNA]


SPX1243
1243
3904
288
864
602
2.20E-92
“[LN:ACCD_SYNP7]
168









[AC:Q54776]









[GN:ACCD]









[OR:Synechococcus sp]









[SR:,strain PCC 7942:Anacystis nidulans R2]









[EC:6.4.1.2]









[DE:(EC 6.4.1.2) (ACCASE BETA CHAIN)]









[SP:Q54776]”


SPX1244
1244
3905
456
1368
1101
1.50E-181
[LN:A69581]
170









[AC:A69581]









[PN:acetyl-CoA carboxylase (biotin carboxylase subunit) accC]









[GN:accC]









[CL:biotin carboxylase:biotin carboxylase homology]









[OR:Bacillus subtilis]


SPX1245
1245
3906
141
423
299
1.60E-49
“[LN:D70065]
201









[AC:D70065]









[PN:(3R)-hydroxymyristoyl-[acyl carrier protein]









dehydratase, ywpB]









[GN:ywpB]









[CL:(3R)-hydroxymyristoyl-[acyl carrier protein]









dehydratase]









[OR:Bacillus subtilis]









[EC:4.2.1.-]”


SPX1246
1246
3907
162
486
248
1.10E-34
“[LN:C75558]
195









[AC:C75558]









[PN:acetyl-CoA carboxylase, bitoin carboxyl carrier protein]









[GN:DR0118]









[CL:biotin carboxyl carrier protein:lipoyl/biotin-binding homology]









[OR:Deinococcus radiodurans]”


SPX1247
1247
3908
93
279
134
1.30E-13
[LN:FAB2_MYCTU]
152









[AC:Q10525]









[GN:RV2246:MTCY427.27]









[OR:Mycobacterium tuberculosis]









[EC:2.3.1.41]









[DE:(BETA-KETOACYL-ACP SYNTHASE 2) (KAS 2)]









[SP:Q10525]


SPX1248
1248
3909
360
1080
477
2.60E-113
“[LN:S77464]
237









[AC:S77464]









[PN:3-oxoacyl-[acyl-carrier-protein]









synthase, beta chain:beta ketoacyl-acyl carrier protein synthase:protein sll1069:beta ketoacyl-acyl carrier protein synthase:protein sll1069]









[GN:fabF]









[OR:Synechocystis sp.]”


SPX1249
1249
3910
244
732
482
2.10E-76
[LN:FABG_CUPLA]
138









[AC:P28643]









[GN:CLKR27]









[OR:Cuphea lanceolata]









[EC:1.1.1.100]









[DE:(3-KETOACYL-ACYL CARRIER PROTEIN REDUCTASE)]









[SP:P28643]


SPX1250
1250
3911
74
222
81
9.50E-05
[LN:H72482]
92









[AC:H72482]









[PN:hypothetical protein APE2504]









[GN:APE2504]









[OR:Aeropyrum pernix]


SPX1251
1251
3912
307
921
374
1.00E-85
“[LN:B41856]
249









[AC:B41856:A42147:S20443:A64853]









[PN:[acyl-carrier-protein]









S-malonyltransferase,]









[GN:fabD:tfpA]









[CL:[acyl-carrier-protein]









S-malonyltransferase:[acyl-carrier-protein]









S-malonyltransferase homology]









[OR:Escherichia coli]









[EC:2.3.1.39]”


SPX1252
1252
3913
325
975
681
5.90E-101
[LN:A72335]
96









[AC:A72335]









[PN:conserved hypothetical protein]









[GN:TM0800]









[OR:Thermotoga maritima]


SPX1253
1253
3914
75
225
80
1.80E-12
[LN:ACP_BACSU]
122









[AC:P80643:P51832]









[GN:ACPA:ACPP]









[OR:Bacillus subtilis]









[DE:ACYL CARRIER PROTEIN (ACP)]









[SP:P80643:P51832]


SPX1254
1254
3915
189
567
202
6.90E-38
“[LN:S75457]
236









[AC:S75457]









[PN:beta-ketoacyl-acyl carrier protein synthase III:protein slr1511:protein slr1511]









[GN:fabH]









[CL:3-oxoacyl-[acyl-carrier-protein]









synthase III]









[OR:Synechocystis sp.]









[SR:PCC 6803, , PCC 6803]









[SR:PCC 6803, ]”


SPX1255
1255
3916
140
420
269
1.30E-46
[GI:7416010]
177









[LN:AB025973]









[AC:AB025973]









[PN:3-oxoacyl-[acyl-carrier-protein]









synthase III]









[GN:accS]









[OR:Lactobacillus plantarum]









[SR:Lactobacillus plantarum (strain:L137) DNA]


SPX1256
1256
3917
66
198


NO-HIT
6


SPX1257
1257
3918
145
435
139
5.00E-12
[GI:4139249]
84









[LN:AF110185]









[AC:AF110185]









[PN:unknown]









[OR:Burkholderia pseudomallei]


SPX1258
1258
3919
66
198


NO-HIT
6


SPX1259
1259
3920
98
294
138
7.10E-13
[GI:3253198]
91









[LN:AF029714]









[AC:AF029714:Z71175]









[PN:PhaB]









[GN:phaB]









[OR:Pseudomonas putida]


SPX1260
1260
3921
76
228
156
9.00E-18
[GI:1914870]
81









[LN:SPZ82001]









[AC:Z82001]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX1261
1261
3922
455
1365
1240
6.10E-166
[LN:A69763]
147









[AC:A69763]









[PN:homoserine dehydrogenase homolog yclM]









[GN:yclM]









[CL:aspartate kinase:aspartate kinase homology]









[OR:Bacillus subtilis]


SPX1262
1262
3923
124
372
493
2.80E-64
[GI:5669858]
93









[LN:AF130465]









[AC:AF130465]









[PN:unknown]









[GN:manO]









[OR:Streptococcus salivarius]


SPX1263
1263
3924
375
1125
564
8.90E-141
“[LN:SYS_BACSU]
145









[AC:P37464]









[GN:SERS]









[OR:Bacillus subtilis]









[EC:6.1.1.11]









[DE:SERYL-TRNA SYNTHETASE, (SERINE--TRNA LIGASE) (SERRS)]









[SP:P37464]”


SPX1264
1264
3925
91
273
101
6.30E-08
“[LN:SYS_MYCGE]
155









[AC:P47251]









[GN:SERS:MG005]









[OR:Mycoplasma genitalium]









[EC:6.1.1.11]









[DE:SERYL-TRNA SYNTHETASE, (SERINE--TRNA LIGASE) (SERRS)]









[SP:P47251]”


SPX1265
1265
3926
304
912


NO-HIT
6


SPX1266
1266
3927
69
207


NO-HIT
6


SPX1267
1267
3928
183
549
217
2.40E-57
[GI:7379894]
125









[LN:NMA4Z2491]









[AC:AL162755:AL157959]









[PN:hypothetical protein NMA1203]









[GN:NMA1203]









[OR:Neisseria meningitidis]


SPX1268
1268
3929
441
1323
611
6.80E-118
“[LN:D71327]
210









[AC:D71327]









[PN:probable D-alanine glycine permease (dagA)]









[GN:TP0414]









[CL:sodium-dependent D-alanine/glycine transport protein]









[OR:Treponema pallidum subsp. pallidum]









[SR:, syphilis spirochete]”


SPX1269
1269
3930
779
2337
671
5.70E-155
[LN:MUS2_BACSU]
92









[AC:P94545]









[GN:MUTS2]









[OR:Bacillus subtilis]









[DE:MUTS2 PROTEIN]









[SP:P94545]


SPX1270
1270
3931
251
753
175
7.10E-43
[GI:6746427]
90









[LN:AF179847]









[AC:AF179847]









[PN:putative transposase]









[OR:Lactococcus lactis]


SPX1271
1271
3932
65
195


NO-HIT
6


SPX1272
1272
3933
182
546
107
1.20E-15
[GI:3849798]
118









[LN:U91581]









[AC:U91581:U04057]









[PN:putative transposase]









[GN:tpase]









[OR:Lactococcus lactis subsp. lactis]


SPX1273
1273
3934
183
549
95
4.30E-13
[LN:B69985]
87









[AC:B69985]









[PN:hypothetical protein yshB]









[GN:yshB]









[OR:Bacillus subtilis]


SPX1274
1274
3935
104
312


NO-HIT
6


SPX1275
1275
3936
294
882
1444
8.00E-194
“[LN:RNH2_STRPN]
130









[AC:O07874]









[GN:RNHB]









[OR:Streptococcus pneumoniae]









[EC:3.1.26.4]









[DE:RIBONUCLEASE HII, (RNASE HII)]









[SP:O07874]”


SPX1276
1276
3937
205
615
1065
6.70E-145
“[LN:LEP_STRPN]
155









[AC:O07344]









[GN:LEPB:SPI]









[OR:Streptococcus pneumoniae]









[EC:3.4.21.89]









[DE:SIGNAL PEPTIDASE I, (SPASE I) (LEADER PEPTIDASE I)]









[SP:O07344]”


SPX1277
1277
3938
93
279


NO-HIT
6


SPX1278
1278
3939
789
2367
738
5.80E-165
[LN:A69979]
103









[AC:A69979]









[PN:conjugation transfer protein homolog yrrC]









[GN:yrrC]









[OR:Bacillus subtilis]


SPX1279
1279
3940
428
1284
1691
1.40E-223
[GI:3549287]
88









[LN:AF073922]









[AC:AF073922]









[PN:RopA]









[GN:ropA]









[OR:Streptococcus pyogenes]


SPX1280
1280
3941
379
1137
1350
2.20E-182
“[LN:MTLD_STRMU]
134









[AC:Q02418]









[GN:MTLD]









[OR:Streptococcus mutans]









[EC:1.1.1.17]









[DE:MANNITOL-1-PHOSPHATE 5-DEHYDROGENASE,]









[SP:Q02418]”


SPX1281
1281
3942
146
438
544
5.30E-71
[LN:PTMA_STRMU]
119









[AC:Q02420]









[GN:MTLF]









[OR:Streptococcus mutans]









[EC:2.7.1.69]









[DE:(EC 2.7.1.69) (EIII-MTL)]









[SP:Q02420]


SPX1282
1282
3943
652
1956
392
1.00E-47
[LN:YMTF_STRMU]
126









[AC:Q02425]









[OR:Streptococcus mutans]









[DE:HYPOTHETICAL PROTEIN IN MTLF 5′REGION (ORFX) (FRAGMENT)]









[SP:Q02425]


SPX1283
1283
3944
596
1788
1099
4.90E-194
[LN:PTMB_BACST]
125









[AC:P50852]









[GN:MTLA]









[OR:Bacillus stearothermophilus]









[EC:2.7.1.69]









[DE:(EC 2.7.1.69) (EII-MTL)]









[SP:P50852]


SPX1284
1284
3945
67
201


NO-HIT
6


SPX1285
1285
3946
191
573
422
2.30E-53
[LN:B30868]
81









[AC:B30868]









[PN:hypothetical protein 1]









[OR:Streptococcus agalactiae]


SPX1286
1286
3947
278
834
582
1.50E-140
[LN:A33595]
107









[AC:A33595:A30868]









[PN:probable transposase]









[CL:transposase IS3]









[OR:Streptococcus agalactiae]


SPX1287
1287
3948
341
1023
1142
5.00E-219
[GI:1914875]
101









[LN:SPZ82002]









[AC:Z82002]









[PN:PCPC]









[GN:pcpC]









[FN:unknown]









[OR:Streptococcus pneumoniae]


SPX1288
1288
3949
98
294
194
3.40E-25
[GI:4586910]
161









[LN:AB017447]









[AC:AB017447]









[PN:protective antigen SpaA.1]









[OR:Erysipelothrix rhusiopathiae]









[SR:Erysipelothrix rhusiopathiae (strain:Fujisawa) DNA]


SPX1289
1289
3950
219
657
104
1.50E-08
[LN:S25140]
119









[AC:S25140]









[PN:serine proteinase homolog]









[CL:staphylococcal serine proteinase]









[OR:Enterococcus faecalis]


SPX1290
1290
3951
80
240
296
8.20E-35
[GI:1914874]
81









[LN:SPZ82002]









[AC:Z82002]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX1291
1291
3952
91
273
146
3.20E-14
[GI:4584089]
155









[LN:BAJ10128]









[AC:AJ010128]









[PN:DNA alkylation repair enzyme]









[GN:alkD]









[FN:complements DNA alkylation repair deficiency]









[OR:Bacillus cereus]


SPX1292
1292
3953
85
255
102
2.90E-08
[GI:4584089]
155









[LN:BAJ10128]









[AC:AJ010128]









[PN:DNA alkylation repair enzyme]









[GN:alkD]









[FN:complements DNA alkylation repair deficiency]









[OR:Bacillus cereus]


SPX1293
1293
3954
211
633
1040
1.50E-139
[GI:5830527]
104









[LN:SPAJ6393]









[AC:AJ006393]









[PN:response regulator]









[GN:rr03]









[OR:Streptococcus pneumoniae]


SPX1294
1294
3955
332
996
1603
3.60E-220
[GI:5830526]
102









[LN:SPAJ6393]









[AC:AJ006393]









[PN:histidine kinase]









[GN:hk03]









[OR:Streptococcus pneumoniae]


SPX1295
1295
3956
233
699
104
1.50E-11
[LN:G70045]
87









[AC:G70045]









[PN:hypothetical protein yvqF]









[GN:yvqF]









[OR:Bacillus subtilis]


SPX1296
1296
3957
337
1011
151
6.20E-42
[LN:D75084]
162









[AC:D75084]









[PN:carotenoid biosynthetic gene erwcrts related PAB1662]









[GN:PAB1662]









[CL:carotenoid biosynthesis protein homolog]









[OR:Pyrococcus abyssi]


SPX1297
1297
3958
336
1008
67
0.00053
“[LN:KIME_METJA]
126









[AC:Q58487]









[GN:MJ1087]









[OR:Methanococcus jannaschii]









[EC:2.7.1.36]









[DE:MEVALONATE KINASE, (MK)]









[SP:Q58487]”


SPX1298
1298
3959
345
1035
141
5.90E-28
[GI:6625790]
116









[LN:AF203779]









[AC:AF203779]









[PN:diphosphomevalonate decarboxylase MVD1]









[GN:MVD1]









[OR:Candida albicans]


SPX1299
1299
3960
293
879
134
1.60E-20
[LN:F72474]
98









[AC:F72474]









[PN:probable mevalonate kinase APE2439]









[GN:APE2439]









[OR:Aeropyrum pernix]


SPX1300
1300
3961
110
330
193
8.50E-21
[GI:1914875]
101









[LN:SPZ82002]









[AC:Z82002]









[PN:PCPC]









[GN:pcpC]









[FN:unknown]









[OR:Streptococcus pneumoniae]


SPX1301
1301
3962
292
876


NO-HIT
6


SPX1302
1302
3963
411
1233
97
4.90E-10
[GI:3582221]
114









[LN:AE001272]









[AC:AE001272]









[PN:conserved hypothetical protein]









[GN:ORF00049]









[OR:Lactococcus lactis]


SPX1303
1303
3964
333
999
402
1.50E-124
[GI:1914875]
101









[LN:SPZ82002]









[AC:Z82002]









[PN:PCPC]









[GN:pcpC]









[FN:unknown]









[OR:Streptococcus pneumoniae]


SPX1304
1304
3965
371
1113
289
1.70E-89
[GI:1914875]
101









[LN:SPZ82002]









[AC:Z82002]









[PN:PCPC]









[GN:pcpC]









[FN:unknown]









[OR:Streptococcus pneumoniae]


SPX1305
1305
3966
230
690
212
7.30E-56
[GI:3599371]
139









[LN:AF082668]









[AC:AF082668]









[PN:CsrR]









[GN:csrR]









[FN:negative regulator of hyaluronic acid capsule]









[OR:Streptococcus pyogenes]


SPX1306
1306
3967
458
1374
801
5.10E-226
[GI:3033358]
100









[LN:LLU74322]









[AC:U74322]









[PN:6-phosphogluconate dehydrogenase]









[OR:Lactococcus lactis]


SPX1307
1307
3968
465
1395
109
1.10E-06
[GI:1684847]
78









[LN:HSU77718]









[AC:U77718]









[PN:pinin]









[OR:Homo sapiens]









[SR:human]


SPX1308
1308
3969
386
1158
678
1.20E-133
[LN:YPSC_BACSU]
147









[AC:P50840]









[GN:YPSC]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 43.5 KD PROTEIN IN COTD-KDUD INTERGENIC REGION PRECURSOR]









[SP:P50840]


SPX1309
1309
3970
110
330
166
6.70E-18
[LN:YPSB_BACSU]
137









[AC:P50839]









[GN:YPSB]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 11.6 KD PROTEIN IN COTD-KDUD INTERGENIC REGION]









[SP:P50839]


SPX1310
1310
3971
176
528
147
8.20E-19
[LN:YPSA_BACSU]
137









[AC:P50838]









[GN:YPSA]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 21.1 KD PROTEIN IN COTD-KDUD INTERGENIC REGION]









[SP:P50838]


SPX1311
1311
3972
199
597
1043
3.40E-141
[LN:YPOA_STRPN]
120









[AC:P38034]









[OR:Streptococcus pneumoniae]









[DE:HYPOTHETICAL 23.1 KD PROTEIN IN PONA 5′REGION]









[SP:P38034]


SPX1312
1312
3973
720
2160
3734
0
[GI:6563337]
116









[LN:AF210745]









[AC:AF210745]









[PN:penicillin-binding protein 1A]









[GN:pbp1a]









[OR:Streptococcus pneumoniae]


SPX1313
1313
3974
68
204


NO-HIT
6


SPX1314
1314
3975
1768
5304
1762
9.10E-232
[GI:1658320]
77









[LN:SPDEXCAP]









[AC:Z47210]









[GN:orf]









[OR:Streptococcus pneumoniae]


SPX1315
1315
3976
661
1983
3378
0
LN:ALIA_STRPN]
201









[AC:P35592:Q54782:O54620:O52228]









[GN:ALIA:EXP1:PLPA]









[OR:Streptococcus pneumoniae]









[DE:OLIGOPEPTIDE-BINDING PROTEIN ALIA PRECURSOR (EXPORTED PROTEIN 1)]









[SP:P35592:Q54782:O54620:O52228]


SPX1316
1316
3977
78
234
87
0.00034
“[GI:5824139]
137









[LN:POL245436]









[AC:AJ245436:J04618:J04619:S50571:X52935:X65936]









[PN:hypothetical protein, 57.8 kD]









[OR:Pseudomonas putida]”


SPX1317
1317
3978
150
450
94
3.20E-15
“[LN:Y4HP_RHISN]
128









[AC:P50360]









[GN:Y4HP]









[OR:Rhizobium sp]









[SR:,strain NGR234]









[DE:HYPOTHETICAL 61.7 KD PROTEIN Y4HP]









[SP:P50360]”


SPX1318
1318
3979
58
174


NO-HIT
6


SPX1319
1319
3980
86
258
80
8.90E-06
“[LN:Y4HP_RHISN]
128









[AC:P50360]









[GN:Y4HP]









[OR:Rhizobium sp]









[SR:,strain NGR234]









[DE:HYPOTHETICAL 61.7 KD PROTEIN Y4HP]









[SP:P50360]”


SPX1320
1320
3981
143
429
84
9.20E-08
“[GI:6009407]
140









[LN:AB024946]









[AC:AB024946]









[GN:orf31]









[OR:Escherichia coli]









[SR:Escherichia coli (sub_species:enteropathogenic, strain:B171]”


SPX1321
1321
3982
284
852
1480
1.00E-198
[GI:2804705]
110









[LN:AF030362]









[AC:AF030362]









[PN:dTDP-L-rhamnose synthase]









[GN:cpsO]









[OR:Streptococcus pneumoniae]


SPX1322
1322
3983
350
1050
1853
2.90E-249
[GI:4200435]
92









[LN:AF026471]









[AC:AF026471]









[PN:Cps2N]









[GN:cps2N]









[OR:Streptococcus pneumoniae]


SPX1323
1323
3984
199
597
1027
4.50E-137
“[GI:3907611]
131









[LN:AF094575]









[AC:AF094575]









[PN:dTDP-4-keto-6-deoxyglucose-3,5-epimerase]









[GN:cps19aM]









[OR:Streptococcus pneumoniae]”


SPX1324
1324
3985
290
870
1430
7.20E-193
[GI:4406249]
131









[LN:AF105113]









[AC:AF105113]









[PN:glucose-1-phosphate thymidylyl transferase]









[GN:cps19AL]









[OR:Streptococcus pneumoniae]


SPX1325
1325
3986
476
1428
2017
3.10E-287
[GI:3907608]
129









[LN:AF094575]









[AC:AF094575]









[PN:putative repeat unit transporter Cps19aJ]









[GN:cps19aJ]









[OR:Streptococcus pneumoniae]


SPX1326
1326
3987
95
285


NO-HIT
6


SPX1327
1327
3988
448
1344
148
6.90E-31
[GI:3907607]
122









[LN:AF094575]









[AC:AF094575]









[PN:polysaccharide polymerase Cps19aI]









[GN:cps19aI]









[OR:Streptococcus pneumoniae]


SPX1328
1328
3989
329
987
178
2.00E-31
[LN:T00087]
86









[AC:T00087]









[PN:rhamnosyltransferase]









[GN:rgpBc]









[OR:Streptococcus mutans]


SPX1329
1329
3990
242
726
93
1.90E-06
[LN:T35395]
92









[AC:T35395]









[PN:probable transferase]









[GN:SC6A5.04]









[OR:Streptomyces coelicolor]


SPX1330
1330
3991
186
558
154
3.00E-14
[GI:2209209]
96









[LN:AF004325]









[AC:AF004325]









[PN:unknown]









[GN:cps19bG]









[OR:Streptococcus pneumoniae]


SPX1331
1331
3992
315
945
96
6.50E-16
[GI:3132871]
104









[LN:AF019375]









[AC:AF019375]









[PN:UDP-glucose:(glucosyl) LPS]









[GN:waaR]









[OR:Escherichia coli]


SPX1332
1332
3993
456
1368
1141
0
[GI:3907603]
129









[LN:AF094575]









[AC:AF094575]









[PN:glucosyl-1-phosphate transferase Cps19aE]









[GN:cps19aE]









[OR:Streptococcus pneumoniae]


SPX1333
1333
3994
227
681
1055
4.60E-145
[GI:3907602]
136









[LN:AF094575]









[AC:AF094575]









[PN:Cps19aD]









[GN:cps19aD]









[FN:chain length regulation and export]









[OR:Streptococcus pneumoniae]


SPX1334
1334
3995
232
696
1061
2.00E-141
[GI:3907601]
136









[LN:AF094575]









[AC:AF094575]









[PN:Cps19aC]









[GN:cps19aC]









[FN:chain length regulation and export]









[OR:Streptococcus pneumoniae]


SPX1335
1335
3996
260
780
1195
2.90E-162
[GI:3907600]
96









[LN:AF094575]









[AC:AF094575]









[PN:Cps19aB]









[GN:cps19aB]









[OR:Streptococcus pneumoniae]


SPX1336
1336
3997
485
1455
2238
0
[GI:3550627]
83









[LN:SPAJ6986]









[AC:AJ006986]









[GN:cap33fA]









[OR:Streptococcus pneumoniae]


SPX1337
1337
3998
358
1074
1690
9.20E-228
[LN:TRA2_STRPN]
116









[AC:Q54513]









[OR:Streptococcus pneumoniae]









[DE:TRANSPOSASE FOR INSERTION SEQUENCE IS1202]









[SP:Q54513]


SPX1338
1338
3999
120
360
581
6.60E-75
[LN:TRA2_STRPN]
116









[AC:Q54513]









[OR:Streptococcus pneumoniae]









[DE:TRANSPOSASE FOR INSERTION SEQUENCE IS1202]









[SP:Q54513]


SPX1339
1339
4000
317
951
267
3.80E-61
“““[GI:6332767]
194









[LN:AB033763]









[AC:AB033763:AB014419:AB014429:AB014439]









[PN:hypothetical protein]









[OR:Staphylococcus aureus]









[SR:Staphylococcus aureus (strain:NCTC10442) DNA, clone_lib:Lambda das]”””


SPX1340
1340
4001
179
537
551
1.10E-70
[LN:B30868]
81









[AC:B30868]









[PN:hypothetical protein 1]









[OR:Streptococcus agalactiae]


SPX1341
1341
4002
161
483
550
2.00E-80
[LN:A33595]
107









[AC:A33595:A30868]









[PN:probable transposase]









[CL:transposase IS3]









[OR:Streptococcus agalactiae]


SPX1342
1342
4003
278
834
587
1.60E-140
[LN:A33595]
107









[AC:A33595:A30868]









[PN:probable transposase]









[CL:transposase IS3]









[OR:Streptococcus agalactiae]


SPX1343
1343
4004
537
1611
2499
0
“[GI:3320387]
110









[LN:AF030373]









[AC:AF030373]









[PN:alpha, 1-6-glucosidase]









[GN:dexB]









[OR:Streptococcus pneumoniae]”


SPX1344
1344
4005
495
1485


NO-HIT
6


SPX1345
1345
4006
161
483
288
9.40E-46
[LN:D75280]
143









[AC:D75280]









[PN:conserved hypothetical protein]









[GN:DR2387]









[CL:conserved hypothetical protein HI0491]









[OR:Deinococcus radiodurans]


SPX1346
1346
4007
702
2106
2049
0
[GI:871784]
147









[LN:BOVCLPAB]









[AC:L34677]









[PN:Clp-like ATP-dependent protease binding subunit]









[OR:Bos taurus]









[SR:Bos taurus calf thymus cDNA to mRNA]


SPX1347
1347
4008
80
240


NO-HIT
6


SPX1348
1348
4009
327
981
1619
8.40E-229
[GI:4009489]
132









[LN:AF068903]









[AC:AF068903]









[PN:undecaprenyl-phosphate-UDP-MurNAc-pentapeptide]









[GN:mraY]









[OR:Streptococcus pneumoniae]


SPX1349
1349
4010
751
2253
3812
0
[LN:PBPX_STRPN]
131









[AC:P14677]









[GN:PBPX]









[OR:Streptococcus pneumoniae]









[DE:PENICILLIN-BINDING PROTEIN 2X (PBP-2X) (PBP2X)]









[SP:P14677]


SPX1350
1350
4011
106
318
505
1.40E-65
[GI:4009487]
90









[LN:AF068903]









[AC:AF068903]









[PN:YllD]









[GN:yllD]









[OR:Streptococcus pneumoniae]


SPX1351
1351
4012
317
951
1604
2.70E-217
[GI:4009486]
90









[LN:AF068903]









[AC:AF068903]









[PN:YllC]









[GN:yllC]









[OR:Streptococcus pneumoniae]


SPX1352
1352
4013
65
195
323
1.20E-40
[GI:1536960]
115









[LN:SOORFS]









[AC:Z79691]









[GN:yorfE]









[FN:putative transcription regulator]









[OR:Streptococcus pneumoniae]


SPX1353
1353
4014
142
426
291
1.40E-36
[GI:1524349]
87









[LN:SOORFS]









[AC:Z79691]









[PN:OrfC]









[GN:yorfC]









[OR:Streptococcus pneumoniae]


SPX1354
1354
4015
94
282


NO-HIT
6


SPX1355
1355
4016
85
255
178
5.70E-20
[GI:1536959]
87









[LN:SOORFS]









[AC:Z79691]









[PN:OrfB]









[GN:yorfb]









[OR:Streptococcus pneumoniae]


SPX1356
1356
4017
81
243
391
2.00E-51
[GI:1536959]
87









[LN:SOORFS]









[AC:Z79691]









[PN:OrfB]









[GN:yorfb]









[OR:Streptococcus pneumoniae]


SPX1357
1357
4018
112
336
219
4.90E-27
[GI:1536959]
87









[LN:SOORFS]









[AC:Z79691]









[PN:OrfB]









[GN:yorfb]









[OR:Streptococcus pneumoniae]


SPX1358
1358
4019
64
192
111
4.30E-10
[GI:1536959]
87









[LN:SOORFS]









[AC:Z79691]









[PN:OrfB]









[GN:yorfb]









[OR:Streptococcus pneumoniae]


SPX1359
1359
4020
334
1002
1703
2.00E-229
“[GI:1536958]
139









[LN:SOORFS]









[AC:Z79691]









[PN:RegR]









[GN:regR]









[FN:putative transcription regulator, member GalR]









[OR:Streptococcus pneumoniae]”


SPX1360
1360
4021
634
1902
1094
3.90E-148
[GI:1524347]
87









[LN:SOORFS]









[AC:Z79691]









[PN:OrfA]









[GN:yorfA]









[OR:Streptococcus pneumoniae]


SPX1361
1361
4022
98
294
96
7.80E-07
[LN:D70408]
120









[AC:D70408]









[PN:conserved hypothetical protein aq_1254]









[GN:aq_1254]









[CL:yajC protein]









[OR:Aquifex aeolicus]


SPX1362
1362
4023
273
819
268
3.50E-51
“[LN:PTPD_ECOLI]
102









[AC:P42911]









[GN:AGAD]









[OR:Escherichia coli]









[DE:ENZYME II, D COMPONENT)]









[SP:P42911]”


SPX1363
1363
4024
260
780
170
4.30E-27
[GI:1732200]
115









[LN:VFU65015]









[AC:U65015]









[PN:PTS permease for mannose subunit IIPMan]









[GN:manY]









[OR:Vibrio furnissii]


SPX1364
1364
4025
164
492
286
3.40E-44
“[LN:PTPV_ECOLI]
133









[AC:P42904:P76669]









[GN:AGAV]









[OR:Escherichia coli]









[EC:2.7.1.69]









[DE:ENZYME II, B COMPONENT 2),]









[SP:P42904:P76669]”


SPX1365
1365
4026
336
1008
475
2.70E-95
[GI:5869507]
148









[LN:AB019619]









[AC:AB019619]









[PN:unsaturated glucuronyl hydrolase]









[GN:ugl]









[OR:Bacillus sp. GL1]









[SR:Bacillus sp. GL1 (strain:GL1) DNA]


SPX1366
1366
4027
146
438


NO-HIT
6


SPX1367
1367
4028
145
435
129
3.30E-17
[GI:5669855]
128









[LN:AF130465]









[AC:AF130465]









[PN:mannose-specific phosphotransferase system]









[GN:manL]









[OR:Streptococcus salivarius]


SPX1368
1368
4029
218
654
436
1.40E-55
[LN:YJGU_ECOLI]
102









[AC:P39345]









[GN:YJGU]









[OR:Escherichia coli]









[EC:1.-.-.-]









[DE:(EC 1.-.-.-)]









[SP:P39345]


SPX1369
1369
4030
125
375


NO-HIT
6


SPX1370
1370
4031
98
294
169
2.50E-19
[LN:YJGU_ECOLI]
102









[AC:P39345]









[GN:YJGU]









[OR:Escherichia coli]









[EC:1.-.-.-]









[DE:(EC 1.-.-.-)]









[SP:P39345]


SPX1371
1371
4032
214
642


NO-HIT
6


SPX1372
1372
4033
334
1002
317
1.00E-46
[LN:G72422]
112









[AC:G72422]









[PN:2-keto-3-deoxygluconate kinase]









[GN:TM0067]









[CL:ribokinase]









[OR:Thermotoga maritima]


SPX1373
1373
4034
210
630
271
6.10E-46
[LN:F72422]
190









[AC:F72422]









[PN:2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutarate aldolase]









[GN:TM0066]









[CL:2-dehydro-3-deoxyphosphogluconate aldolase]









[OR:Thermotoga maritima]


SPX1374
1374
4035
118
354
264
1.50E-50
[GI:1841332]
178









[LN:D64071]









[AC:D64071]









[PN:putative protein of unknown function]









[OR:Actinobacillus actinomycetemcomitans]









[SR:Actinobacillus actinomycetemcomitans (strain:Y4) DNA]


SPX1375
1375
4036
1079
3237
4863
0
“[LN:HYSA_STRPN]
156









[AC:Q54873:Q54874]









[OR:Streptococcus pneumoniae]









[EC:4.2.2.1]









[DE:HYALURONATE LYASE PRECURSOR, (HYALURONIDASE) (HYASE)]









[SP:Q54873:Q54874]”


SPX1376
1376
4037
159
477
482
1.90E-62
[GI:2598550]
100









[LN:LLAJ109]









[AC:AJ000109]









[PN:gluthatione peroxidase]









[GN:gpo]









[OR:Lactococcus lactis]


SPX1377
1377
4038
738
2214
181
4.50E-33
[GI:6686567]
120









[LN:AAC252161]









[AC:AJ252161]









[PN:putative alpha-glucosidase]









[GN:glcA]









[OR:Alicyclobacillus acidocaldarius]


SPX1378
1378
4039
61
183


NO-HIT
6


SPX1379
1379
4040
449
1347
231
3.40E-63
“[LN:PTCC_BACST]
157









[AC:Q45400]









[GN:CELB]









[OR:Bacillus stearothermophilus]









[DE:PERMEASE IIC COMPONENT) (PHOSPHOTRANSFERASE ENZYME II, C COMPONENT)]









[SP:Q45400]”


SPX1380
1380
4041
169
507


NO-HIT
6


SPX1381
1381
4042
105
315
234
2.00E-27
[LN:PTCA_BACSU]
121









[AC:P46319]









[GN:CELC:LICA]









[OR:Bacillus subtilis]









[EC:2.7.1.69]









[DE:(EC 2.7.1.69) (EIII-CEL)]









[SP:P46319]


SPX1382
1382
4043
660
1980
138
9.20E-51
[LN:CELR_BACSU]
112









[AC:P46321]









[GN:CELR:LICR]









[OR:Bacillus subtilis]









[DE:PUTATIVE CEL OPERON REGULATOR]









[SP:P46321]


SPX1383
1383
4044
114
342
84
2.40E-08
[LN:PTCB_BACST]
115









[AC:Q45399]









[GN:CELA]









[OR:Bacillus stearothermophilus]









[EC:2.7.1.69]









[DE:(EC 2.7.1.69)]









[SP:Q45399]


SPX1384
1384
4045
80
240
142
1.20E-15
[LN:Y110_METJA]
114









[AC:Q57574]









[GN:MJ0110]









[OR:Methanococcus jannaschii]









[DE:HYPOTHETICAL PROTEIN MJ0110]









[SP:Q57574]


SPX1385
1385
4046
493
1479
797
2.50E-225
[LN:JE0395]
120









[AC:JE0395]









[PN:phospho-beta-galactosidase I]









[CL:Agrobacterium beta-glucosidase]









[OR:Lactobacillus gasseri]


SPX1386
1386
4047
122
366


NO-HIT
6


SPX1387
1387
4048
69
207
359
2.90E-46
[GI:5019553]
97









[LN:SPN239004]









[AC:AJ239004]









[PN:putative transposase]









[OR:Streptococcus pneumoniae]


SPX1388
1388
4049
131
393
456
1.30E-58
[LN:RS9_BACST]
118









[AC:P07842]









[GN:RPSI]









[OR:Bacillus stearothermophilus]









[DE:30S RIBOSOMAL PROTEIN S9 (BS10)]









[SP:P07842]


SPX1389
1389
4050
149
447
487
2.30E-62
[LN:RL13_STACA]
109









[AC:Q00990]









[GN:RPLM]









[OR:Staphylococcus carnosus]









[DE:50S RIBOSOMAL PROTEIN L13]









[SP:Q00990]


SPX1390
1390
4051
122
366


NO-HIT
6


SPX1391
1391
4052
106
318


NO-HIT
6


SPX1392
1392
4053
131
393
630
8.40E-84
“[LN:SULD_STRPN]
181









[AC:P22291:O33697]









[GN:SULD]









[OR:Streptococcus pneumoniae]









[EC:4.1.2.25:2.7.6.3]









[DE:HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE) (PPPK)]]









[SP:P22291:O33697]”


SPX1393
1393
4054
170
510
834
1.40E-111
“[LN:A36704]
220









[AC:A36704]









[PN:bifunctional folate biosynthesis enzyme sulD:6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase:7, 8-dihydro-6-hydroxymethylpterin pyrophosphokinase]









[GN:sulD]









[OR:Streptococcus pneumoniae]”


SPX1394
1394
4055
185
555
938
4.90E-127
“[LN:GCH1_STRPN]
133









[AC:P51595]









[GN:SULC]









[OR:Streptococcus pneumoniae]









[EC:3.5.4.16]









[DE:GTP CYCLOHYDROLASE I, (GTP-CH-I)]









[SP:P51595]”


SPX1395
1395
4056
441
1323
2219
0
146


SPX1396
1396
4057
327
981
1485
7.00E-201
[LN:DHPS_STRPN]
117









[AC:P05382]









[GN:SULA]









[OR:Streptococcus pneumoniae]









[EC:2.5.1.15]









[DE:PYROPHOSPHORYLASE)]









[SP:P05382]


SPX1397
1397
4058
236
708
143
3.00E-13
[GI:1402529]
128









[LN:D78257]









[AC:D78257]









[PN:ORF8]









[GN:orf8]









[OR:Enterococcus faecalis]









[SR:Enterococcus faecalis plasmid:pYI17 DNA]


SPX1398
1398
4059
62
186


NO-HIT
6


SPX1399
1399
4060
494
1482
447
1.70E-116
[GI:6624219]
127









[LN:AB023289]









[AC:AB023289]









[GN:ORFX]









[OR:Pseudomonas fluorescens]









[SR:Pseudomonas fluorescens (strain:No.33) DNA]


SPX1400
1400
4061
271
813
199
8.70E-36
[LN:F69841]
178









[AC:F69841]









[PN:conserved hypothetical protein yitU]









[GN:yitU]









[CL:Methanobacterium thermoautotrophicum conserved hypothetical protein MTH1071]









[OR:Bacillus subtilis]


SPX1401
1401
4062
311
933
861
2.70E-156
[GI:7379448]
124









[LN:NMA3Z2491]









[AC:AL162754:AL157959]









[PN:putative alcohol dehydrogenase]









[GN:adhA]









[OR:Neisseria meningitidis]


SPX1402
1402
4063
333
999
795
2.40E-188
[GI:5669855]
128









[LN:AF130465]









[AC:AF130465]









[PN:mannose-specific phosphotransferase system]









[GN:manL]









[OR:Streptococcus salivarius]


SPX1403
1403
4064
268
804
974
1.10E-144
[GI:5669856]
128









[LN:AF130465]









[AC:AF130465]









[PN:mannose-specific phosphotransferase system]









[GN:manM]









[OR:Streptococcus salivarius]


SPX1404
1404
4065
304
912
1157
3.60E-158
[GI:5669857]
128









[LN:AF130465]









[AC:AF130465]









[PN:mannose-specific phosphotransferase system]









[GN:manN]









[OR:Streptococcus salivarius]


SPX1405
1405
4066
445
1335
1900
4.00E-256
“[LN:PEPC_STRTR]
120









[AC:Q56115]









[GN:PEPC]









[OR:Streptococcus thermophilus]









[EC:3.4.22.-]









[DE:AMINOPEPTIDASE C,]









[SP:Q56115]”


SPX1406
1406
4067
241
723
223
1.50E-59
[GI:7328274]
103









[LN:SAY14816]









[AC:Y14816]









[PN:hypothetical protein]









[GN:ORF231]









[OR:Staphylococcus aureus]


SPX1407
1407
4068
137
411
328
2.80E-41
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX1408
1408
4069
77
231


NO-HIT
6


SPX1409
1409
4070
77
231
154
1.90E-17
[LN:B69770]
97









[AC:B69770]









[PN:conserved hypothetical protein ydaS]









[GN:ydaS]









[OR:Bacillus subtilis]


SPX1410
1410
4071
414
1242
1792
6.20E-241
[GI:4731022]
107









[LN:AF102860]









[AC:AF102860]









[PN:aminopeptidase PepS]









[GN:pepS]









[OR:Streptococcus thermophilus]


SPX1411
1411
4072
60
180


NO-HIT
6


SPX1412
1412
4073
77
231


NO-HIT
6


SPX1413
1413
4074
93
279
110
1.90E-19
“[LN:B71883]
188









[AC:B71883]









[PN:hypothetical protein jhp0831]









[GN:jhp0831]









[CL:conserved hypothetical protein HI0711]









[OR:Helicobacter pylori]









[SR:strain J99, , strain J99]









[SR:strain J99, ]”


SPX1414
1414
4075
88
264
80
0.00012
[LN:DINJ_ECOLI]
107









[AC:Q47150]









[GN:DINJ]









[OR:Escherichia coli]









[DE:DNA-DAMAGE-INDUCIBLE PROTEIN J]









[SP:Q47150]


SPX1415
1415
4076
1464
4392
1689
0
“[GI:143342]
109









[LN:BACPOLC]









[AC:M22996]









[GN:polC]









[OR:Bacillus subtilis]









[SR:B.subtilis SB19 DNA, clone PRO10]”


SPX1416
1416
4077
694
2082
2833
0
[LN:T44380]
191









[AC:T44380]









[PN:translation elongation factor EF-G fus [imported]]









[GN:fus]









[CL:translation elongation factor G:translation elongation factor Tu homology]









[OR:Bacillus halodurans]


SPX1417
1417
4078
119
357
86
5.20E-10
[LN:YHA2_EIKCO]
115









[AC:P35649]









[OR:Eikenella corrodens]









[DE:HYPOTHETICAL 66.3 KD PROTEIN IN HAG2 5′REGION]









[SP:P35649]


SPX1418
1418
4079
150
450
88
1.30E-08
[LN:YHA2_EIKCO]
115









[AC:P35649]









[OR:Eikenella corrodens]









[DE:HYPOTHETICAL 66.3 KD PROTEIN IN HAG2 5′REGION]









[SP:P35649]


SPX1419
1419
4080
144
432
173
1.90E-17
[GI:7576785]
112









[LN:AF214675]









[AC:AF214675]









[PN:unknown in vivo-induced protein 131-19]









[OR:Pseudomonas aeruginosa]


SPX1420
1420
4081
157
471
633
1.10E-83
[LN:F69699]
161









[AC:F69699:S11357]









[PN:ribosomal protein S7 (rpsG):ribosomal protein BS7]









[GN:rpsG]









[CL:Escherichia coli ribosomal protein S7]









[OR:Bacillus subtilis]


SPX1421
1421
4082
138
414
699
1.70E-91
[LN:RS12_STRPN]
114









[AC:P30891]









[GN:RPSL:STR]









[OR:Streptococcus pneumoniae]









[DE:30S RIBOSOMAL PROTEIN S12]









[SP:P30891]


SPX1422
1422
4083
1205
3615
1478
0
[GI:1665738]
125









[LN:D78258]









[AC:D78258]









[PN:alkaline amylopullulanase]









[OR:Bacillus sp.]









[SR:Bacillus sp. (strain:KSM-1378) DNA]


SPX1423
1423
4084
308
924
655
1.70E-115
“[GI:2735505]
114









[LN:SCU96107]









[AC:U96107]









[PN:N5,N10-methylenetetrahydromethanopterin]









[OR:Staphylococcus carnosus]”


SPX1424
1424
4085
603
1809
963
3.70E-194
“[LN:B69633]
210









[AC:B69633]









[PN:glutamine--fructose-6-phosphate transaminase (isomerizing), glmS]









[GN:glmS]









[CL:glutamine--fructose-6-phosphate aminotransferase (isomerizing)]









[OR:Bacillus subtilis]









[EC:2.6.1.16]”


SPX1425
1425
4086
460
1380
851
2.00E-207
[LN:D69785]
127









[AC:D69785]









[PN:beta-glucosidase homolog ydhP]









[GN:ydhP]









[CL:Agrobacterium beta-glucosidase]









[OR:Bacillus subtilis]


SPX1426
1426
4087
347
1041
298
1.30E-82
“[LN:G69682]
153









[AC:G69682]









[PN:proline--tRNA ligase, proS:prolyl-tRNA synthetase]









[GN:proS]









[CL:proline--tRNA ligase]









[OR:Bacillus subtilis]









[EC:6.1.1.15]”


SPX1427
1427
4088
336
1008
691
5.20E-109
“[LN:G69682]
153









[AC:G69682]









[PN:proline--tRNA ligase, proS:prolyl-tRNA synthetase]









[GN:proS]









[CL:proline--tRNA ligase]









[OR:Bacillus subtilis]









[EC:6.1.1.15]”


SPX1428
1428
4089
420
1260
436
8.50E-136
[GI:5714510]
129









[LN:AF152237]









[AC:AF152237]









[PN:Eep]









[GN:eep]









[FN:determinant for enhanced expression of]









[OR:Enterococcus faecalis]


SPX1429
1429
4090
268
804
202
1.20E-51
[LN:CDSA_BACSU]
101









[AC:O31752]









[GN:CDSA]









[OR:Bacillus subtilis]









[EC:2.7.7.41]









[DE:SYNTHASE)]









[SP:O31752]


SPX1430
1430
4091
259
777
490
2.80E-90
[LN:UPPS_BACSU]
136









[AC:O31751]









[GN:UPPS]









[OR:Bacillus subtilis]









[EC:2.5.1.31]









[DE:(DI-TRANS-POLY-CIS-DECAPRENYLCISTRANSFERASE)]









[SP:O31751]


SPX1431
1431
4092
191
573
127
1.50E-11
[LN:S70841]
192









[AC:S70841]









[PN:hypothetical transmembrane protein (sipS 3′region)]









[CL:Bradyrhizobium japonicum hypothetical transmembrane protein (sipS 3′region)]









[OR:Bradyrhizobium japonicum]


SPX1432
1432
4093
333
999
1045
1.50E-140
[LN:H81105]
124









[AC:H81105]









[PN:Holliday junction DNA helicase RuvB NMB1243 [imported]]









[GN:NMB1243]









[OR:Neisseria meningitidis]


SPX1433
1433
4094
35
105
76
0.00015
[LN:H72613]
92









[AC:H72613]









[PN:hypothetical protein APE1371]









[GN:APE1371]









[OR:Aeropyrum pernix]


SPX1434
1434
4095
139
417
103
1.50E-06
[GI:5616248]
95









[LN:AF158628]









[AC:AF158628]









[PN:hypothetical protein]









[OR:Prochlorococcus PCC9511]


SPX1435
1435
4096
232
696
482
1.50E-73
“[LN:YIW2_YEAST]
155









[AC:P40586]









[GN:YIR042C]









[OR:Saccharomyces cerevisiae]









[SR:,Baker′s yeast]









[DE:HYPOTHETICAL 27.4 KD PROTEIN IN HYR1 3′REGION]









[SP:P40586]”


SPX1436
1436
4097
64
192


NO-HIT
6


SPX1437
1437
4098
834
2502
944
0
“LN:C70131]
199









[AC:C70131]









[PN:leucine--tRNA ligase, leuS:leucyl-tRNA synthetase:leucyl-tRNA synthetase]









[CL:leucine--tRNA ligase]









[OR:Borrelia burgdorferi]









[SR:, Lyme disease spirochete]









[EC:6.1.1.4]”


SPX1438
1438
4099
363
1089
998
1.00E-137
“[LN:GLDA_BACST]
137









[AC:P32816]









[GN:GLDA:GLD]









[OR:Bacillus stearothermophilus]









[EC:1.1.1.6]









[DE:GLYCEROL DEHYDROGENASE, (GLDH)]









[SP:P32816]”


SPX1439
1439
4100
223
669
356
8.20E-53
[GI:2582658]
142









[LN:CBAJ2527]









[AC:AJ002527]









[PN:OrfX]









[GN:orfX]









[FN:putative transaldolase (37.4% identity to talC]









[OR:Clostridium beijerinckii]


SPX1440
1440
4101
816
2448
992
1.80E-275
[LN:PFLF_ECOLI]
99









[AC:P75793]









[GN:YBIW]









[OR:Escherichia coli]









[EC:2.3.1.54]









[DE:LYASE 3)]









[SP:P75793]


SPX1441
1441
4102
427
1281
337
4.90E-89
“[LN:PTCC_BACST]
157









[AC:Q45400]









[GN:CELB]









[OR:Bacillus stearothermophilus]









[DE:PERMEASE IIC COMPONENT) (PHOSPHOTRANSFERASE ENZYME II, C COMPONENT)]









[SP:Q45400]”


SPX1442
1442
4103
103
309
194
3.50E-22
[LN:A69785]
189









[AC:A69785]









[PN:cellobiose phosphotransferase system enzym homolog ydhM]









[GN:ydhM]









[CL:phosphotransferase system enzyme II cellobiose-specific factor IIB]









[OR:Bacillus subtilis]


SPX1443
1443
4104
107
321
186
5.70E-21
[LN:PTCA_BACSU]
121









[AC:P46319]









[GN:CELC:LICA]









[OR:Bacillus subtilis]









[EC:2.7.1.69]









[DE:(EC 2.7.1.69) (EIII-CEL)]









[SP:P46319]


SPX1444
1444
4105
327
981
265
2.80E-49
[LN:SORC_KLEPN]
130









[AC:P37078]









[GN:SORC]









[OR:Klebsiella pneumoniae]









[DE:SORBITOL OPERON REGULATOR (SOR OPERON ACTIVATOR)]









[SP:P37078]


SPX1445
1445
4106
249
747
252
6.10E-57
[LN:YCIT_ECOLI]
145









[AC:P76034]









[GN:YCIT]









[OR:Escherichia coli]









[DE:HYPOTHETICAL TRANSCRIPTIONAL REGULATOR IN OSMB-RNB INTERGENIC REGION]









[SP:P76034]


SPX1446
1446
4107
259
777
266
4.40E-55
“[LN:PFLE_ECOLI]
145









[AC:P75794]









[GN:YBIY]









[OR:Escherichia coli]









[EC:1.97.1.4]









[DE:PUTATIVE PYRUVATE FORMATE-LYASE 3 ACTIVATING ENZYME,]









[SP:P75794]”


SPX1447
1447
4108
83
249
105
3.60E-08
[GI:7331182]
88









[LN:AF235048]









[AC:AF235048]









[PN:AgpT]









[GN:agpT]









[OR:Sinorhizobium meliloti]


SPX1448
1448
4109
65
195
177
4.60E-18
[GI:6127225]
129









[LN:SHU75349]









[AC:U75349]









[PN:periplasmic-iron-binding protein BitA]









[GN:bit operon]









[OR:Brachyspira hyodysenteriae]


SPX1449
1449
4110
123
369
242
1.10E-26
[GI:6127225]
129









[LN:SHU75349]









[AC:U75349]









[PN:periplasmic-iron-binding protein BitA]









[GN:bit operon]









[OR:Brachyspira hyodysenteriae]


SPX1450
1450
4111
318
954
799
1.70E-113
[GI:2766194]
121









[LN:SHU75349]









[AC:U75349]









[PN:putative ABC transporter BitD]









[GN:bit operon]









[OR:Brachyspira hyodysenteriae]


SPX1451
1451
4112
209
627
283
2.70E-40
[GI:2766195]
114









[LN:SHU75349]









[AC:U75349]









[PN:putative permease BitE]









[GN:bit operon]









[OR:Brachyspira hyodysenteriae]


SPX1452
1452
4113
257
771
295
1.50E-68
[GI:2766196]
114









[LN:SHU75349]









[AC:U75349]









[PN:putative permease BitF]









[GN:bit operon]









[OR:Brachyspira hyodysenteriae]


SPX1453
1453
4114
66
198
164
3.20E-17
[GI:2766196]
114









[LN:SHU75349]









[AC:U75349]









[PN:putative permease BitF]









[GN:bit operon]









[OR:Brachyspira hyodysenteriae]


SPX1454
1454
4115
250
750
137
3.20E-10
[LN:PMGY_TREPA]
122









[AC:P96121]









[GN:GPM:PGM:TP0168]









[OR:Treponema pallidum]









[EC:5.4.2.1]









[DE:(BPG-DEPENDENT PGAM)]









[SP:P96121]


SPX1455
1455
4116
446
1338
855
6.60E-196
[GI:7380543]
127









[LN:NMA6Z2491]









[AC:AL162757:AL157959]









[PN:conserved hypothetical protein]









[GN:NMA1908]









[OR:Neisseria meningitidis]


SPX1456
1456
4117
120
360
123
9.30E-21
[LN:E64494]
86









[AC:E64494]









[PN:hypothetical protein MJ1558]









[OR:Methanococcus jannaschii]


SPX1457
1457
4118
129
387
282
2.20E-58
[LN:T44411]
140









[AC:T44411]









[PN:ribosomal protein L17 [imported]]









[GN:rplQ]









[CL:Escherichia coli ribosomal protein L17]









[OR:Bacillus halodurans]


SPX1458
1458
4119
312
936
963
6.70E-130
[LN:RPOA_BACSU]
134









[AC:P20429]









[GN:RPOA]









[OR:Bacillus subtilis]









[EC:2.7.7.6]









[DE:ALPHA CHAIN) (RNA POLYMERASE ALPHA SUBUNIT)]









[SP:P20429]


SPX1459
1459
4120
134
402


NO-HIT
6


SPX1460
1460
4121
141
423
494
1.80E-63
[LN:RS11_BACSU]
110









[AC:P04969]









[GN:RPSK]









[OR:Bacillus subtilis]









[DE:30S RIBOSOMAL PROTEIN S11 (BS11)]









[SP:P04969]


SPX1461
1461
4122
122
366
433
1.70E-55
[GI:1044989]
97









[LN:BACRPLP]









[AC:L47971]









[PN:ribosomal protein S13]









[GN:rpsM]









[OR:Bacillus subtilis]


SPX1462
1462
4123
56
168
237
1.10E-28
[LN:S17988]
151









[AC:S17988]









[PN:translation initiation factor IF-1]









[GN:infA]









[CL:translation initiation factor IF-1]









[OR:Lactococcus lactis subsp. lactis]


SPX1463
1463
4124
213
639
560
8.10E-95
“[LN:KAD_LACLA]
177









[AC:P27143]









[GN:ADK]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:2.7.4.3]









[DE:ADENYLATE KINASE, (ATP-AMP TRANSPHOSPHORYLASE)]









[SP:P27143]”


SPX1464
1464
4125
437
1311
927
4.30E-126
“[LN:SECY_LACLA]
155









[AC:P27148]









[GN:SECY]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[DE:PREPROTEIN TRANSLOCASE SECY SUBUNIT]









[SP:P27148]”


SPX1465
1465
4126
147
441
614
7.90E-79
[LN:RL15_STAAU]
107









[AC:O06445]









[GN:RPLO]









[OR:Staphylococcus aureus]









[DE:50S RIBOSOMAL PROTEIN L15]









[SP:O06445]


SPX1466
1466
4127
61
183
185
6.90E-21
[LN:RL30_STAAU]
107









[AC:O06444]









[GN:RPMD]









[OR:Staphylococcus aureus]









[DE:50S RIBOSOMAL PROTEIN L30]









[SP:O06444]


SPX1467
1467
4128
165
495
621
8.70E-81
[LN:RS5_BACST]
117









[AC:P02357]









[GN:RPSE]









[OR:Bacillus stearothermophilus]









[DE:30S RIBOSOMAL PROTEIN S5 (BS5)]









[SP:P02357]


SPX1468
1468
4129
119
357
232
2.60E-53
[LN:RL18_BACSU]
117









[AC:P46899:P70969]









[GN:RPLR]









[OR:Bacillus subtilis]









[DE:50S RIBOSOMAL PROTEIN L18]









[SP:P46899:P70969]


SPX1469
1469
4130
175
525
478
2.00E-66
[LN:B69695]
136









[AC:B69695]









[PN:ribosomal protein L6 (BL8) rplF]









[GN:rplF]









[CL:Escherichia coli ribosomal protein L6]









[OR:Bacillus subtilis]


SPX1470
1470
4131
133
399
521
2.60E-67
[GI:1044978]
96









[LN:BACRPLP]









[AC:L47971]









[PN:ribosomal protein S8]









[GN:rpsH]









[OR:Bacillus subtilis]


SPX1471
1471
4132
79
237


NO-HIT
6


SPX1472
1472
4133
90
270
325
8.80E-41
[LN:F69835]
140









[AC:F69835]









[PN:ribosomal protein S14 homolog yhzA]









[GN:yhzA]









[CL:Escherichia coli ribosomal protein S14]









[OR:Bacillus subtilis]


SPX1473
1473
4134
181
543
728
6.40E-96
[LN:T44395]
138









[AC:T44395]









[PN:ribosomal protein L5 [imported]]









[GN:rplE]









[CL:Escherichia coli ribosomal protein L5]









[OR:Bacillus halodurans]


SPX1474
1474
4135
102
306
508
2.80E-65
[GI:4927751]
91









[LN:AF126059]









[AC:AF126059]









[PN:RpL24]









[GN:rplX]









[OR:Streptococcus pneumoniae]


SPX1475
1475
4136
123
369
597
2.20E-78
[GI:4927750]
91









[LN:AF126059]









[AC:AF126059]









[PN:RpL14]









[GN:rplN]









[OR:Streptococcus pneumoniae]


SPX1476
1476
4137
110
330
100
4.40E-07
[LN:E71186]
150









[AC:E71186]









[PN:hypothetical protein PH1769]









[GN:PH1769]









[CL:Pyrococcus horikoshii hypothetical protein PH1769]









[OR:Pyrococcus horikoshii]


SPX1477
1477
4138
87
261
430
3.10E-55
[GI:4927749]
91









[LN:AF126059]









[AC:AF126059]









[PN:RpS17]









[GN:rpsQ]









[OR:Streptococcus pneumoniae]


SPX1478
1478
4139
133
399


NO-HIT
6


SPX1479
1479
4140
69
207
324
8.90E-40
[GI:4927748]
91









[LN:AF126059]









[AC:AF126059]









[PN:RpL29]









[GN:rpmC]









[OR:Streptococcus pneumoniae]


SPX1480
1480
4141
138
414
708
1.30E-94
[GI:4927747]
91









[LN:AF126059]









[AC:AF126059]









[PN:RpL16]









[GN:rplP]









[OR:Streptococcus pneumoniae]


SPX1481
1481
4142
209
627
1063
2.10E-142
[GI:4927746]
90









[LN:AF126059]









[AC:AF126059]









[PN:RpS3]









[GN:rpsC]









[OR:Streptococcus pneumoniae]


SPX1482
1482
4143
75
225
356
1.60E-44
[GI:4927745]
91









[LN:AF126059]









[AC:AF126059]









[PN:RpL22]









[GN:rplV]









[OR:Streptococcus pneumoniae]


SPX1483
1483
4144
82
246


NO-HIT
6


SPX1484
1484
4145
94
282
492
5.20E-64
[GI:4927744]
91









[LN:AF126059]









[AC:AF126059]









[PN:RpS19]









[GN:rpsS]









[OR:Streptococcus pneumoniae]


SPX1485
1485
4146
278
834
1144
2.80E-152
[LN:RL2_BACST]
111









[AC:P04257]









[GN:RPLB]









[OR:Bacillus stearothermophilus]









[DE:50S RIBOSOMAL PROTEIN L2]









[SP:P04257]


SPX1486
1486
4147
99
297
162
1.30E-30
[GI:3273331]
138









[LN:AB015722]









[AC:AB015722]









[PN:ribosomal protrein L23]









[OR:Bacillus stearothermophilus]









[SR:Bacillus stearothermophilus DNA]


SPX1487
1487
4148
208
624
696
6.80E-91
[LN:RL4_BACST]
111









[AC:P28601]









[GN:RPLD]









[OR:Bacillus stearothermophilus]









[DE:50S RIBOSOMAL PROTEIN L4]









[SP:P28601]


SPX1488
1488
4149
209
627
496
6.60E-110
[LN:RL3_BACSU]
107









[AC:P42920]









[GN:RPLC]









[OR:Bacillus subtilis]









[DE:50S RIBOSOMAL PROTEIN L3 (BL3)]









[SP:P42920]


SPX1489
1489
4150
103
309
494
3.40E-64
[LN:RS10_STRMU]
106









[AC:P48853]









[GN:RPSJ]









[OR:Streptococcus mutans]









[DE:30S RIBOSOMAL PROTEIN S10]









[SP:P48853]


SPX1490
1490
4151
206
618
71
0.00018
[GI:7302797]
105









[LN:AE003803]









[AC:AE003803:AE002787]









[GN:CG4798]









[OR:Drosophila melanogaster]









[SR:fruit fly]


SPX1491
1491
4152
197
591
843
3.60E-112
[GI:4098082]
167









[LN:LLU73336]









[AC:U73336]









[PN:anaerobic ribonucleotide reductase activator]









[GN:nrdG]









[FN:activation of anaerobic]









[OR:Lactococcus lactis subsp. cremoris]


SPX1492
1492
4153
69
207


NO-HIT
6


SPX1493
1493
4154
169
507
187
4.50E-19
[LN:G75479]
90









[AC:G75479]









[PN:hypothetical protein]









[GN:DR0763]









[OR:Deinococcus radiodurans]


SPX1494
1494
4155
155
465


NO-HIT
6


SPX1495
1495
4156
738
2214
1123
1.10E-231
[GI:4098081]
128









[LN:LLU73336]









[AC:U73336]









[PN:anaerobic ribonucleotide reductase]









[GN:nrdD]









[OR:Lactococcus lactis subsp. cremoris]


SPX1496
1496
4157
519
1557


NO-HIT
6


SPX1497
1497
4158
492
1476
519
3.70E-97
[LN:YWAP_STRMU]
119









[AC:P34001]









[OR:Streptococcus mutans]









[DE:HYPOTHETICAL PROTEIN IN WAPA 3′REGION (FRAGMENT)]









[SP:P34001]


SPX1498
1498
4159
186
558
93
0.00012
[LN:A26892]
84









[AC:A26892]









[PN:Mopa box protein]









[OR:Mus musculus]









[SR:, house mouse]”


SPX1499
1499
4160
70
210


NO-HIT
6


SPX1500
1500
4161
130
390
66
7.30E-09
[GI:1119198]
122









[LN:BACCOMC]









[AC:M30805]









[PN:unknown protein]









[OR:Bacillus subtilis]









[SR:Bacillus subtilis (strain IS75) DNA]


SPX1501
1501
4162
161
483
119
5.10E-16
[LN:FOLC_LACCA]
111









[AC:P15925]









[GN:FGS]









[OR:Lactobacillus casei]









[EC:6.3.2.17]









[DE:SYNTHETASE) (FPGS)]









[SP:P15925]


SPX1502
1502
4163
164
492
251
2.00E-38
[LN:FOLC_BACSU]
110









[AC:Q05865]









[GN:FOLC]









[OR:Bacillus subtilis]









[EC:6.3.2.17]









[DE:SYNTHETASE) (FPGS)]









[SP:Q05865]


SPX1503
1503
4164
102
306
87
5.90E-11
[LN:A69982]
87









[AC:A69982]









[PN:hypothetical protein yrzB]









[GN:yrzB]









[OR:Bacillus subtilis]


SPX1504
1504
4165
140
420
327
2.00E-40
[LN:D69979]
163









[AC:D69979]









[PN:conserved hypothetical protein yrrK]









[GN:yrrK]









[CL:Haemophilus influenzae conserved hypothetical protein HI0305]









[OR:Bacillus subtilis]


SPX1505
1505
4166
89
267


NO-HIT
6


SPX1506
1506
4167
190
570


NO-HIT
6


SPX1507
1507
4168
133
399
315
1.80E-38
[GI:6650536]
81









[LN:AF103794]









[AC:AF103794]









[PN:unknown]









[OR:Listeria monocytogenes]


SPX1508
1508
4169
126
378
333
1.60E-40
[GI:517210]
65









[LN:SPU11799]









[AC:U11799]









[OR:Streptococcus pyogenes]


SPX1509
1509
4170
131
393
340
3.70E-41
[GI:517210]
65









[LN:SPU11799]









[AC:U11799]









[OR:Streptococcus pyogenes]


SPX1510
1510
4171
296
888
1035
8.50E-139
[GI:6318592]
185









[LN:AF146529]









[AC:AF146529]









[PN:aromatic amino acid aminotransferase]









[GN:araT]









[FN:catalyzes the last reaction in the biosynthesis]









[OR:Lactococcus lactis subsp. cremoris]


SPX1511
1511
4172
62
186


NO-HIT
6


SPX1512
1512
4173
257
771
297
2.20E-40
[LN:YQXN_BACSU]
89









[AC:P42095]









[GN:YQXN:YQFI]









[OR:Bacillus subtilis]









[DE:(ORF3)]









[SP:P42095]


SPX1513
1513
4174
331
993
623
6.80E-120
[LN:H69679]
148









[AC:H69679]









[PN:involved in fatty acid/phospholipid synthesis plsX]









[GN:plsX]









[CL:phospholipid synthesis protein]









[OR:Bacillus subtilis]


SPX1514
1514
4175
112
336


NO-HIT
6


SPX1515
1515
4176
78
234
129
1.40E-17
[LN:C72349]
142









[AC:C72349]









[PN:acyl carrier protein]









[GN:TM0662]









[CL:acyl carrier protein:acyl carrier protein homology]









[OR:Thermotoga maritima]


SPX1516
1516
4177
98
294
320
4.80E-40
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX1517
1517
4178
77
231
64
3.00E-06
[GI:2695624]
128









[LN:STU93029]









[AC:U93029]









[PN:amphipathic pore-forming peptide precursor]









[GN:thmA]









[OR:Streptococcus thermophilus]


SPX1518
1518
4179
69
207


NO-HIT
6


SPX1519
1519
4180
720
2160
3571
0
[LN:COMA_STRPN]
119









[AC:Q03727]









[GN:COMA]









[OR:Streptococcus pneumoniae]









[DE:TRANSPORT ATP-BINDING PROTEIN COMA]









[SP:Q03727]


SPX1520
1520
4181
450
1350
2184
8.20E-289
[LN:COMB_STRPN]
107









[AC:P36498]









[GN:COMB]









[OR:Streptococcus pneumoniae]









[DE:TRANSPORT PROTEIN COMB]









[SP:P36498]


SPX1521
1521
4182
250
750
1189
1.40E-160
[LN:PUR7_STRPN]
117









[AC:Q07296]









[GN:PURC]









[OR:Streptococcus pneumoniae]









[EC:6.3.2.6]









[DE:(SAICAR SYNTHETASE)]









[SP:Q07296]


SPX1522
1522
4183
254
762
127
2.80E-08
“““[LN:C69492]
217









[AC:C69492]









[PN:phosphoribosylformylglycinamidine synthase, component II:formylglycinamide ribotide amidotransferase:phosphoribosylformylglycinamidine synthetase]









[OR:Archaeoglobus fulgidus]









[EC:6.3.5.3]”””


SPX1523
1523
4184
95
285
155
3.80E-15
[GI:4928281]
110









[LN:AF132127]









[AC:AF132127]









[PN:glucose-6-phosphate isomerase]









[GN:gpi]









[OR:Streptococcus mutans]


SPX1524
1524
4185
457
1371
1764
1.20E-238
[GI:4928281]
110









[LN:AF132127]









[AC:AF132127]









[PN:glucose-6-phosphate isomerase]









[GN:gpi]









[OR:Streptococcus mutans]


SPX1525
1525
4186
246
738
246
3.10E-28
“[LN:YDP3_LACLA]
162









[AC:P22347]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[DE:HYPOTHETICAL 18.7 KD PROTEIN IN PEPX 3′REGION (ORF3)]









[SP:P22347]”


SPX1526
1526
4187
604
1812
1001
2.10E-222
[GI:4104142]
99









[LN:AF033015]









[AC:AF033015]









[PN:ABC transporter homolog Z]









[OR:Listeria monocytogenes]


SPX1527
1527
4188
72
216


NO-HIT
6


SPX1528
1528
4189
108
324
105
1.60E-07
[GI:6015958]
110









[LN:SSU18930]









[AC:Y18930]









[PN:hypothetical protein]









[GN:ORF-c22_037]









[OR:Sulfolobus solfataricus]


SPX1529
1529
4190
196
588
455
7.30E-58
[GI:4104141]
99









[LN:AF033015]









[AC:AF033015]









[PN:ABC transporter homolog Y]









[OR:Listeria monocytogenes]


SPX1530
1530
4191
361
1083
422
2.80E-66
[GI:4104140]
99









[LN:AF033015]









[AC:AF033015]









[PN:ABC transporter homolog X]









[OR:Listeria monocytogenes]


SPX1531
1531
4192
655
1965
3290
0
[LN:HEXA_STRPN]
117









[AC:P10564]









[GN:HEXA]









[OR:Streptococcus pneumoniae]









[DE:DNA MISMATCH REPAIR PROTEIN HEXA]









[SP:P10564]


SPX1532
1532
4193
182
546
859
6.40E-114
[LN:HEXA_STRPN]
117









[AC:P10564]









[GN:HEXA]









[OR:Streptococcus pneumoniae]









[DE:DNA MISMATCH REPAIR PROTEIN HEXA]









[SP:P10564]


SPX1533
1533
4194
149
447
740
7.50E-99
[LN:ARGR_STRPN]
112









[AC:Q54870]









[GN:ARGR]









[OR:Streptococcus pneumoniae]









[DE:PROBABLE ARGININE REPRESSOR]









[SP:Q54870]


SPX1534
1534
4195
564
1692
365
3.20E-102
“[LN:SYRC_YEAST]
154









[AC:Q05506]









[GN:YDR341C:D9651.10]









[OR:Saccharomyces cerevisiae]









[SR:,Baker′s yeast]









[EC:6.1.1.19]









[DE:-TRNA LIGASE) (ARGRS)]









[SP:Q05506]”


SPX1535
1535
4196
150
450
398
6.20E-51
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX1536
1536
4197
68
204


NO-HIT
6


SPX1537
1537
4198
95
285
102
6.20E-17
“[LN:S74709]
124









[AC:S74709]









[PN:hypothetical protein sll1188]









[OR:Synechocystis sp.]









[SR:PCC 6803, , PCC 6803]









[SR:PCC 6803, ]”


SPX1538
1538
4199
236
708
1209
4.90E-164
[GI:5830529]
104









[LN:SPAJ6394]









[AC:AJ006394]









[PN:response regulator]









[GN:phoP]









[OR:Streptococcus pneumoniae]


SPX1539
1539
4200
444
1332
2196
4.10E-300
[GI:5830530]
102









[LN:SPAJ6394]









[AC:AJ006394]









[PN:histidine kinase]









[GN:phoR]









[OR:Streptococcus pneumoniae]


SPX1540
1540
4201
292
876
1435
1.70E-188
[GI:4530447]
116









[LN:AF118229]









[AC:AF118229]









[PN:phosphate binding protein PstS]









[GN:pstS]









[OR:Streptococcus pneumoniae]


SPX1541
1541
4202
272
816
1333
2.80E-185
[GI:4530448]
112









[LN:AF118229]









[AC:AF118229]









[PN:transmembrane protein PstC]









[GN:pstC]









[OR:Streptococcus pneumoniae]


SPX1542
1542
4203
272
816
1312
1.10E-182
[GI:4530449]
112









[LN:AF118229]









[AC:AF118229]









[PN:transmembrane protein PstA]









[GN:PstA]









[OR:Streptococcus pneumoniae]


SPX1543
1543
4204
251
753
1284
2.00E-174
[GI:4530450]
119









[LN:AF118229]









[AC:AF118229]









[PN:ATP-binding cassette protein PstB]









[GN:pstB]









[OR:Streptococcus pneumoniae]


SPX1544
1544
4205
217
651
1067
8.20E-144
[GI:4530451]
90









[LN:AF118229]









[AC:AF118229]









[PN:PhoU]









[GN:phoU]









[OR:Streptococcus pneumoniae]


SPX1545
1545
4206
142
426
131
2.90E-10
[GI:5822769]
109









[LN:AB024553]









[AC:AB024553]









[OR:Bacillus halodurans]









[SR:Bacillus halodurans (strain:C-125) DNA]


SPX1546
1546
4207
73
219


NO-HIT
6


SPX1547
1547
4208
153
459


NO-HIT
6


SPX1548
1548
4209
339
1017
921
6.40E-122
[LN:GPDA_BACSU]
144









[AC:P46919]









[GN:GPSA:GLYC]









[OR:Bacillus subtilis]









[EC:1.1.1.94]









[DE:DEPENDENT DIHYDROXYACETONE-PHOSPHATE REDUCTASE)]









[SP:P46919]


SPX1549
1549
4210
300
900
1481
1.60E-199
[GI:3550619]
159









[LN:SPAJ4869]









[AC:AJ004869]









[PN:UTP-glucose-1-phosphate uridylyltransferase]









[GN:galU]









[FN:synthesis of UDP-glucose]









[OR:Streptococcus pneumoniae]


SPX1550
1550
4211
225
675


NO-HIT
6


SPX1551
1551
4212
227
681
520
1.90E-70
[LN:SUB400707]
80









[AC:AJ400707]









[PN:hypothetical protein]









[OR:Streptococcus uberis]


SPX1552
1552
4213
182
546
236
1.30E-55
[GI:3192049]
108









[LN:AB001562]









[AC:AB001562]









[OR:Streptococcus mutans]









[SR:Streptococcus mutans (strain:Xc) DNA]


SPX1553
1553
4214
377
1131
622
4.50E-119
[LN:G69866]
119









[AC:G69866]









[PN:hippurate hydrolase homolog ykuR]









[GN:ykuR]









[CL:hippurate hydrolase]









[OR:Bacillus subtilis]


SPX1554
1554
4215
233
699
578
1.10E-86
“[LN:H72245]
146









[AC:H72245]









[PN:2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase-related protein]









[GN:TM1519]









[OR:Thermotoga maritima]”


SPX1555
1555
4216
153
459
75
5.50E-08
[GI:6103625]
71









[LN:AF172095]









[AC:AF172095]









[PN:unknown]









[OR:Picea rubens]


SPX1556
1556
4217
72
216


NO-HIT
6


SPX1557
1557
4218
278
834
214
2.60E-30
[LN:YDED_BACSU]
136









[AC:P96661]









[GN:YDED]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 35.3 KD PROTEIN IN CSPC-NAP INTERGENIC REGION]









[SP:P96661]


SPX1558
1558
4219
821
2463
4147
0
[GI:6165962]
116









[LN:AF101781]









[AC:AF101781]









[PN:penicillin-binding protein 1b]









[GN:pbp1b]









[OR:Streptococcus pneumoniae]


SPX1559
1559
4220
419
1257
697
1.90E-174
[LN:SYY1_BACSU]
100









[AC:P22326]









[GN:TYRS]









[OR:Bacillus subtilis]









[EC:6.1.1.1]









[DE:(TYRRS 1)]









[SP:P22326]


SPX1560
1560
4221
691
2073
218
1.60E-63
“[LN:COPA_ENTHR]
148









[AC:P32113:Q47841]









[GN:COPA]









[OR:Enterococcus hirae]









[EC:3.6.1.36]









[DE:COPPER/POTASSIUM-TRANSPORTING ATPASE A,]









[SP:P32113:Q47841]”


SPX1561
1561
4222
65
195


NO-HIT
6


SPX1562
1562
4223
88
264
109
2.90E-08
[LN:RRMA_ECOLI]
109









[AC:P36999]









[GN:RRMA]









[OR:Escherichia coli]









[EC:2.1.1.51]









[DE:METHYLTRANSFERASE)]









[SP:P36999]


SPX1563
1563
4224
197
591
192
1.90E-25
[LN:YXJB_BACSU]
128









[AC:P42313]









[GN:YXJB:N15I]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 31.5 KD PROTEIN IN KATB 3′REGION]









[SP:P42313]


SPX1564
1564
4225
57
171


NO-HIT
6


SPX1565
1565
4226
191
573


NO-HIT
6


SPX1566
1566
4227
753
2259
473
5.80E-165
“[LN:PHSG_BACSU]
116









[AC:P39123]









[GN:GLGP]









[OR:Bacillus subtilis]









[EC:2.4.1.1]









[DE:GLYCOGEN PHOSPHORYLASE,]









[SP:P39123]”


SPX1567
1567
4228
506
1518
2687
0
[LN:MALQ_STRPN]
137









[AC:P29851]









[GN:MALM]









[OR:Streptococcus pneumoniae]









[EC:2.4.1.25]









[DE:(DISPROPORTIONATING ENZYME) (D-ENZYME)]









[SP:P29851]


SPX1568
1568
4229
424
1272
2167
3.30E-288
[LN:MALX_STRPN]
131









[AC:P29850]









[GN:MALX]









[OR:Streptococcus pneumoniae]









[DE:MALTOSE/MALTODEXTRIN-BINDING PROTEIN PRECURSOR]









[SP:P29850]


SPX1569
1569
4230
431
1293
2176
0
[LN:MALC_STRPN]
136









[AC:Q04698]









[GN:MALC]









[OR:Streptococcus pneumoniae]









[DE:MALTODEXTRIN TRANSPORT SYSTEM PERMEASE PROTEIN MALC]









[SP:Q04698]


SPX1570
1570
4231
281
843
1265
2.40E-177
[LN:MALD_STRPN]
136









[AC:Q04699]









[GN:MALD]









[OR:Streptococcus pneumoniae]









[DE:MALTODEXTRIN TRANSPORT SYSTEM PERMEASE PROTEIN MALD]









[SP:Q04699]


SPX1571
1571
4232
267
801
540
1.70E-145
[LN:MALA_STRPN]
97









[AC:Q08510]









[GN:MALA]









[OR:Streptococcus pneumoniae]









[DE:MALA PROTEIN]









[SP:Q08510]


SPX1572
1572
4233
329
987
1668
7.30E-227
[GI:2656094]
146









[LN:STRMALR]









[AC:L21856]









[PN:repressor protein]









[GN:malR]









[FN:maltose operon transcriptional repressor]









[OR:Streptococcus pneumoniae]


SPX1573
1573
4234
114
342


NO-HIT
6


SPX1574
1574
4235
127
381
378
8.30E-48
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX1575
1575
4236
314
942
463
6.90E-73
[GI:1620924]
62









[LN:BS168NPRB]









[AC:Z79580]









[OR:Bacillus subtilis]


SPX1576
1576
4237
588
1764
701
1.30E-229
[LN:SYD_BACSU]
98









[AC:O32038]









[GN:ASPS]









[OR:Bacillus subtilis]









[EC:6.1.1.12]









[DE:(ASPRS)]









[SP:O32038]


SPX1577
1577
4238
144
432


NO-HIT
6


SPX1578
1578
4239
64
192


NO-HIT
6


SPX1579
1579
4240
77
231


NO-HIT
6


SPX1580
1580
4241
214
642
120
9.80E-14
[GI:1402529]
128









[LN:D78257]









[AC:D78257]









[PN:ORF8]









[GN:orf8]









[OR:Enterococcus faecalis]









[SR:Enterococcus faecalis plasmid:pYI17 DNA]


SPX1581
1581
4242
247
741


NO-HIT
6


SPX1582
1582
4243
67
201


NO-HIT
6


SPX1583
1583
4244
155
465
78
0.00011
[LN:T07291]
89









[AC:T07291]









[PN:hypothetical protein 42c]









[OR:chloroplast Chlorella vulgaris]


SPX1584
1584
4245
62
186


NO-HIT
6


SPX1585
1585
4246
64
192


NO-HIT
6


SPX1586
1586
4247
63
189
200
7.00E-24
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX1587
1587
4248
430
1290
1740
7.50E-236
[LN:SYH_STREQ]
106









[AC:P30053]









[GN:HISS]









[OR:Streptococcus equisimilis]









[EC:6.1.1.21]









[DE:(HISRS)]









[SP:P30053]


SPX1588
1588
4249
307
921


NO-HIT
6


SPX1589
1589
4250
416
1248
334
2.10E-57
[GI:3582221]
114









[LN:AE001272]









[AC:AE001272]









[PN:conserved hypothetical protein]









[GN:ORF00049]









[OR:Lactococcus lactis]


SPX1590
1590
4251
133
399


NO-HIT
6


SPX1591
1591
4252
284
852
301
1.70E-34
[LN:RGG_STRGC]
100









[AC:P49330]









[GN:RGG]









[OR:Streptococcus gordonii challis]









[DE:RGG PROTEIN]









[SP:P49330]


SPX1592
1592
4253
114
342
227
6.60E-27
[GI:2258088]
96









[LN:AB000631]









[AC:AB000631]









[OR:Streptococcus mutans]









[SR:Streptococcus mutans DNA]


SPX1593
1593
4254
568
1704
994
1.30E-207
“[LN:S76895]
148









[AC:S76895]









[PN:hypothetical protein]









[CL:dihydroxy-acid dehydratase]









[OR:Synechocystis sp.]









[SR:PCC 6803, , PCC 6803]









[SR:PCC 6803, ]”


SPX1594
1594
4255
311
933
272
2.40E-45
“[LN:TKTC_METJA]
149









[AC:Q58092]









[GN:MJ0679]









[OR:Methanococcus jannaschii]









[EC:2.2.1.1]









[DE:PUTATIVE TRANSKETOLASE C-TERMINAL SECTION, (TK)]









[SP:Q58092]”


SPX1595
1595
4256
286
858
347
7.70E-66
“[LN:TKTN_METJA]
149









[AC:Q58094]









[GN:MJ0681]









[OR:Methanococcus jannaschii]









[EC:2.2.1.1]









[DE:PUTATIVE TRANSKETOLASE N-TERMINAL SECTION, (TK)]









[SP:Q58094]”


SPX1596
1596
4257
449
1347
535
9.90E-132
[LN:T37066]
107









[AC:T37066]









[PN:probable integral membrane protein]









[GN:SCJ21.17c]









[OR:Streptomyces coelicolor]


SPX1597
1597
4258
95
285


NO-HIT
6


SPX1598
1598
4259
677
2031
197
8.80E-31
“[GI:4512373]
144









[LN:AB011837]









[AC:AB011837]









[GN:yjdC]









[OR:Bacillus halodurans]









[SR:Bacillus halodurans (strain:C-125) DNA, clone_lib:lambda no.9]”


SPX1599
1599
4260
336
1008
133
1.30E-18
[GI:6689167]
118









[LN:SCE20]









[AC:AL136058]









[PN:putative membrane protein]









[GN:SCE20.08c]









[OR:Streptomyces coelicolor A3(2)]


SPX1600
1600
4261
67
201


NO-HIT
6


SPX1601
1601
4262
61
183
240
3.00E-28
“[LN:RL32_LACLC]
149









[AC:O34101]









[GN:RPMF]









[OR:Lactococcus lactis]









[SR:,subspcremoris:Streptococcus cremoris]









[DE:50S RIBOSOMAL PROTEIN L32]









[SP:O34101]”


SPX1602
1602
4263
642
1926
1320
0
[GI:1914872]
88









[LN:SPZ82001]









[AC:Z82001]









[PN:PCPA]









[GN:pcpA]









[OR:Streptococcus pneumoniae]


SPX1603
1603
4264
76
228


NO-HIT
6


SPX1604
1604
4265
192
576
429
4.10E-54
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX1605
1605
4266
126
378
303
4.10E-37
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX1606
1606
4267
109
327
495
7.70E-65
[GI:1914871]
81









[LN:SPZ82001]









[AC:Z82001]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX1607
1607
4268
627
1881
95
0.00073
[LN:T27355]
100









[AC:T27355]









[PN:hypothetical protein Y70D2A.2]









[GN:Y70D2A.2]









[OR:Caenorhabditis elegans]


SPX1608
1608
4269
290
870
108
2.70E-22
“[LN:F70203]
181









[AC:F70203]









[PN:xylose operon regulatory protein (xylR-2) homolog]









[CL:glucose kinase:glucose kinase homology]









[OR:Borrelia burgdorferi]









[SR:, Lyme disease spirochete]”


SPX1609
1609
4270
887
2661
345
6.30E-65
[LN:YBGG_ECOLI]
151









[AC:P54746:P75753]









[GN:YBGG]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 100.0 KD PROTEIN IN HRSA-CYDA INTERGENIC REGION]









[SP:P54746:P75753]


SPX1610
1610
4271
435
1305
409
6.20E-106
[LN:T37125]
101









[AC:T37125]









[PN:hypothetical protein SCJ4.42c]









[GN:SCJ4.42c]









[OR:Streptomyces coelicolor]


SPX1611
1611
4272
695
2085
408
9.50E-105
[GI:5759293]
108









[LN:AF175722]









[AC:AF175722]









[PN:immunoreactive 89kD antigen PG87]









[OR:Porphyromonas gingivalis]


SPX1612
1612
4273
560
1680
249
2.20E-63
“[GI:4096756]
170









[LN:SSU39394]









[AC:U39394]









[PN:alpha-1,3/4-fucosidase precursor]









[FN:alpha-fucosidase specific for alpha-1,3 and]









[OR:Streptomyces sp.]









[SR:Streptomyces sp]”


SPX1613
1613
4274
410
1230
942
1.30E-244
[LN:SAGP_STRPY]
114









[AC:P16962]









[GN:SAGP]









[OR:Streptococcus pyogenes]









[DE:STREPTOCOCCAL ACID GLYCOPROTEIN]









[SP:P16962]


SPX1614
1614
4275
339
1017
897
3.80E-184
[GI:2764612]
108









[LN:LSAJ1330]









[AC:AJ001330]









[PN:ornithine transcarbamoylase]









[GN:arcB]









[OR:Lactobacillus sakei]


SPX1615
1615
4276
316
948
465
3.40E-129
[GI:2894540]
143









[LN:EFAJ3331]









[AC:AJ223331]









[PN:carbamate kinase]









[GN:arcC]









[FN:synthesis of ATP from carbamylphosphate]









[OR:Enterococcus faecium]


SPX1616
1616
4277
504
1512
426
4.50E-106
[GI:2697115]
75









[LN:AF008219]









[AC:AF008219]









[PN:unknown]









[OR:Borrelia afzelii]


SPX1617
1617
4278
444
1332
277
8.20E-67
[LN:S43914]
101









[AC:S43914]









[PN:hypothetical protein 1]









[CL:peptidase V]









[OR:Bacillus stearothermophilus]


SPX1618
1618
4279
64
192


NO-HIT
6


SPX1619
1619
4280
79
237


NO-HIT
6


SPX1620
1620
4281
89
267


NO-HIT
6


SPX1621
1621
4282
51
153


NO-HIT
6


SPX1622
1622
4283
72
216
176
4.20E-20
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX1623
1623
4284
55
165


NO-HIT
6


SPX1624
1624
4285
300
900
560
2.70E-78
[GI:6714460]
98









[LN:ATAC008261]









[AC:AC008261]









[GN:T4P13.3]









[OR:Arabidopsis thaliana]









[SR:thale cress]


SPX1625
1625
4286
64
192


NO-HIT
6


SPX1626
1626
4287
384
1152
840
1.50E-119
“[LN:ADH2_ECOLI]
123









[AC:P37686]









[GN:YIAY]









[OR:Escherichia coli]









[EC:1.1.1.1]









[DE:PROBABLE ALCOHOL DEHYDROGENASE,]









[SP:P37686]”


SPX1627
1627
4288
589
1767
874
7.80E-287
[GI:6015981]
108









[LN:AF137263]









[AC:AF137263]









[PN:L-fucose isomerase]









[GN:fucI]









[OR:Bacteroides thetaiotaomicron]


SPX1628
1628
4289
243
729
201
8.40E-20
“[LN:B70645]
155









[AC:B70645]









[PN:L-fuculose-phosphate aldolase,]









[GN:fucA]









[CL:L-ribulose-phosphate 4-epimerase]









[OR:Mycobacterium tuberculosis]









[EC:4.1.2.17]”


SPX1629
1629
4290
1029
3087


NO-HIT
6


SPX1630
1630
4291
738
2214
1709
3.00E-243
[GI:4567098]
113









[LN:AF130985]









[AC:AF130985]









[PN:alpha-galactosidase AgaN]









[GN:agaN]









[OR:Bacillus stearothermophilus]


SPX1631
1631
4292
624
1872
112
5.60E-07
[LN:T36462]
101









[AC:T36462]









[PN:hypothetical protein SCF85.02]









[GN:SCF85.02]









[OR:Streptomyces coelicolor]


SPX1632
1632
4293
440
1320
174
1.10E-50
[LN:T36467]
123









[AC:T36467]









[PN:probable glycosyl hydrolase]









[GN:SCF85.07]









[CL:alpha-L-fucosidase]









[OR:Streptomyces coelicolor]


SPX1633
1633
4294
62
186


NO-HIT
6


SPX1634
1634
4295
295
885
372
3.60E-50
[LN:YURM_BACSU]
128









[AC:O32154]









[GN:YURM]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL ABC TRANSPORTER PERMEASE PROTEIN YURM]









[SP:O32154]


SPX1635
1635
4296
310
930
163
7.70E-27
“[LN:E72357]
140









[AC:E72357]









[PN:sugar ABC transporter, permease protein]









[GN:TM0596]









[CL:inner membrane protein malF]









[OR:Thermotoga maritima]”


SPX1636
1636
4297
431
1293
84
5.60E-07
[GI:1524333]
116









[LN:SCMALREFG]









[AC:Y07706]









[PN:putative maltose-binding pootein]









[GN:malE]









[OR:Streptomyces coelicolor]


SPX1637
1637
4298
468
1404
210
2.00E-81
“[LN:E70014]
117









[AC:E70014]









[PN:rhamnulokinase, yulC]









[GN:yulC]









[CL:rhamnulokinase]









[OR:Bacillus subtilis]









[EC:2.7.1.5]”


SPX1638
1638
4299
59
177


NO-HIT
6


SPX1639
1639
4300
258
774
123
7.20E-21
[LN:SRLR_ECOLI]
121









[AC:P15082:P77030]









[GN:SRLR:GUTR]









[OR:Escherichia coli]









[DE:GLUCITOL OPERON REPRESSOR]









[SP:P15082:P77030]


SPX1640
1640
4301
73
219


NO-HIT
6


SPX1641
1641
4302
69
207


NO-HIT
6


SPX1642
1642
4303
502
1506
2158
8.80E-289
[LN:T46756]
107









[AC:T46756]









[PN:Zn-binding lipoprotein adcA [imported]]









[GN:adcA]









[OR:Streptococcus pneumoniae]


SPX1643
1643
4304
269
807
1261
4.10E-177
[LN:T46755]
101









[AC:T46755]









[PN:membrane protein adcB [imported]]









[GN:adcB]









[OR:Streptococcus pneumoniae]


SPX1644
1644
4305
235
705
1247
1.40E-168
[LN:T46754]
92









[AC:T46754]









[PN:AdcC protein [imported]]









[GN:adcC]









[OR:Streptococcus pneumoniae]


SPX1645
1645
4306
64
192
89
1.20E-06
[LN:G72536]
92









[AC:G72536]









[PN:hypothetical protein APE1580]









[GN:APE1580]









[OR:Aeropyrum pernix]


SPX1646
1646
4307
167
501
728
1.10E-95
[LN:T46753]
102









[AC:T46753]









[PN:repressor protein adcR [imported]]









[GN:adcR]









[OR:Streptococcus pneumoniae]


SPX1647
1647
4308
428
1284
612
1.10E-162
[GI:3403204]
96









[LN:AF050517]









[AC:AF050517:S78492]









[PN:unknown]









[GN:dlt4]









[OR:Streptococcus mutans]


SPX1648
1648
4309
80
240
360
8.20E-46
[GI:2981430]
93









[LN:AF049357]









[AC:AF049357:S78492]









[PN:Glg3]









[GN:glg3]









[OR:Streptococcus mutans]


SPX1649
1649
4310
415
1245
1236
2.30E-227
[GI:2952530]
107









[LN:AF051356]









[AC:AF051356]









[PN:integral membrane protein]









[GN:dltB]









[OR:Streptococcus mutans]


SPX1650
1650
4311
517
1551
2154
1.90E-292
[LN:DLTA_STRMU]
144









[AC:Q53526:O68576]









[GN:DLTA]









[OR:Streptococcus mutans]









[EC:6.3.2.-]









[DE:ALANYL CARRIER PROTEIN LIGASE) (DCL)]









[SP:Q53526:O68576]


SPX1651
1651
4312
66
198


NO-HIT
6


SPX1652
1652
4313
174
522
215
3.50E-24
[LN:H69812]
97









[AC:H69812]









[PN:conserved hypothetical protein yfmI]









[GN:yfmI]









[OR:Bacillus subtilis]


SPX1653
1653
4314
237
711
97
2.60E-14
[LN:H69812]
97









[AC:H69812]









[PN:conserved hypothetical protein yfmI]









[GN:yfmI]









[OR:Bacillus subtilis]


SPX1654
1654
4315
62
186


NO-HIT
6


SPX1655
1655
4316
63
189


NO-HIT
6


SPX1656
1656
4317
331
993
1712
2.40E-235
[GI:2804734]
100









[LN:AF030367]









[AC:AF030367]









[PN:maturase-related protein]









[OR:Streptococcus pneumoniae]


SPX1657
1657
4318
94
282
470
6.40E-60
[GI:2804734]
100









[LN:AF030367]









[AC:AF030367]









[PN:maturase-related protein]









[OR:Streptococcus pneumoniae]


SPX1658
1658
4319
82
246


NO-HIT
6


SPX1659
1659
4320
66
198


NO-HIT
6


SPX1660
1660
4321
196
588


NO-HIT
6


SPX1661
1661
4322
68
204
344
4.40E-42
[GI:1217989]
78









[LN:SPU12567]









[AC:U12567]









[PN:ORF3]









[OR:Streptococcus pneumoniae]


SPX1662
1662
4323
253
759
968
2.20E-159
[LN:GLPF_STRPN]
120









[AC:P52281]









[GN:GLPF]









[OR:Streptococcus pneumoniae]









[DE:GLYCEROL UPTAKE FACILITATOR PROTEIN]









[SP:P52281]


SPX1663
1663
4324
609
1827
3058
0
[GI:3551774]
154









[LN:SPU94770]









[AC:U94770]









[PN:alpha-glycerophosphate oxidase]









[GN:glpO]









[FN:oxidizes alpha-glycerophosphate to]









[OR:Streptococcus pneumoniae]


SPX1664
1664
4325
100
300
302
1.90E-38
“[LN:S67936]
166









[AC:S67936]









[PN:glycerol-3-phosphate dehydrogenase homolog GlpD]









[GN:glpD]









[OR:Streptococcus pneumoniae]









[SR:strain P13, , strain P13]









[SR:strain P13, ]”


SPX1665
1665
4326
503
1509
1251
2.90E-274
“[LN:GLPK_ENTFA]
147









[AC:O34154]









[GN:GLPK]









[OR:Enterococcus faecalis]









[SR:,Streptococcus faecalis]









[EC:2.7.1.30]









[DE:(GLYCEROKINASE) (GK)]









[SP:O34154]”


SPX1666
1666
4327
476
1428


NO-HIT
6


SPX1667
1667
4328
66
198


NO-HIT
6


SPX1668
1668
4329
291
873
1063
2.60E-140
[GI:4033717]
79









[LN:SPU49397]









[AC:U49397]









[PN:unknown]









[OR:Streptococcus pyogenes]


SPX1669
1669
4330
327
981
1303
4.70E-175
[GI:4033718]
79









[LN:SPU49397]









[AC:U49397]









[PN:unknown]









[OR:Streptococcus pyogenes]


SPX1670
1670
4331
63
189


NO-HIT
6


SPX1671
1671
4332
222
666
235
4.10E-25
[GI:558538]
179









[LN:SUHSAPI]









[AC:D38490]









[PN:sperm-activating peptide I precursor]









[OR:Hemicentrotus pulcherrimus]









[SR:Hemicentrotus pulcherrimus female ovary accessory cell (library]


SPX1672
1672
4333
451
1353
500
6.50E-65
[GI:4838563]
98









[LN:AF145055]









[AC:AF145055]









[PN:surface protein C PspC]









[OR:Streptococcus pneumoniae]


SPX1673
1673
4334
183
549
213
1.70E-21
[GI:7293488]
106









[LN:AE003509]









[AC:AE003509:AE002593]









[GN:CG15040]









[OR:Drosophila melanogaster]









[SR:fruit fly]


SPX1674
1674
4335
176
528
112
1.00E-08
[GI:406446]
64









[LN:MGU02192]









[AC:U02192]









[OR:Mycoplasma genitalium]


SPX1675
1675
4336
182
546
107
1.20E-15
[GI:3849798]
118









[LN:U91581]









[AC:U91581:U04057]









[PN:putative transposase]









[GN:tpase]









[OR:Lactococcus lactis subsp. lactis]


SPX1676
1676
4337
251
753
175
7.10E-43
[GI:6746427]
90









[LN:AF179847]









[AC:AF179847]









[PN:putative transposase]









[OR:Lactococcus lactis]


SPX1677
1677
4338
65
195


NO-HIT
6


SPX1678
1678
4339
55
165
183
1.50E-19
[GI:2576331]
112









[LN:SPSPSA2]









[AC:AJ002054]









[PN:SpsA protein]









[FN:IgA binding protein]









[OR:Streptococcus pneumoniae]


SPX1679
1679
4340
419
1257
2039
1.30E-284
[GI:2804700]
87









[LN:AF030361]









[AC:AF030361]









[PN:transposase]









[OR:Streptococcus pneumoniae]


SPX1680
1680
4341
232
696
1296
1.20E-171
[GI:4097980]
101









[LN:SPU72655]









[AC:U72655]









[PN:surface protein C]









[GN:pspC]









[OR:Streptococcus pneumoniae]


SPX1681
1681
4342
110
330


NO-HIT
6


SPX1682
1682
4343
105
315
98
7.50E-05
[LN:T14867]
79









[AC:T14867]









[PN:interaptin]









[GN:abpD]









[OR:Dictyostelium discoideum]


SPX1683
1683
4344
217
651
599
1.00E-117
[GI:6469845]
93









[LN:AF068645]









[AC:AF068645]









[PN:unknown]









[GN:pspC]









[OR:Streptococcus pneumoniae]


SPX1684
1684
4345
73
219
66
0.001
“[GI:340613]
163









[LN:LEIKPMURF2]









[AC:L07545]









[GN:MURF2]









[OR:Kinetoplast Leishmania tarentolae]









[SR:Kinetoplast Leishmania tarentolae (strain UC, organelle Kinetoplas]”


SPX1685
1685
4346
105
315
94
1.40E-05
“[LN:YHU3_YEAST]
119









[AC:P38844]









[GN:YHR143W]









[OR:Saccharomyces cerevisiae]









[SR:,Baker′s yeast]









[DE:PRECURSOR]









[SP:P38844]”


SPX1686
1686
4347
276
828
697
7.60E-123
[GI:2576333]
113









[LN:SPSPSA47]









[AC:AJ002055]









[PN:SpsA protein]









[FN:IgA binding protein]









[OR:Streptococcus pneumoniae]


SPX1687
1687
4348
176
528
382
1.80E-50
[LN:F81147]
119









[AC:F81147]









[PN:conserved hypothetical protein NMB0883 [imported]]









[GN:NMB0883]









[OR:Neisseria meningitidis]


SPX1688
1688
4349
447
1341
1245
0
[GI:5830533]
102









[LN:SPAJ6395]









[AC:AJ006395]









[PN:histidine kinase]









[GN:hk06]









[OR:Streptococcus pneumoniae]


SPX1689
1689
4350
218
654
1100
3.60E-150
[GI:5830532]
104









[LN:SPAJ6395]









[AC:AJ006395]









[PN:response regulator]









[GN:rr06]









[OR:Streptococcus pneumoniae]


SPX1690
1690
4351
75
225


NO-HIT
6


SPX1691
1691
4352
811
2433
1102
3.30E-266
[GI:4103472]
84









[LN:AF023422]









[AC:AF023422]









[PN:ClpC]









[GN:clpC]









[OR:Lactococcus lactis]


SPX1692
1692
4353
174
522
323
4.90E-44
[LN:LLA249133]
111









[AC:AJ249133]









[PN:CtsR protein]









[GN:ctsR]









[FN:transcriptional regulator]









[OR:Lactococcus lactis]


SPX1693
1693
4354
243
729
255
1.80E-47
“[LN:B72369]
180









[AC:B72369]









[PN:ABC transporter, ATP-binding protein]









[GN:TM0483]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Thermotoga maritima]”


SPX1694
1694
4355
336
1008
561
9.10E-87
[LN:C72369]
93









[AC:C72369]









[PN:hypothetical protein TM0484]









[GN:TM0484]









[OR:Thermotoga maritima]


SPX1695
1695
4356
136
408


NO-HIT
6


SPX1696
1696
4357
250
750
440
1.10E-58
“[LN:D72369]
165









[AC:D72369]









[PN:ABC transporter, permease protein, cysTW family]









[GN:TM0485]









[CL:Synechococcus nitrate transport protein nrtB]









[OR:Thermotoga maritima]”


SPX1697
1697
4358
97
291
118
4.00E-14
[LN:YVI2_CLOPE]
126









[AC:Q46213]









[OR:Clostridium perfringens]









[DE:HYPOTHETICAL 10.7 KD PROTEIN IN VIRR 5′REGION (ORF2)]









[SP:Q46213]


SPX1698
1698
4359
284
852
319
8.30E-35
[LN:S57721]
98









[AC:S57721]









[PN:cspB protein]









[CL:cpl repeat homology]









[OR:Clostridium acetobutylicum]


SPX1699
1699
4360
138
414
102
7.10E-06
[GI:1340128]
63









[LN:SA1234]









[AC:X97985]









[OR:Staphylococcus aureus]


SPX1700
1700
4361
89
267
72
3.10E-05
[LN:VEG_BACSU]
87









[AC:P37466]









[GN:VEG]









[OR:Bacillus subtilis]









[DE:VEG PROTEIN]









[SP:P37466]


SPX1701
1701
4362
451
1353
827
1.60E-171
“[LN:DNAC_BACSU]
118









[AC:P37469]









[GN:DNAC]









[OR:Bacillus subtilis]









[EC:3.6.1.-]









[DE:REPLICATIVE DNA HELICASE,]









[SP:P37469]”


SPX1702
1702
4363
151
453
193
1.20E-44
[LN:RL9_BACST]
118









[AC:P02417]









[GN:RPLI]









[OR:Bacillus stearothermophilus]









[DE:50S RIBOSOMAL PROTEIN L9 (BL17)]









[SP:P02417]


SPX1703
1703
4364
658
1974
301
6.60E-68
[LN:YYBT_BACSU]
137









[AC:P37484]









[GN:YYBT]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 74.3 KD PROTEIN IN RPLI-COTF INTERGENIC REGION]









[SP:P37484]


SPX1704
1704
4365
183
549
358
5.10E-68
[LN:LLA249134]
78









[AC:AJ249134]









[PN:hypothetical protein]









[OR:Lactococcus lactis]


SPX1705
1705
4366
221
663
143
2.90E-23
[LN:CMF3_BACSU]
106









[AC:P39147]









[GN:COMFC:COMF3]









[OR:Bacillus subtilis]









[DE:COMF OPERON PROTEIN 3]









[SP:P39147]


SPX1706
1706
4367
433
1299
269
2.00E-31
[LN:CMF1_BACSU]
106









[AC:P39145]









[GN:COMFA:COMF1]









[OR:Bacillus subtilis]









[DE:COMF OPERON PROTEIN 1]









[SP:P39145]


SPX1707
1707
4368
212
636
475
1.00E-60
[LN:YVYE_BACSU]
156









[AC:P32437:P96500]









[GN:YVYE:YVHK]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 24.8 KD PROTEIN IN DEGS-TAGO INTERGENIC REGION]









[SP:P32437:P96500]


SPX1708
1708
4369
309
927
1289
7.30E-171
[GI:6567187]
141









[LN:AB028865]









[AC:AB028865]









[PN:O-acetylserine lyase]









[GN:cysM]









[OR:Streptococcus suis]









[SR:Streptococcus suis (strain:SMR) DNA]


SPX1709
1709
4370
347
1041
498
1.10E-82
[LN:EFTS_BACSU]
119









[AC:P80700:O31748]









[GN:TSF]









[OR:Bacillus subtilis]









[DE:ELONGATION FACTOR TS (EF-TS)]









[SP:P80700:O31748]


SPX1710
1710
4371
129
387


NO-HIT
6


SPX1711
1711
4372
288
864
1013
1.60E-135
[LN:RS2_PEDAC]
108









[AC:P49668]









[GN:RPSB]









[OR:Pediococcus acidilactici]









[DE:30S RIBOSOMAL PROTEIN S2]









[SP:P49668]


SPX1712
1712
4373
75
225


NO-HIT
6


SPX1713
1713
4374
393
1179
459
3.30E-76
[LN:JN0097]
83









[AC:JN0097]









[PN:secreted 45K protein precursor]









[OR:Lactococcus lactis]


SPX1714
1714
4375
80
240


NO-HIT
6


SPX1715
1715
4376
165
495
108
7.90E-08
[LN:MRED_BACSU]
117









[AC:Q01467]









[GN:MRED:RODB]









[OR:Bacillus subtilis]









[DE:ROD SHAPE-DETERMINING PROTEIN MRED]









[SP:Q01467]


SPX1716
1716
4377
273
819
141
1.60E-17
[LN:MREC_BACSU]
112









[AC:Q01466]









[GN:MREC]









[OR:Bacillus subtilis]









[DE:ROD SHAPE-DETERMINING PROTEIN MREC]









[SP:Q01466]


SPX1717
1717
4378
265
795
694
1.30E-95
[LN:F69742]
87









[AC:F69742]









[PN:hypothetical protein ybaF]









[GN:ybaF]









[OR:Bacillus subtilis]


SPX1718
1718
4379
57
171


NO-HIT
6


SPX1719
1719
4380
280
840
623
4.20E-94
[LN:E69742]
188









[AC:E69742]









[PN:ABC transporter (ATP-binding protein) homolog ybaE]









[GN:ybaE]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Bacillus subtilis]


SPX1720
1720
4381
116
348
127
7.40E-11
[LN:C71234]
95









[AC:C71234]









[PN:hypothetical protein PH0133]









[GN:PH0133]









[OR:Pyrococcus horikoshii]


SPX1721
1721
4382
262
786
853
1.50E-116
[GI:3426368]
119









[LN:AF082738]









[AC:AF082738]









[PN:ABC transporter ATP-binding protein]









[GN:stpA]









[OR:Streptococcus pyogenes]


SPX1722
1722
4383
75
225
106
1.30E-09
[LN:A71007]
95









[AC:A71007]









[PN:hypothetical protein PH1351]









[GN:PH1351]









[OR:Pyrococcus horikoshii]


SPX1723
1723
4384
182
546
531
6.40E-72
[GI:3426367]
121









[LN:AF082738]









[AC:AF082738]









[PN:phosphotidylglycerophosphate synthase]









[GN:pgsA]









[OR:Streptococcus pyogenes]


SPX1724
1724
4385
277
831
100
1.50E-21
[GI:3426366]
81









[LN:AF082738]









[AC:AF082738]









[PN:unknown]









[OR:Streptococcus pyogenes]


SPX1725
1725
4386
428
1284
403
1.10E-102
[GI:3426365]
81









[LN:AF082738]









[AC:AF082738]









[PN:unknown]









[OR:Streptococcus pyogenes]


SPX1726
1726
4387
417
1251
694
2.70E-103
[GI:3426364]
81









[LN:AF082738]









[AC:AF082738]









[PN:unknown]









[OR:Streptococcus pyogenes]


SPX1727
1727
4388
123
369
148
1.20E-26
[LN:JC4754]
89









[AC:JC4754]









[PN:hypothetical 13.6k protein]









[GN:recF]









[OR:Lactococcus lactis]


SPX1728
1728
4389
366
1098
1127
1.20E-163
[LN:RECF_STRPY]
95









[AC:P49999]









[GN:RECF]









[OR:Streptococcus pyogenes]









[DE:RECF PROTEIN]









[SP:P49999]


SPX1729
1729
4390
493
1479
2283
0
[LN:IMDH_STRPY]
127









[AC:P50099]









[GN:GUAB]









[OR:Streptococcus pyogenes]









[EC:1.1.1.205]









[DE:DEHYDROGENASE) (IMPDH) (IMPD)]









[SP:P50099]


SPX1730
1730
4391
49
147
99
1.30E-07
[LN:F71456]
95









[AC:F71456]









[PN:hypothetical protein PH0308]









[GN:PH0308]









[OR:Pyrococcus horikoshii]


SPX1731
1731
4392
342
1026
672
2.00E-153
[LN:SYW_CLOLO]
108









[AC:Q46127]









[GN:TRPS:TRSA]









[OR:Clostridium longisporum]









[EC:6.1.1.2]









[DE:(TRPRS)]









[SP:Q46127]


SPX1732
1732
4393
541
1623
1364
9.40E-252
[LN:E69861]
188









[AC:E69861]









[PN:ABC transporter (ATP-binding protein) homolog ykpA]









[GN:ykpA]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Bacillus subtilis]


SPX1733
1733
4394
851
2553
503
1.40E-88
[GI:3043878]
94









[LN:LLU95840]









[AC:U95840]









[PN:transmembrane protein Tmp5]









[OR:Lactococcus lactis]


SPX1734
1734
4395
105
315
181
5.50E-19
[LN:YHGE_BACSU]
144









[AC:P32399]









[GN:YHGE]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 84.1 KD PROTEIN IN HEMY-GLTT INTERGENIC REGION (ORFB)]









[SP:P32399]


SPX1735
1735
4396
113
339
138
1.10E-11
[LN:YHGE_BACSU]
144









[AC:P32399]









[GN:YHGE]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 84.1 KD PROTEIN IN HEMY-GLTT INTERGENIC REGION (ORFB)]









[SP:P32399]


SPX1736
1736
4397
256
768
307
2.50E-46
[GI:3043882]
94









[LN:LLU95842]









[AC:U95842]









[PN:transmembrane protein Tmp7]









[OR:Lactococcus lactis]


SPX1737
1737
4398
181
543
98
5.30E-09
[GI:6899263]
113









[LN:AE002125]









[AC:AE002125:AF222894]









[PN:unique hypothetical]









[GN:UU290]









[OR:Ureaplasma urealyticum]


SPX1738
1738
4399
251
753
1294
2.50E-176
[GI:1613769]
102









[LN:SPU33315]









[AC:U33315]









[PN:response regulator]









[GN:comE]









[OR:Streptococcus pneumoniae]


SPX1739
1739
4400
442
1326
2246
0
[GI:1613768]
108









[LN:SPU33315]









[AC:U33315]









[PN:histidine protein kinase]









[GN:comD]









[OR:Streptococcus pneumoniae]


SPX1740
1740
4401
160
480
781
4.50E-104
[GI:2109449]
83









[LN:SPDNAARG]









[AC:AF000658]









[FN:unknown]









[OR:Streptococcus pneumoniae]


SPX1741
1741
4402
398
1194
1963
8.90E-259
[GI:2109443]
112









[LN:SPDNAARG]









[AC:AF000658]









[PN:putative serine protease]









[GN:sphtra]









[OR:Streptococcus pneumoniae]


SPX1742
1742
4403
253
759
1225
5.80E-163
[GI:2109444]
107









[LN:SPDNAARG]









[AC:AF000658]









[PN:SPSpoJ]









[GN:spspoJ]









[FN:unknown]









[OR:Streptococcus pneumoniae]


SPX1743
1743
4404
454
1362
2287
0
[LN:DNAA_STRPN]
131









[AC:O08397]









[GN:DNAA]









[OR:Streptococcus pneumoniae]









[DE:CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA]









[SP:O08397]


SPX1744
1744
4405
379
1137
1857
2.90E-250
“[LN:DP3B_STRPN]
131









[AC:O06672]









[GN:DNAN]









[OR:Streptococcus pneumoniae]









[EC:2.7.7.7]









[DE:DNA POLYMERASE III, BETA CHAIN,]









[SP:O06672]”


SPX1745
1745
4406
65
195
339
1.60E-43
[GI:2109447]
83









[LN:SPDNAARG]









[AC:AF000658]









[FN:unknown]









[OR:Streptococcus pneumoniae]


SPX1746
1746
4407
375
1125
710
9.10E-176
[LN:YYAF_BACSU]
84









[AC:P37518]









[GN:YYAF]









[OR:Bacillus subtilis]









[DE:REGION]









[SP:P37518]


SPX1747
1747
4408
190
570
368
3.70E-62
[LN:SP5C_BACSU]
119









[AC:P37470]









[GN:SPOVC:PTH]









[OR:Bacillus subtilis]









[EC:3.1.1.29]









[DE:SPORULATION PROTEIN C)]









[SP:P37470]


SPX1748
1748
4409
1170
3510
2088
0
[GI:3511015]
116









[LN:AF054624]









[AC:AF054624]









[PN:transcription-repair coupling factor]









[GN:mfd]









[OR:Lactobacillus sakei]


SPX1749
1749
4410
99
297


NO-HIT
6


SPX1750
1750
4411
89
267
275
3.50E-33
[LN:YABO_BACSU]
136









[AC:P37557]









[GN:YABO]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 9.7 KD PROTEIN IN MFD-DIVIC INTERGENIC REGION]









[SP:P37557]


SPX1751
1751
4412
123
369
112
1.50E-08
[GI:4090866]
97









[LN:AF023181]









[AC:AF023181]









[PN:DivIC homolog]









[GN:divL]









[OR:Listeria monocytogenes]


SPX1752
1752
4413
74
222


NO-HIT
6


SPX1753
1753
4414
446
1338


NO-HIT
6


SPX1754
1754
4415
426
1278
128
6.70E-28
[LN:D72358]
129









[AC:D72358]









[PN:conserved hypothetical protein]









[GN:TM0579]









[CL:hypothetical protein HI0404]









[OR:Thermotoga maritima]


SPX1755
1755
4416
181
543
374
1.10E-80
“[LN:HPRT_LACLA]
142









[AC:Q02522]









[GN:HPT]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:2.4.2.8]









[DE:(HGPRTASE)]









[SP:Q02522]”


SPX1756
1756
4417
653
1959
3277
0
[GI:5030426]
112









[LN:AF061748]









[AC:AF061748]









[PN:cell division protein FtsH]









[GN:ftsH]









[OR:Streptococcus pneumoniae]


SPX1757
1757
4418
208
624
181
9.80E-25
[LN:A71115]
95









[AC:A71115]









[PN:hypothetical protein PH0688]









[GN:PH0688]









[OR:Pyrococcus horikoshii]


SPX1758
1758
4419
36
108


NO-HIT
6


SPX1759
1759
4420
160
480
844
9.40E-114
[GI:5739312]
126









[LN:AF161700]









[AC:AF161700]









[PN:ComX1]









[GN:comX1]









[FN:transcriptional regulator of]









[OR:Streptococcus pneumoniae]


SPX1760
1760
4421
82
246


NO-HIT
6


SPX1761
1761
4422
50
150
82
7.60E-06
[LN:G71244]
95









[AC:G71244]









[PN:hypothetical protein PH0217]









[GN:PH0217]









[OR:Pyrococcus horikoshii]


SPX1762
1762
4423
62
186


NO-HIT
6


SPX1763
1763
4424
87
261
136
3.90E-14
[LN:G81516]
130









[AC:G81516]









[PN:hypothetical protein CP0988 [imported]]









[GN:CP0988]









[OR:Chlamydophila pneumoniae:Chlamydia pneumoniae]


SPX1764
1764
4425
136
408


NO-HIT
6


SPX1765
1765
4426
52
156


NO-HIT
6


SPX1766
1766
4427
52
156
87
3.30E-06
[LN:D75542]
90









[AC:D75542]









[PN:hypothetical protein]









[GN:DR0254]









[OR:Deinococcus radiodurans]


SPX1767
1767
4428
82
246
247
1.10E-29
[LN:F81737]
131









[AC:F81737]









[PN:hypothetical protein TC0129 [imported]]









[GN:TC0129]









[OR:Chlamydia muridarum:Chlamydia trachomatis MoPn]


SPX1768
1768
4429
78
234
143
4.90E-15
[LN:F71245]
95









[AC:F71245]









[PN:hypothetical protein PHS004]









[GN:PHS004]









[OR:Pyrococcus horikoshii]


SPX1769
1769
4430
69
207
340
7.40E-44
[GI:5019553]
97









[LN:SPN239004]









[AC:AJ239004]









[PN:putative transposase]









[OR:Streptococcus pneumoniae]


SPX1770
1770
4431
82
246
256
1.40E-36
[GI:663279]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX1771
1771
4432
47
141
119
1.30E-09
[GI:2804700]
87









[LN:AF030361]









[AC:AF030361]









[PN:transposase]









[OR:Streptococcus pneumoniae]


SPX1772
1772
4433
91
273
387
3.30E-50
[GI:663278]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX1773
1773
4434
81
243


NO-HIT
6


SPX1774
1774
4435
443
1329
1739
2.60E-235
“[LN:A42280]
175









[AC:S65968:A42280:H69683]









[PN:adenylosuccinate synthase, purA:IMP--aspartate ligase]









[GN:purA]









[CL:adenylosuccinate synthase]









[OR:Bacillus subtilis]









[EC:6.3.4.4]”


SPX1775
1775
4436
141
423
365
1.90E-46
[LN:YAAJ_BACSU]
137









[AC:P21335]









[GN:YAAJ]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 17.8 KD PROTEIN IN SERS-DNAH INTERGENIC REGION]









[SP:P21335]


SPX1776
1776
4437
148
444
205
2.80E-38
[GI:2765131]
76









[LN:LLABIKORF]









[AC:Y11901]









[PN:dUTPase]









[OR:Lactococcus lactis]


SPX1777
1777
4438
186
558


NO-HIT
6


SPX1778
1778
4439
68
204


NO-HIT
6


SPX1779
1779
4440
455
1365
1167
1.60E-201
[LN:RADA_BACSU]
146









[AC:P37572]









[GN:RADA:SMS]









[OR:Bacillus subtilis]









[DE:DNA REPAIR PROTEIN RADA HOMOLOG (DNA REPAIR PROTEIN SMS HOMOLOG)]









[SP:P37572]


SPX1780
1780
4441
207
621


NO-HIT
6


SPX1781
1781
4442
166
498
268
2.80E-38
[LN:Y023_MYCTU]
130









[AC:Q10612]









[GN:MTCY373.03]









[OR:Mycobacterium tuberculosis]









[DE:HYPOTHETICAL 18.2 KD PROTEIN CY373.03]









[SP:Q10612]


SPX1782
1782
4443
264
792


NO-HIT
6


SPX1783
1783
4444
323
969
607
9.40E-148
[GI:532204]
118









[LN:LISTMS]









[AC:M92842]









[GN:prs]









[OR:Listeria monocytogenes]









[SR:Listeria monocytogenes (strain L028) DNA]


SPX1784
1784
4445
160
480
493
3.90E-65
[GI:663278]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX1785
1785
4446
113
339


NO-HIT
6


SPX1786
1786
4447
122
366


NO-HIT
6


SPX1787
1787
4448
131
393


NO-HIT
6


SPX1788
1788
4449
118
354


NO-HIT
6


SPX1789
1789
4450
890
2670
4412
0
“[LN:DPO1_STRPN]
125









[AC:P13252]









[GN:POLA]









[OR:Streptococcus pneumoniae]









[EC:2.7.7.7]









[DE:DNA POLYMERASE I, (POL I)]









[SP:P13252]”


SPX1790
1790
4451
124
372
181
3.30E-32
[LN:B69892]
128









[AC:B69892]









[PN:conserved hypothetical protein yneT]









[GN:yneT]









[CL:hypothetical protein yneT]









[OR:Bacillus subtilis]


SPX1791
1791
4452
137
411
328
2.80E-41
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX1792
1792
4453
105
315
83
0.00036
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX1793
1793
4454
239
717
398
3.00E-50
[LN:YOR3_BACCE]
104









[AC:O31352]









[OR:Bacillus cereus]









[DE:HYPOTHETICAL PROTEIN (ORF3) (FRAGMENT)]









[SP:O31352]


SPX1794
1794
4455
171
513
212
5.40E-30
[LN:YF05_METTH]
128









[AC:O27549]









[GN:MTH1505]









[OR:Methanobacterium thermoautotrophicum]









[DE:HYPOTHETICAL PROTEIN MTH1505]









[SP:O27549]


SPX1795
1795
4456
126
378


NO-HIT
6


SPX1796
1796
4457
167
501
456
2.50E-57
[LN:RL10_BACSU]
111









[AC:P42923]









[GN:RPLJ]









[OR:Bacillus subtilis]









[DE:(VEGETATIVE PROTEIN 300) (VEG300)]









[SP:P42923]


SPX1797
1797
4458
123
369
255
1.30E-46
“[LN:RL7_MICLU]
150









[AC:P02395]









[GN:RPLL]









[OR:Micrococcus luteus]









[SR:,Micrococcus lysodeikticus]









[DE:50S RIBOSOMAL PROTEIN L7/L12 (MA1/MA2)]









[SP:P02395]”


SPX1798
1798
4459
115
345
98
1.30E-05
[LN:T40374]
92









[AC:T40374]









[PN:hypothetical protein SPBC3D6.14c]









[OR:Schizosaccharomyces pombe]


SPX1799
1799
4460
196
588


NO-HIT
6


SPX1800
1800
4461
505
1515
214
1.60E-47
[LN:T35180]
160









[AC:T35180]









[PN:hypothetical protein SC5A7.31]









[GN:SC5A7.31]









[CL:Streptomyces coelicolor hypothetical protein SC5A7.31]









[OR:Streptomyces coelicolor]


SPX1801
1801
4462
198
594
136
6.60E-20
[GI:290801]
133









[LN:FRNVALAB]









[AC:L17003]









[GN:valA]









[OR:Francisella tularensis var. novicida]









[SR:Francisella novicida (strain U112) DNA]


SPX1802
1802
4463
97
291


NO-HIT
6


SPX1803
1803
4464
247
741
357
1.50E-55
[GI:7288062]
139









[LN:SCD40A]









[AC:AL161691]









[PN:putative ABC-transporter ATP-binding protein]









[GN:SCD40A.12c]









[OR:Streptomyces coelicolor A3(2)]


SPX1804
1804
4465
60
180


NO-HIT
6


SPX1805
1805
4466
129
387
90
6.90E-06
[LN:F72598]
92









[AC:F72598]









[PN:hypothetical protein APE1254]









[GN:APE1254]









[OR:Aeropyrum pernix]


SPX1806
1806
4467
440
1320


NO-HIT
6


SPX1807
1807
4468
60
180


NO-HIT
6


SPX1808
1808
4469
74
222


NO-HIT
6


SPX1809
1809
4470
45
135
109
3.10E-09
“[LN:Y4PE_RHISN]
138









[AC:P55614]









[GN:Y4PE,Y4SA]









[OR:Rhizobium sp]









[SR:,strain NGR234]









[DE:HYPOTHETICAL 15.5 KD PROTEIN Y4PE/Y4SA]









[SP:P55614]”


SPX1810
1810
4471
88
264
301
4.50E-37
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX1811
1811
4472
233
699
331
2.60E-64
“[LN:C70180]
125









[AC:C70180]









[PN:conserved hypothetical protein BB0644]









[OR:Borrelia burgdorferi]









[SR:, Lyme disease spirochete]”


SPX1812
1812
4473
308
924
98
4.30E-21
[LN:I40867]
80









[AC:I40867]









[PN:hypothetical protein 2]









[OR:Clostridium perfringens]


SPX1813
1813
4474
543
1629
102
3.10E-21
[LN:B71130]
143









[AC:B71130]









[PN:probable oligopeptide binding protein APPA]









[GN:PH0807]









[CL:dipeptide transport protein]









[OR:Pyrococcus horikoshii]


SPX1814
1814
4475
317
951
335
2.30E-78
“[LN:D75202]
166









[AC:D75202]









[PN:dipeptide abc transporter, dipeptide-binding protein PAB0092]









[GN:dppB-1:PAB0092]









[CL:transmembrane protein dppB]









[OR:Pyrococcus abyssi]”


SPX1815
1815
4476
296
888
642
5.70E-87
[LN:APPC_BACSU]
122









[AC:P42063]









[GN:APPC]









[OR:Bacillus subtilis]









[DE:OLIGOPEPTIDE TRANSPORT PERMEASE PROTEIN APPC]









[SP:P42063]


SPX1816
1816
4477
204
612


NO-HIT
6


SPX1817
1817
4478
661
1983
644
1.60E-146
[LN:YLIA_ECOLI]
130









[AC:P75796]









[GN:YLIA]









[OR:Escherichia coli]









[DE:HYPOTHETICAL ABC TRANSPORTER ATP-BINDING PROTEIN YLIA]









[SP:P75796]


SPX1818
1818
4479
66
198


NO-HIT
6


SPX1819
1819
4480
470
1410


NO-HIT
6


SPX1820
1820
4481
163
489
450
8.60E-58
[LN:YUTG_BACSU]
136









[AC:O32124]









[GN:YUTG]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 18.7 KD PROTEIN IN HOM-MRGA INTERGENIC REGION]









[SP:O32124]


SPX1821
1821
4482
136
408
190
1.30E-38
“[LN:CDD_BACSU]
142









[AC:P19079]









[GN:CDD]









[OR:Bacillus subtilis]









[EC:3.5.4.5]









[DE:CYTIDINE DEAMINASE, (CYTIDINE AMINOHYDROLASE) (CDA)]









[SP:P19079]”


SPX1822
1822
4483
95
285


NO-HIT
6


SPX1823
1823
4484
274
822
771
1.10E-101
[GI:2385360]
100









[LN:CTSIALIDA]









[AC:Y08695]









[PN:putative acylneuraminate lyase]









[OR:Clostridium tertium]


SPX1824
1824
4485
68
204
173
1.10E-18
[LN:S43901]
87









[AC:S43901:S27537]









[PN:hypothetical protein A]









[OR:Clostridium perfringens]


SPX1825
1825
4486
173
519
145
3.80E-20
[GI:2668605]
82









[LN:AF015453]









[AC:AF015453]









[PN:unknown]









[OR:Lactobacillus rhamnosus]


SPX1826
1826
4487
214
642
509
7.20E-64
[GI:6318176]
131









[LN:BSP250862]









[AC:AJ250862]









[PN:MrsT protein]









[GN:mrsT]









[FN:putative ABC-transporter]









[OR:Bacillus sp. HIL-Y85/54728]


SPX1827
1827
4488
63
189


NO-HIT
6


SPX1828
1828
4489
449
1347
731
5.00E-191
[GI:3702805]
121









[LN:AF056335]









[AC:AF056335]









[PN:NADP-specific glutamate dehydrogenase]









[GN:gdhA]









[OR:Bacillus licheniformis]


SPX1829
1829
4490
138
414
99
6.40E-06
[LN:S31840]
82









[AC:S31840]









[PN:probable transposase]









[OR:Bacillus stearothermophilus]


SPX1830
1830
4491
57
171
94
3.30E-07
“[LN:Y4PE_RHISN]
138









[AC:P55614]









[GN:Y4PE,Y4SA]









[OR:Rhizobium sp]









[SR:,strain NGR234]









[DE:HYPOTHETICAL 15.5 KD PROTEIN Y4PE/Y4SA]









[SP:P55614]”


SPX1831
1831
4492
218
654
154
1.00E-20
[GI:722339]
100









[LN:AXU22323]









[AC:U22323]









[PN:unknown]









[OR:Acetobacter xylinus]









[SR:Acetobacter xylinum]


SPX1832
1832
4493
73
219


NO-HIT
6


SPX1833
1833
4494
95
285
146
8.10E-34
[GI:4193373]
105









[LN:AF072894]









[AC:AF072894]









[PN:ribosomal protein L31]









[GN:rpmE]









[OR:Listeria monocytogenes]


SPX1834
1834
4495
312
936
397
7.80E-97
[LN:F69999]
150









[AC:F69999]









[PN:conserved hypothetical protein ytqI]









[GN:ytqI]









[CL:Mycoplasma conserved hypothetical protein MG190]









[OR:Bacillus subtilis]


SPX1835
1835
4496
145
435
271
2.00E-32
[LN:FLAV_BACSU]
99









[AC:O34737]









[GN:YKUN]









[OR:Bacillus subtilis]









[DE:PROBABLE FLAVODOXIN 1]









[SP:O34737]


SPX1836
1836
4497
89
267
117
2.80E-11
[LN:Y246_METJA]
114









[AC:Q57696]









[GN:MJ0246]









[OR:Methanococcus jannaschii]









[DE:HYPOTHETICAL PROTEIN MJ0246]









[SP:Q57696]


SPX1837
1837
4498
125
375
169
5.60E-18
[LN:C75108]
118









[AC:C75108]









[PN:crcb protein PAB1925]









[GN:PAB1925]









[CL:hypothetical protein MJ1523]









[OR:Pyrococcus abyssi]


SPX1838
1838
4499
110
330
93
1.20E-10
[LN:B71026]
128









[AC:B71026]









[PN:hypothetical protein PH1502]









[GN:PH1502]









[CL:hypothetical protein MJ1523]









[OR:Pyrococcus horikoshii]


SPX1839
1839
4500
116
348
537
4.70E-71
[LN:RL19_STRTR]
112









[AC:O34031]









[GN:RPLS]









[OR:Streptococcus thermophilus]









[DE:50S RIBOSOMAL PROTEIN L19]









[SP:O34031]


SPX1840
1840
4501
269
807
354
2.70E-85
[LN:YIDA_ECOLI]
150









[AC:P09997:P76737]









[GN:YIDA]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 29.7 KD PROTEIN IN IBPA-GYRB INTERGENIC REGION]









[SP:P09997:P76737]


SPX1841
1841
4502
448
1344
561
2.90E-126
[LN:YWFO_BACSU]
130









[AC:P39651]









[GN:YWFO:IPA-93D]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 51.0 KD PROTEIN IN PTA 3′REGION]









[SP:P39651]


SPX1842
1842
4503
126
378


NO-HIT
6


SPX1843
1843
4504
111
333
499
3.70E-65
[GI:1850606]
97









[LN:SMU88582]









[AC:U88582]









[PN:YlxM]









[GN:ylxM]









[FN:unknown]









[OR:Streptococcus mutans]


SPX1844
1844
4505
185
555


NO-HIT
6


SPX1845
1845
4506
524
1572
1993
5.90E-290
[LN:SR54_STRMU]
150









[AC:Q54431:P96469]









[GN:FFH]









[OR:Streptococcus mutans]









[DE:SIGNAL RECOGNITION PARTICLE PROTEIN (FIFTY-FOUR HOMOLOG)]









[SP:Q54431:P96469]


SPX1846
1846
4507
163
489


NO-HIT
6


SPX1847
1847
4508
257
771
500
1.10E-87
[LN:PYRP_BACCL]
118









[AC:P41006]









[GN:PYRP]









[OR:Bacillus caldolyticus]









[DE:URACIL PERMEASE (URACIL TRANSPORTER)]









[SP:P41006]


SPX1848
1848
4509
147
441
231
5.00E-42
[LN:LLA132624]
86









[AC:AJ132624]









[PN:uracil transporter]









[GN:pyrP]









[OR:Lactococcus lactis]


SPX1849
1849
4510
238
714
353
3.70E-81
[LN:GIDB_BACSU]
114









[AC:P25813]









[GN:GIDB]









[OR:Bacillus subtilis]









[DE:GLUCOSE INHIBITED DIVISION PROTEIN B]









[SP:P25813]


SPX1850
1850
4511
187
561
261
1.60E-57
[GI:1519287]
86









[LN:LMU66186]









[AC:U66186]









[PN:LemA]









[GN:lemA]









[OR:Listeria monocytogenes]


SPX1851
1851
4512
303
909
757
1.70E-165
[LN:HTPX_STRGC]
123









[AC:O30795]









[GN:HTPX]









[OR:Streptococcus gordonii challis]









[DE:PUTATIVE HEAT SHOCK PROTEIN HTPX]









[SP:O30795]


SPX1852
1852
4513
520
1560
197
1.40E-47
[LN:YHES_ECOLI]
130









[AC:P45535]









[GN:YHES]









[OR:Escherichia coli]









[DE:HYPOTHETICAL ABC TRANSPORTER ATP-BINDING PROTEIN YHES]









[SP:P45535]


SPX1853
1853
4514
92
276


NO-HIT
6


SPX1854
1854
4515
122
366


NO-HIT
6


SPX1855
1855
4516
181
543
64
6.40E-07
[LN:C69875]
87









[AC:C69875]









[PN:hypothetical protein ylbN]









[GN:ylbN]









[OR:Bacillus subtilis]


SPX1856
1856
4517
62
186


NO-HIT
6


SPX1857
1857
4518
210
630
446
2.10E-57
[LN:END3_BACSU]
122









[AC:P39788]









[GN:NTH:JOOB]









[OR:Bacillus subtilis]









[EC:4.2.99.18]









[DE:APYRIMIDINIC SITE) LYASE)]









[SP:P39788]


SPX1858
1858
4519
174
522
626
4.30E-82
[LN:LLA132624]
141









[AC:AJ132624]









[PN:pyrimidine regulatory protein]









[GN:pyrR]









[FN:Regulates expression of the pyrimidine]









[OR:Lactococcus lactis]


SPX1859
1859
4520
308
924
942
6.40E-134
[LN:LLA132624]
95









[AC:AJ132624]









[PN:aspartate transcarbamoylase]









[GN:pyrB]









[OR:Lactococcus lactis]


SPX1860
1860
4521
360
1080
1492
2.60E-202
[LN:LLA132624]
112









[AC:AJ132624]









[PN:carbamoyl phosphate synthetase small subunit]









[GN:carA]









[OR:Lactococcus lactis]


SPX1861
1861
4522
1059
3177
4000
0
[GI:2598551]
108









[LN:LLAJ109]









[AC:AJ000109]









[PN:carbamoylphosphate synthetase]









[GN:carB]









[OR:Lactococcus lactis]


SPX1862
1862
4523
70
210


NO-HIT
6


SPX1863
1863
4524
281
843
1425
1.90E-195
[GI:5001693]
92









[LN:AF106539]









[AC:AF106539]









[PN:LicD2]









[GN:licD2]









[OR:Streptococcus pneumoniae]


SPX1864
1864
4525
268
804
1419
6.40E-194
[GI:5001692]
92









[LN:AF106539]









[AC:AF106539]









[PN:LicD1]









[GN:licD1]









[OR:Streptococcus pneumoniae]


SPX1865
1865
4526
496
1488
2483
0
[GI:5001691]
83









[LN:AF106539]









[AC:AF106539]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX1866
1866
4527
236
708
96
7.30E-17
[LN:S60902]
100









[AC:S60902:S49238:S44071]









[PN:CDP-ribitol pyrophosphorylase]









[OR:Haemophilus influenzae]


SPX1867
1867
4528
347
1041
66
6.20E-05
[LN:YJJN_ECOLI]
94









[AC:P39400]









[GN:YJJN]









[OR:Escherichia coli]









[DE:INTERGENIC REGION]









[SP:P39400]


SPX1868
1868
4529
290
870
1361
2.10E-181
[GI:2708632]
99









[LN:AF036951]









[AC:AF036951]









[PN:choline kinase]









[GN:pck]









[OR:Streptococcus pneumoniae]


SPX1869
1869
4530
293
879
156
1.70E-15
[LN:LICB_HAEIN]
130









[AC:P14182:Q57357:O05075]









[GN:LICB:HI1538]









[OR:Haemophilus influenzae]









[DE:LICB PROTEIN]









[SP:P14182:Q57357:O05075]


SPX1870
1870
4531
230
690
345
4.10E-54
[LN:D64128]
82









[AC:D64128]









[PN:lic-1 protein C]









[GN:licC]









[OR:Haemophilus influenzae]


SPX1871
1871
4532
283
849
458
8.00E-59
[LN:C72399]
88









[AC:C72399]









[PN:DNA processing chain A]









[GN:TM0250]









[OR:Thermotoga maritima]


SPX1872
1872
4533
171
513
309
5.10E-41
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX1873
1873
4534
152
456
107
1.30E-07
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX1874
1874
4535
69
207


NO-HIT
6


SPX1875
1875
4536
348
1044
179
2.10E-23
[LN:Y678_METJA]
114









[AC:Q58091]









[GN:MJ0678]









[OR:Methanococcus jannaschii]









[DE:HYPOTHETICAL PROTEIN MJ0678]









[SP:Q58091]


SPX1876
1876
4537
702
2106
1065
0
[LN:TOP1_BACSU]
128









[AC:P39814]









[GN:TOPA:TOPI]









[OR:Bacillus subtilis]









[EC:5.99.1.2]









[DE:(UNTWISTING ENZYME) (SWIVELASE)]









[SP:P39814]


SPX1877
1877
4538
120
360
208
4.20E-25
[LN:YBAN_ECOLI]
149









[AC:P45808:P77478]









[GN:YBAN]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 14.8 KD PROTEIN IN PRIC-APT INTERGENIC REGION]









[SP:P45808:P77478]


SPX1878
1878
4539
211
633
181
2.30E-34
[GI:4680703]
89









[LN:AF132966]









[AC:AF132966]









[PN:CGI-32 protein]









[OR:Homo sapiens]









[SR:human]


SPX1879
1879
4540
219
657
142
3.40E-22
[LN:YYAQ_BACSU]
137









[AC:P37507]









[GN:YYAQ]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 13.9 KD PROTEIN IN COTF-TETB INTERGENIC REGION]









[SP:P37507]


SPX1880
1880
4541
211
633
596
1.30E-93
[GI:2565151]
96









[LN:LLU92974]









[AC:U92974:M90760:M90761]









[PN:LeuA]









[GN:leuA]









[OR:Lactococcus lactis]


SPX1881
1881
4542
70
210


NO-HIT
6


SPX1882
1882
4543
145
435
308
6.00E-39
“[LN:LEU1_LACLA]
166









[AC:Q02141]









[GN:LEUA]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:4.1.3.12]









[DE:SYNTHASE) (ALPHA-IPM SYNTHETASE)]









[SP:Q02141]”


SPX1883
1883
4544
346
1038
608
4.50E-153
“[LN:LEU3_LACLA]
151









[AC:Q02143]









[GN:LEUB]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:1.1.1.85]









[DE:(IMDH) (3-IPM-DH)]









[SP:Q02143]”


SPX1884
1884
4545
90
270
129
8.30E-13
[LN:G69983]
87









[AC:G69983]









[PN:hypothetical protein ysdA]









[GN:ysdA]









[OR:Bacillus subtilis]


SPX1885
1885
4546
120
360
373
9.40E-47
“[LN:LEUD_LACLA]
183









[AC:Q02144]









[GN:LEUD]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:4.2.1.33]









[DE:(ISOPROPYLMALATE ISOMERASE) (ALPHA-IPM ISOMERASE)]









[SP:Q02144]”


SPX1886
1886
4547
79
237


NO-HIT
6


SPX1887
1887
4548
89
267


NO-HIT
6


SPX1888
1888
4549
645
1935
138
1.60E-33
“[LN:MCRB_ECOLI]
145









[AC:P15005]









[GN:MCRB:RGLB]









[OR:Escherichia coli]









[EC:3.1.21.-]









[DE:5-METHYLCYTOSINE-SPECIFIC RESTRICTION ENZYME B,]









[SP:P15005]”


SPX1889
1889
4550
448
1344
96
4.40E-09
[LN:D81431]
105









[AC:D81431]









[PN:hypothetical protein Cj0140 [imported]]









[GN:Cj0140]









[OR:Campylobacter jejuni]


SPX1890
1890
4551
329
987
913
1.40E-171
“[LN:C70015]
237









[AC:C70015]









[PN:probable GMP reductase, yumD:guanosine monophosphate reductase]









[GN:yumD]









[CL:GMP reductase:IMP dehydrogenase amino-terminal homology:IMP dehydrogenase catalytic homology]









[OR:Bacillus subtilis]









[EC:1.6.6.8]”


SPX1891
1891
4552
78
234


NO-HIT
6


SPX1892
1892
4553
67
201


NO-HIT
6


SPX1893
1893
4554
233
699
538
1.70E-69
“[LN:B69693]
188









[AC:B69693:JC4821]









[PN:ribonuclease III,:RNase D:RNase O]









[GN:rncS:srb]









[CL:ribonuclease III:double-stranded RNA-binding repeat homology]









[OR:Bacillus subtilis]









[EC:3.1.26.3]”


SPX1894
1894
4555
737
2211
1258
7.10E-169
[LN:G69708]
189









[AC:G69708:JC4819:PC4029]









[PN:chromosome segregation SMC protein:minichromosome stabilizing protein SMC]









[GN:smc]









[CL:conserved hypothetical P115 protein]









[OR:Bacillus subtilis]


SPX1895
1895
4556
217
651
139
2.70E-09
[GI:2246532]
148









[LN:U93872]









[AC:U93872]









[OR:Kaposi′s sarcoma-associated herpesvirus]









[SR:Kaposi′s sarcoma-associated herpesvirus - Human herpesvirus 8]


SPX1896
1896
4557
102
306
95
0.00014
[LN:P115_MYCHR]
83









[AC:P41508]









[OR:Mycoplasma hyorhinis]









[DE:P115 PROTEIN]









[SP:P41508]


SPX1897
1897
4558
196
588
428
2.90E-69
[LN:G69708]
189









[AC:G69708:JC4819:PC4029]









[PN:chromosome segregation SMC protein:minichromosome stabilizing protein SMC]









[GN:smc]









[CL:conserved hypothetical P115 protein]









[OR:Bacillus subtilis]


SPX1898
1898
4559
265
795
206
4.40E-31
“[GI:4062428]
178









[LN:D90722]









[AC:D90722:AB001340]









[PN:Hypothetical 30.2 kd protein in idh-deoR]









[OR:Escherichia coli]









[SR:Escherichia coli(strain:K12) DNA, clone:Kohara clone #209]”


SPX1899
1899
4560
273
819
220
3.10E-42
[LN:YIDA_ECOLI]
150









[AC:P09997:P76737]









[GN:YIDA]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 29.7 KD PROTEIN IN IBPA-GYRB INTERGENIC REGION]









[SP:P09997:P76737]


SPX1900
1900
4561
430
1290
675
1.30E-113
[GI:2633967]
184









[LN:BSUB0009]









[AC:Z99112:AL009126]









[PN:signal recognition particle (docking protein)]









[GN:ftsY]









[FN:involved in secretion of extracellular proteins]









[OR:Bacillus subtilis]


SPX1901
1901
4562
419
1257
2039
1.30E-284
[GI:2804700]
87









[LN:AF030361]









[AC:AF030361]









[PN:transposase]









[OR:Streptococcus pneumoniae]


SPX1902
1902
4563
85
255
350
2.40E-45
[GI:663279]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX1903
1903
4564
109
327
288
1.40E-35
[GI:2804700]
87









[LN:AF030361]









[AC:AF030361]









[PN:transposase]









[OR:Streptococcus pneumoniae]


SPX1904
1904
4565
173
519
858
5.70E-116
[GI:663278]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX1905
1905
4566
496
1488
779
6.50E-166
[LN:G6PD_BACSU]
110









[AC:P54547]









[GN:ZWF]









[OR:Bacillus subtilis]









[EC:1.1.1.49]









[DE:PROTEIN 11) (VEG11)]









[SP:P54547]


SPX1906
1906
4567
247
741
772
4.80E-102
[LN:H69334]
162









[AC:H69334]









[PN:glutamine transport protein glnQ]









[GN:glnQ]









[CL:inner membrane protein malK:ATP-binding cassette homology]









[OR:Archaeoglobus fulgidus]


SPX1907
1907
4568
493
1479
508
2.50E-80
[GI:6560693]
148









[LN:AF141644]









[AC:AF141644]









[PN:putative integral membrane protein]









[FN:putative inner membrane component of a]









[OR:Lactococcus lactis]


SPX1908
1908
4569
237
711
91
0.00087
“[LN:S76167]
116









[AC:S76167]









[PN:hypothetical protein]









[OR:Synechocystis sp.]









[SR:PCC 6803, , PCC 6803]









[SR:PCC 6803, ]”


SPX1909
1909
4570
90
270
80
4.20E-05
[LN:T34651]
102









[AC:T34651]









[PN:probable transmembrane protein]









[GN:SC1A9.02]









[OR:Streptomyces coelicolor]


SPX1910
1910
4571
663
1989
3350
0
[LN:UVRB_STRPN]
118









[AC:Q54986]









[GN:UVRB:UVS402]









[OR:Streptococcus pneumoniae]









[DE:EXCINUCLEASE ABC SUBUNIT B]









[SP:Q54986]


SPX1911
1911
4572
188
564
110
3.20E-15
[LN:G75474]
96









[AC:G75474]









[PN:probable acetyltransferase]









[GN:DR0796]









[OR:Deinococcus radiodurans]


SPX1912
1912
4573
130
390
65
1.50E-06
[LN:T39482]
169









[AC:T39482]









[PN:N-acetyltransferase]









[GN:SPBC15D4.06]









[CL:Escherichia coli ribosomal-protein-alanine N-acetyltransferase rimI]









[OR:Schizosaccharomyces pombe]


SPX1913
1913
4574
156
468
110
3.50E-09
[LN:G70031]
121









[AC:G70031]









[PN:mutator MutT protein homolog yvcI]









[GN:yvcI]









[CL:mutT domain homology]









[OR:Bacillus subtilis]


SPX1914
1914
4575
172
516
206
7.90E-37
“[LN:F72234]
116









[AC:F72234]









[PN:transcription regulator, biotin repressor family]









[GN:TM1602]









[OR:Thermotoga maritima]”


SPX1915
1915
4576
194
582


NO-HIT
6


SPX1916
1916
4577
167
501
81
4.70E-09
[GI:806536]
92









[LN:BAMALAMYA]









[AC:Z22520]









[PN:membrane protein]









[OR:Bacillus acidopullulyticus]


SPX1917
1917
4578
184
552
465
2.50E-59
[LN:DFP_STRMU]
138









[AC:Q54433]









[GN:DFP]









[OR:Streptococcus mutans]









[DE:DNA/PANTOTHENATE METABOLISM FLAVOPROTEIN HOMOLOG (FRAGMENT)]









[SP:Q54433]


SPX1918
1918
4579
253
759
120
2.90E-19
[LN:D69029]
230









[AC:D69029]









[PN:pantothenate metabolism flavoprotein dfp homolog MTH1216:probable aspartate 1-decarboxylase activase]









[GN:MTH1216]









[CL:pantothenate metabolism flavoprotein dfp]









[OR:Methanobacterium thermoautotrophicum]


SPX1919
1919
4580
181
543


NO-HIT
6


SPX1920
1920
4581
557
1671
2475
0
[LN:FTHS_STRMU]
132









[AC:Q59925:Q59926]









[GN:FHS]









[OR:Streptococcus mutans]









[EC:6.3.4.3]









[DE:SYNTHETASE) (FHS) (FTHFS)]









[SP:Q59925:Q59926]


SPX1921
1921
4582
80
240
145
9.20E-16
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX1922
1922
4583
392
1176
989
4.20E-132
[GI:6782414]
166









[LN:SPN271596]









[AC:AJ271596]









[PN:A/G specific adenine glycosylase]









[GN:mutY]









[FN:antimutator prevents C to A transversions]









[OR:Streptococcus pneumoniae]


SPX1923
1923
4584
235
705
1194
9.00E-161
[GI:5830523]
104









[LN:SPAJ6392]









[AC:AJ006392]









[PN:response regulator]









[GN:rr02]









[OR:Streptococcus pneumoniae]


SPX1924
1924
4585
452
1356
2249
0
[GI:5830524]
102









[LN:SPAJ6392]









[AC:AJ006392]









[PN:histidine kinase]









[GN:hk02]









[OR:Streptococcus pneumoniae]


SPX1925
1925
4586
270
810
1379
5.30E-185
[GI:6689278]
112









[LN:SPN012049]









[AC:AJ012049]









[PN:VicX protein]









[GN:vicX]









[FN:unknown]









[OR:Streptococcus pneumoniae]


SPX1926
1926
4587
81
243


NO-HIT
6


SPX1927
1927
4588
88
264
93
1.90E-06
[LN:D70886]
100









[AC:D70886]









[PN:hypothetical protein Rv2866]









[GN:Rv2866]









[OR:Mycobacterium tuberculosis]


SPX1928
1928
4589
258
774
162
3.00E-20
[LN:C72692]
98









[AC:C72692]









[PN:probable potassium channel APE0955]









[GN:APE0955]









[OR:Aeropyrum pernix]


SPX1929
1929
4590
170
510


NO-HIT
6


SPX1930
1930
4591
333
999
1652
9.40E-223
[GI:2275101]
146









[LN:SPR6LDH]









[AC:AJ000336]









[PN:L-lactate dehydrogenase]









[GN:ldh]









[FN:conversion of pyruvate to lactate]









[OR:Streptococcus pneumoniae]


SPX1931
1931
4592
316
948
1617
3.30E-219
“[LN:GYRA_STRPN]
150









[AC:P72524:Q54716:P72536]









[GN:GYRA]









[OR:Streptococcus pneumoniae]









[EC:5.99.1.3]









[DE:DNA GYRASE SUBUNIT A,]









[SP:P72524:Q54716:P72536]”


SPX1932
1932
4593
119
357
214
7.70E-24
“[LN:GYRA_STRPN]
150









[AC:P72524:Q54716:P72536]









[GN:GYRA]









[OR:Streptococcus pneumoniae]









[EC:5.99.1.3]









[DE:DNA GYRASE SUBUNIT A,]









[SP:P72524:Q54716:P72536]”


SPX1933
1933
4594
507
1521
2300
0
[GI:4138535]
105









[LN:SPN5815]









[AC:AJ005815]









[PN:DNA gyrase subunit A]









[GN:gyrA]









[OR:Streptococcus pneumoniae]


SPX1934
1934
4595
248
744
299
5.50E-36
[GI:488339]
153









[LN:SYNGIP3124]









[AC:M77279]









[PN:alpha-amylase]









[OR:unidentified cloning vector]









[SR:Cloning vector (sub_species Cloning vector pGIP3124) DNA]


SPX1935
1935
4596
266
798
184
6.20E-26
[GI:4433636]
132









[LN:AF029224]









[AC:AF029224:AF029225]









[PN:NirC]









[GN:nirC]









[FN:putative nitrite transporter]









[OR:Staphylococcus carnosus]


SPX1936
1936
4597
372
1116
426
6.30E-115
“[LN:T44655]
186









[AC:T44655]









[PN:O-acetylhomoserine (thiol)-lyase, [imported]









:O-acetylhomoserine sulfhydrylase]









[CL:O-succinylhomoserine (thiol)-lyase]









[OR:Leptospira meyeri]









[EC:4.2.99.10]”


SPX1937
1937
4598
425
1275
101
4.30E-18
[GI:6899348]
116









[LN:AE002133]









[AC:AE002133:AF222894]









[PN:conserved hypothetical]









[GN:UU367]









[OR:Ureaplasma urealyticum]


SPX1938
1938
4599
293
879
661
5.10E-86
[LN:TRUB_BACSU]
103









[AC:P32732]









[GN:TRUB]









[OR:Bacillus subtilis]









[EC:4.2.1.70]









[DE:HYDROLYASE)]









[SP:P32732]


SPX1939
1939
4600
101
303


NO-HIT
6


SPX1940
1940
4601
239
717
707
3.50E-93
[LN:G69728]
99









[AC:G69728]









[PN:uridine kinase udk]









[GN:udk]









[CL:uridine kinase]









[OR:Bacillus subtilis]


SPX1941
1941
4602
447
1341
633
1.60E-115
[LN:EX7L_BACSU]
110









[AC:P54521]









[GN:YQIB]









[OR:Bacillus subtilis]









[EC:3.1.11.6]









[DE:VII LARGE SUBUNIT)]









[SP:P54521]


SPX1942
1942
4603
71
213
113
3.50E-10
[LN:EX7S_ECOLI]
105









[AC:P22938]









[GN:XSEB]









[OR:Escherichia coli]









[EC:3.1.11.6]









[DE:SMALL SUBUNIT)]









[SP:P22938]


SPX1943
1943
4604
292
876
535
1.30E-78
“[LN:ISPA_MICLU]
140









[AC:O66126]









[GN:FPS]









[OR:Micrococcus luteus]









[SR:,Micrococcus lysodeikticus]









[EC:2.5.1.10]









[DE:(FPP SYNTHASE)]









[SP:O66126]”


SPX1944
1944
4605
246
738
353
1.20E-79
[LN:YQXC_BACSU]
142









[AC:P19672]









[GN:YQXC:YQIF]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 29.7 KD PROTEIN IN FOLD-AHRC INTERGENIC REGION]









[SP:P19672]


SPX1945
1945
4606
144
432
182
4.10E-26
[GI:4127534]
133









[LN:BSAJ10954]









[AC:AJ010954]









[PN:arginine repressor]









[GN:argR]









[FN:ADN binding protein]









[OR:Bacillus stearothermophilus]


SPX1946
1946
4607
298
894
317
4.20E-76
[LN:RECN_BACSU]
141









[AC:P17894:P19671]









[GN:RECN]









[OR:Bacillus subtilis]









[DE:DNA REPAIR PROTEIN RECN (RECOMBINATION PROTEIN N)]









[SP:P17894:P19671]


SPX1947
1947
4608
261
783
395
3.20E-68
[LN:RECN_BACSU]
141









[AC:P17894:P19671]









[GN:RECN]









[OR:Bacillus subtilis]









[DE:DNA REPAIR PROTEIN RECN (RECOMBINATION PROTEIN N)]









[SP:P17894:P19671]


SPX1948
1948
4609
243
729
97
4.90E-15
[GI:2352096]
69









[LN:U97022]









[AC:U97022]









[OR:Fervidobacterium islandicum]


SPX1949
1949
4610
345
1035
1284
9.40E-173
[LN:LEPA_BACSU]
102









[AC:P37949]









[GN:LEPA]









[OR:Bacillus subtilis]









[DE:GTP-BINDING PROTEIN LEPA]









[SP:P37949]


SPX1950
1950
4611
304
912
1158
1.80E-156
[LN:LEPA_BACSU]
102









[AC:P37949]









[GN:LEPA]









[OR:Bacillus subtilis]









[DE:GTP-BINDING PROTEIN LEPA]









[SP:P37949]


SPX1951
1951
4612
111
333
95
7.80E-05
“[LN:T04991]
110









[AC:T04991]









[PN:hypothetical protein T16L1.230]









[OR:Arabidopsis thaliana]









[SR:, mouse-ear cress]”


SPX1952
1952
4613
112
336
294
3.40E-35
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX1953
1953
4614
96
288


NO-HIT
6


SPX1954
1954
4615
230
690
70
3.10E-05
[LN:G75468]
90









[AC:G75468]









[PN:hypothetical protein]









[GN:DR0857]









[OR:Deinococcus radiodurans]


SPX1955
1955
4616
60
180


NO-HIT
6


SPX1956
1956
4617
82
246


NO-HIT
6


SPX1957
1957
4618
70
210


NO-HIT
6


SPX1958
1958
4619
68
204
138
3.20E-14
“[LN:LAFX_LACJO]
132









[AC:Q48509]









[GN:LAFX]









[OR:Lactobacillus johnsonii]









[DE:BACTERIOCIN LACTACIN F, SUBUNIT LAFX PRECURSOR]









[SP:Q48509]”


SPX1959
1959
4620
85
255
114
8.90E-21
[GI:5441255]
144









[LN:AB029612]









[AC:AB029612]









[PN:gassericin T1]









[GN:gatA]









[OR:Lactobacillus gasseri]









[SR:Lactobacillus gasseri (strain:SBT2055) DNA]


SPX1960
1960
4621
56
168
79
0.00078
[GI:6751696]
98









[LN:ATAC018908]









[AC:AC018908]









[GN:T7P1.21]









[OR:Arabidopsis thaliana]









[SR:thale cress]


SPX1961
1961
4622
182
546
379
2.90E-48
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX1962
1962
4623
133
399
364
8.90E-50
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX1963
1963
4624
55
165


NO-HIT
6


SPX1964
1964
4625
68
204


NO-HIT
6


SPX1965
1965
4626
69
207


NO-HIT
6


SPX1966
1966
4627
68
204
55
0.00018
[GI:6457574]
106









[LN:AF200347]









[AC:AF200347]









[PN:lactocin 705 beta-subunit precursor]









[OR:Lactobacillus casei]


SPX1967
1967
4628
73
219


NO-HIT
6


SPX1968
1968
4629
718
2154
2269
0
[LN:COMA_STRPN]
119









[AC:Q03727]









[GN:COMA]









[OR:Streptococcus pneumoniae]









[DE:TRANSPORT ATP-BINDING PROTEIN COMA]









[SP:Q03727]


SPX1969
1969
4630
83
249
80
0.00032
[LN:G72510]
92









[AC:G72510]









[PN:hypothetical protein APE2061]









[GN:APE2061]









[OR:Aeropyrum pernix]


SPX1970
1970
4631
454
1362
697
7.40E-90
[GI:1698422]
129









[LN:SGU40139]









[AC:U40139]









[PN:ComB]









[GN:comB]









[OR:Streptococcus gordonii]









[SR:Streptococcus gordonii strain=Challis]


SPX1971
1971
4632
67
201


NO-HIT
6


SPX1972
1972
4633
110
330


NO-HIT
6


SPX1973
1973
4634
447
1341
2062
1.10E-288
[GI:5830551]
102









[LN:SPAJ6401]









[AC:AJ006401]









[PN:histidine kinase]









[GN:hk13]









[OR:Streptococcus pneumoniae]


SPX1974
1974
4635
215
645
972
3.30E-133
[GI:5830550]
104









[LN:SPAJ6401]









[AC:AJ006401]









[PN:response regulator]









[GN:rr13]









[OR:Streptococcus pneumoniae]


SPX1975
1975
4636
61
183
239
4.40E-28
[GI:5830550]
104









[LN:SPAJ6401]









[AC:AJ006401]









[PN:response regulator]









[GN:rr13]









[OR:Streptococcus pneumoniae]


SPX1976
1976
4637
113
339
69
0.000063
[GI:1495671]
107









[LN:LPATOVGNS]









[AC:X94434]









[PN:response regulator PlnC]









[GN:plnC]









[OR:Lactobacillus plantarum]


SPX1977
1977
4638
110
330


NO-HIT
6


SPX1978
1978
4639
69
207


NO-HIT
6


SPX1979
1979
4640
324
972
150
4.10E-24
[LN:ECSB_BACSU]
95









[AC:P55340]









[GN:ECSB:PRST]









[OR:Bacillus subtilis]









[DE:PROTEIN ECSB]









[SP:P55340]


SPX1980
1980
4641
74
222


NO-HIT
6


SPX1981
1981
4642
115
345
333
4.00E-42
[LN:ECSA_BACSU]
128









[AC:P55339]









[GN:ECSA:PRST]









[OR:Bacillus subtilis]









[DE:ABC-TYPE TRANSPORTER ATP-BINDING PROTEIN ECSA]









[SP:P55339]


SPX1982
1982
4643
126
378
391
2.60E-49
[LN:ECSA_BACSU]
128









[AC:P55339]









[GN:ECSA:PRST]









[OR:Bacillus subtilis]









[DE:ABC-TYPE TRANSPORTER ATP-BINDING PROTEIN ECSA]









[SP:P55339]


SPX1983
1983
4644
137
411
334
8.80E-42
[LN:HIT_BACSU]
87









[AC:O07513]









[GN:HIT]









[OR:Bacillus subtilis]









[DE:HIT PROTEIN]









[SP:O07513]


SPX1984
1984
4645
96
288


NO-HIT
6


SPX1985
1985
4646
85
255


NO-HIT
6


SPX1986
1986
4647
379
1137
1885
4.90E-254
[LN:DNAJ_STRPN]
108









[AC:P95830]









[GN:DNAJ]









[OR:Streptococcus pneumoniae]









[DE:DNAJ PROTEIN (FRAGMENT)]









[SP:P95830]


SPX1987
1987
4648
47
141
125
7.20E-10
[GI:5305335]
104









[LN:AF071081]









[AC:AF071081]









[PN:proline-rich mucin homolog]









[OR:Mycobacterium tuberculosis]


SPX1988
1988
4649
119
357


NO-HIT
6


SPX1989
1989
4650
86
258


NO-HIT
6


SPX1990
1990
4651
608
1824
3008
0
[LN:DNAK_STRPN]
143









[AC:P95829:O66035]









[GN:DNAK]









[OR:Streptococcus pneumoniae]









[DE:DNAK PROTEIN (HEAT SHOCK PROTEIN 70) (HSP70)]









[SP:P95829:O66035]


SPX1991
1991
4652
120
360


NO-HIT
6


SPX1992
1992
4653
218
654


NO-HIT
6


SPX1993
1993
4654
183
549
346
3.60E-74
“[LN:GRPE_LACLA]
132









[AC:P42369]









[GN:GRPE]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[DE:GRPE PROTEIN]









[SP:P42369]”


SPX1994
1994
4655
356
1068
1712
6.90E-235
[GI:4566769]
125









[LN:AF117740]









[AC:AF117740]









[PN:heat shock transcription repressor HrcA]









[GN:hrcA]









[OR:Streptococcus pneumoniae]


SPX1995
1995
4656
170
510


NO-HIT
6


SPX1996
1996
4657
778
2334
570
9.20E-238
[LN:I41291]
104









[AC:I41291]









[PN:EcoA type I restriction-modification enzyme R subunit]









[OR:Escherichia coli]


SPX1997
1997
4658
488
1464
846
1.80E-144
[LN:I41293]
165









[AC:I41293]









[PN:EcoE type I restriction modification enzyme M subunit]









[CL:site-specific methyltransferase (adenine-specific) EcoK]









[OR:Escherichia coli]


SPX1998
1998
4659
517
1551
323
1.60E-37
[GI:6899439]
141









[LN:AE002141]









[AC:AE002141:AF222894]









[PN:type I restriction enzyme S protein (fragment)]









[GN:hsdS-5]









[OR:Ureaplasma urealyticum]


SPX1999
1999
4660
430
1290
328
1.40E-38
[GI:6899439]
141









[LN:AE002141]









[AC:AE002141:AF222894]









[PN:type I restriction enzyme S protein (fragment)]









[GN:hsdS-5]









[OR:Ureaplasma urealyticum]


SPX2000
2000
4661
74
222


NO-HIT
6


SPX2001
2001
4662
449
1347
1265
6.40E-246
[GI:1815634]
111









[LN:SAU61271]









[AC:U61271]









[PN:glutamine synthetase type 1]









[GN:glnA]









[OR:Streptococcus agalactiae]


SPX2002
2002
4663
119
357
244
7.30E-29
[LN:GLNR_BACCE]
99









[AC:P19083]









[GN:GLNR]









[OR:Bacillus cereus]









[DE:REGULATORY PROTEIN GLNR]









[SP:P19083]


SPX2003
2003
4664
176
528
100
1.00E-06
[LN:H69815]
87









[AC:H69815]









[PN:hypothetical protein ygaE]









[GN:ygaE]









[OR:Bacillus subtilis]


SPX2004
2004
4665
126
378
137
1.10E-11
[LN:S72776]
74









[AC:S72776]









[PN:B1496_F1_41 protein]









[OR:Mycobacterium leprae]


SPX2005
2005
4666
399
1197
622
6.20E-166
[GI:4490614]
106









[LN:SAU133520]









[AC:AJ133520]









[PN:phosphoglycerate kinase]









[GN:pgk]









[OR:Staphylococcus aureus]


SPX2006
2006
4667
1647
4941
207
3.10E-63
[GI:4204919]
109









[LN:APU59168]









[AC:U59168]









[PN:endo-beta-N-acetylglucosaminidase]









[OR:Arthrobacter protophormiae]


SPX2007
2007
4668
171
513


NO-HIT
6


SPX2008
2008
4669
544
1632
249
3.20E-57
“[LN:H71283]
165









[AC:H71283]









[PN:conserved hypothetical integral membrane protein TP0771]









[GN:TP0771]









[OR:Treponema pallidum subsp. pallidum]









[SR:, syphilis spirochete]”


SPX2009
2009
4670
536
1608
2303
0
[LN:LAJ10153]
97









[AC:AJ010153]









[PN:CTP synthetase]









[GN:pyrG]









[OR:Lactococcus lactis subsp. cremoris]


SPX2010
2010
4671
44
132
137
6.60E-15
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX2011
2011
4672
196
588
169
1.20E-25
“[LN:RPOE_BACSU]
135









[AC:P12464]









[GN:RPOE]









[OR:Bacillus subtilis]









[EC:2.7.7.6]









[DE:DNA-DIRECTED RNA POLYMERASE DELTA SUBUNIT,]









[SP:P12464]”


SPX2012
2012
4673
150
450


NO-HIT
6


SPX2013
2013
4674
130
390


NO-HIT
6


SPX2014
2014
4675
217
651
179
5.00E-19
[LN:S32217]
76









[AC:S32217]









[PN:hypothetical protein 2]









[OR:Bacillus megaterium]


SPX2015
2015
4676
188
564
258
3.20E-32
[LN:YPAA_BACSU]
136









[AC:P50726]









[GN:YPAA]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 20.5 KD PROTEIN IN SERA-FER INTERGENIC REGION]









[SP:P50726]


SPX2016
2016
4677
73
219


NO-HIT
6


SPX2017
2017
4678
156
468
243
6.60E-44
[GI:1381681]
117









[LN:BSU58864]









[AC:U58864]









[PN:CspR]









[GN:cspR]









[OR:Bacillus subtilis]









[SR:Bacillus subtilis strain=JH642]


SPX2018
2018
4679
277
831
83
4.70E-12
[LN:Y181_MYCPN]
119









[AC:Q50292]









[OR:Mycoplasma pneumoniae]









[DE:HYPOTHETICAL PROTEIN MG181 HOMOLOG (GT9_ORF434)]









[SP:Q50292]


SPX2019
2019
4680
416
1248
343
1.40E-50
[LN:G64435]
181









[AC:G64435]









[PN:cobalt transport ATP-binding protein O homolog]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Methanococcus jannaschii]


SPX2020
2020
4681
128
384
230
1.10E-25
[LN:G71192]
189









[AC:G71192]









[PN:probable cobalt transport ATP-binding protein]









[GN:PH1815]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Pyrococcus horikoshii]


SPX2021
2021
4682
71
213


NO-HIT
6


SPX2022
2022
4683
86
258


NO-HIT
6


SPX2023
2023
4684
183
549
494
1.60E-73
[GI:6165407]
91









[LN:LLA012388]









[AC:AJ012388]









[PN:hypothetical protein]









[OR:Lactococcus lactis]


SPX2024
2024
4685
292
876
546
2.00E-98
[LN:E64608]
91









[AC:E64608]









[PN:conserved hypothetical protein HP0709]









[OR:Helicobacter pylori]


SPX2025
2025
4686
450
1350
258
1.20E-60
[LN:F69354]
177









[AC:F69354]









[PN:TRK potassium uptake system protein (trkA-2) homolog]









[CL:Methanococcus jannaschii TRK system potassium uptake protein A]









[OR:Archaeoglobus fulgidus]


SPX2026
2026
4687
479
1437
232
7.20E-73
[LN:G69354]
142









[AC:G69354]









[PN:TRK potassium uptake system protein (trkH) homolog]









[CL:potassium uptake protein trkG]









[OR:Archaeoglobus fulgidus]


SPX2027
2027
4688
560
1680
777
1.20E-171
[LN:PTLB_STRMU]
118









[AC:P50976]









[GN:LACE]









[OR:Streptococcus mutans]









[EC:2.7.1.69]









[DE:(EC 2.7.1.69) (EII-LAC)]









[SP:P50976]


SPX2028
2028
4689
471
1413
643
5.80E-164
“[GI:153755]
122









[LN:STRPBGSL]









[AC:M19454]









[OR:Lactococcus lactis subsp. cremoris]









[SR:S.lactis (strain Z268) DNA, clone X25]”


SPX2029
2029
4690
65
195


NO-HIT
6


SPX2030
2030
4691
115
345
298
8.20E-37
[LN:PTLA_LACCA]
118









[AC:P11502]









[GN:LACF]









[OR:Lactobacillus casei]









[EC:2.7.1.69]









[DE:(EC 2.7.1.69) (EIII-LAC)]









[SP:P11502]


SPX2031
2031
4692
647
1941


NO-HIT
6


SPX2032
2032
4693
441
1323
395
1.00E-89
“[LN:PTCC_BACST]
157









[AC:Q45400]









[GN:CELB]









[OR:Bacillus stearothermophilus]









[DE:PERMEASE IIC COMPONENT) (PHOSPHOTRANSFERASE ENZYME II, C COMPONENT)]









[SP:Q45400]”


SPX2033
2033
4694
408
1224
147
2.50E-21
[LN:XYLR_BACSU]
94









[AC:P16557]









[GN:XYLR]









[OR:Bacillus subtilis]









[DE:XYLOSE REPRESSOR]









[SP:P16557]


SPX2034
2034
4695
73
219


NO-HIT
6


SPX2035
2035
4696
58
174


NO-HIT
6


SPX2036
2036
4697
62
186


NO-HIT
6


SPX2037
2037
4698
95
285
167
2.40E-18
[GI:2707293]
77









[LN:AF036720]









[AC:AF036720]









[PN:unknown]









[OR:Lactococcus lactis]


SPX2038
2038
4699
173
519
879
6.50E-119
[GI:663278]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX2039
2039
4700
256
768
1235
1.10E-172
[GI:663279]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX2040
2040
4701
421
1263
948
4.80E-188
[GI:2687821]
87









[LN:STIS1193]









[AC:Y13713]









[PN:transposase]









[OR:Streptococcus thermophilus]


SPX2041
2041
4702
86
258
149
1.10E-14
[GI:2198546]
78









[LN:SPCPS14E]









[AC:X85787]









[GN:tasA]









[OR:Streptococcus pneumoniae]


SPX2042
2042
4703
775
2325
3774
0
[GI:3168596]
145









[LN:AB014686]









[AC:AB014686]









[PN:pyruvate formate-lyase]









[GN:pfl]









[OR:Streptococcus bovis]









[SR:Streptococcus bovis (strain:JB-1) DNA]


SPX2043
2043
4704
92
276
133
7.70E-20
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX2044
2044
4705
78
234


NO-HIT
6


SPX2045
2045
4706
357
1071
491
2.70E-83
[GI:7380303]
126









[LN:NMA5Z2491]









[AC:AL162756:AL157959]









[PN:impB/mucB/samB family protein]









[GN:NMA1661]









[OR:Neisseria meningitidis]


SPX2046
2046
4707
63
189


NO-HIT
6


SPX2047
2047
4708
282
846
289
6.60E-52
[GI:5739401]
91









[LN:AF169967]









[AC:AF169967]









[PN:BacA]









[GN:bacA]









[OR:Flavobacterium johnsoniae]


SPX2048
2048
4709
217
651
139
3.00E-12
[LN:YIS1_STRCO]
140









[AC:P19780]









[GN:SC3C8.10]









[OR:Streptomyces coelicolor]









[DE:INSERTION ELEMENT IS110 HYPOTHETICAL 43.6 KD PROTEIN]









[SP:P19780]


SPX2049
2049
4710
62
186


NO-HIT
6


SPX2050
2050
4711
631
1893
95
3.20E-08
[LN:H64496]
86









[AC:H64496]









[PN:hypothetical protein MJ1577]









[OR:Methanococcus jannaschii]


SPX2051
2051
4712
522
1566
331
9.10E-53
“[LN:A72357]
146









[AC:A72357]









[PN:amino acid ABC transporter, permease protein]









[GN:TM0592]









[CL:histidine permease protein M]









[OR:Thermotoga maritima]”


SPX2052
2052
4713
247
741
388
9.60E-89
[LN:F81363]
138









[AC:F81363]









[PN:probable glutamine transport ATP-binding protein Cj0902 [imported]]









[GN:glnQ:Cj0902]









[OR:Campylobacter jejuni]


SPX2053
2053
4714
72
216


NO-HIT
6


SPX2054
2054
4715
77
231


NO-HIT
6


SPX2055
2055
4716
66
198
254
1.20E-29
[GI:2804700]
87









[LN:AF030361]









[AC:AF030361]









[PN:transposase]









[OR:Streptococcus pneumoniae]


SPX2056
2056
4717
128
384
511
2.70E-66
[GI:5739312]
126









[LN:AF161700]









[AC:AF161700]









[PN:ComX1]









[GN:comX1]









[FN:transcriptional regulator of]









[OR:Streptococcus pneumoniae]


SPX2057
2057
4718
184
552
442
1.30E-63
[LN:NUSG_BACSU]
120









[AC:Q06795]









[GN:NUSG]









[OR:Bacillus subtilis]









[DE:TRANSCRIPTION ANTITERMINATION PROTEIN NUSG]









[SP:Q06795]


SPX2058
2058
4719
59
177


NO-HIT
6


SPX2059
2059
4720
732
2196
3714
0
[GI:6165960]
116









[LN:AF101780]









[AC:AF101780]









[PN:penicillin-binding protein 2a]









[GN:pbp2a]









[OR:Streptococcus pneumoniae]


SPX2060
2060
4721
292
876
229
4.10E-34
[LN:YHCT_BACSU]
137









[AC:P54604]









[GN:YHCT]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 33.7 KD PROTEIN IN CSPB-GLPP INTERGENIC REGION]









[SP:P54604]


SPX2061
2061
4722
360
1080
1061
2.30E-215
“[LN:A42963]
186









[AC:A42963:B42963:JH0750]









[PN:glyceraldehyde-3-phosphate dehydrogenase,:plasmin receptor]









[CL:glyceraldehyde-3-phosphate dehydrogenase]









[OR:Streptococcus sp.]









[EC:1.2.1.12]”


SPX2062
2062
4723
92
276


NO-HIT
6


SPX2063
2063
4724
317
951
124
1.80E-15
[LN:Y797_METJA]
114









[AC:Q58207]









[GN:MJ0797]









[OR:Methanococcus jannaschii]









[DE:HYPOTHETICAL PROTEIN MJ0797]









[SP:Q58207]


SPX2064
2064
4725
113
339
552
2.20E-73
[GI:5019553]
97









[LN:SPN239004]









[AC:AJ239004]









[PN:putative transposase]









[OR:Streptococcus pneumoniae]


SPX2065
2065
4726
87
261


NO-HIT
6


SPX2066
2066
4727
116
348
577
5.80E-76
[GI:4200438]
96









[LN:AF026471]









[AC:AF026471]









[PN:putative transposase]









[OR:Streptococcus pneumoniae]


SPX2067
2067
4728
300
900
482
2.20E-71
[LN:B70375]
160









[AC:B70375]









[PN:quinolinate phosphoribosyl transferase]









[GN:nadC]









[CL:nicotinate-nucleotide pyrophosphorylase (carboxylating)]









[OR:Aquifex aeolicus]


SPX2068
2068
4729
437
1311
448
2.70E-105
[LN:C81402]
119









[AC:C81402]









[PN:probable integral membrane protein Cj0555 [imported]]









[GN:Cj0555]









[OR:Campylobacter jejuni]


SPX2069
2069
4730
62
186


NO-HIT
6


SPX2070
2070
4731
65
195
111
7.10E-09
“[LN:H81018]
137









[AC:H81018]









[PN:iron(III) ABC transporter, ATP-binding protein NMB1993 [imported]]









[GN:NMB1993]









[OR:Neisseria meningitidis]”


SPX2071
2071
4732
243
729
352
3.20E-72
“[GI:4512387]
143









[LN:AB011838]









[AC:AB011838]









[GN:ydhQ]









[OR:Bacillus halodurans]









[SR:Bacillus halodurans (strain:C-125) DNA, clone_lib:lambda no.]”


SPX2072
2072
4733
470
1410
808
8.30E-181
[LN:D69785]
127









[AC:D69785]









[PN:beta-glucosidase homolog ydhP]









[GN:ydhP]









[CL:Agrobacterium beta-glucosidase]









[OR:Bacillus subtilis]


SPX2073
2073
4734
432
1296
330
7.00E-64
“[LN:PTCC_BACSU]
152









[AC:P46317]









[GN:CELB:LICC]









[OR:Bacillus subtilis]









[DE:PERMEASE IIC COMPONENT) (PHOSPHOTRANSFERASE ENZYME II, C COMPONENT)]









[SP:P46317]”


SPX2074
2074
4735
129
387


NO-HIT
6


SPX2075
2075
4736
103
309
191
2.70E-30
[LN:PTCB_BACST]
115









[AC:Q45399]









[GN:CELA]









[OR:Bacillus stearothermophilus]









[EC:2.7.1.69]









[DE:(EC 2.7.1.69)]









[SP:Q45399]


SPX2076
2076
4737
103
309
210
6.00E-24
[LN:PTCA_BACSU]
121









[AC:P46319]









[GN:CELC:LICA]









[OR:Bacillus subtilis]









[EC:2.7.1.69]









[DE:(EC 2.7.1.69) (EIII-CEL)]









[SP:P46319]


SPX2077
2077
4738
75
225


NO-HIT
6


SPX2078
2078
4739
891
2673
2272
0
“[LN:ADH2_ENTHI]
176









[AC:Q24803:Q27649]









[GN:ADH2]









[OR:Entamoeba histolytica]









[EC:1.1.1.1:1.2.1.10]









[DE:(EC 1.1.1.1) (ADH); ALCETALDEHYDE DEHYDROGENASE, (ACDH)]]









[SP:Q24803:Q27649]”


SPX2079
2079
4740
137
411
168
4.10E-18
[GI:6010051]
113









[LN:ECA270205]









[AC:AJ270205]









[PN:putative phosphatidylinositol-4-phosphate]









[OR:Entodinium caudatum]


SPX2080
2080
4741
143
429
91
7.10E-26
“““[LN:E69808]
161









[AC:E69808]









[PN:protein-tyrosine phosphatase homolog yfkJ]









[GN:yfkJ]









[CL:protein-tyrosine-phosphatase, low molecular weight]









[OR:Bacillus subtilis]”


SPX2081
2081
4742
100
300
177
9.30E-20
[GI:1402532]
130









[LN:D78257]









[AC:D78257]









[PN:ORF11]









[GN:orf11]









[OR:Enterococcus faecalis]









[SR:Enterococcus faecalis plasmid:pYI17 DNA]


SPX2082
2082
4743
659
1977
1671
0
“[LN:TKT_STRPN]
127









[AC:P22976]









[GN:RECP]









[OR:Streptococcus pneumoniae]









[EC:2.2.1.1]









[DE:PROBABLE TRANSKETOLASE, (TK)]









[SP:P22976]”


SPX2083
2083
4744
81
243
171
1.00E-17
“[LN:TKT_STRPN]
127









[AC:P22976]









[GN:RECP]









[OR:Streptococcus pneumoniae]









[EC:2.2.1.1]









[DE:PROBABLE TRANSKETOLASE, (TK)]









[SP:P22976]”


SPX2084
2084
4745
102
306
277
1.50E-33
“[LN:TKT_STRPN]
127









[AC:P22976]









[GN:RECP]









[OR:Streptococcus pneumoniae]









[EC:2.2.1.1]









[DE:PROBABLE TRANSKETOLASE, (TK)]









[SP:P22976]”


SPX2085
2085
4746
245
735
546
8.30E-96
[LN:YJFR_ECOLI]
136









[AC:P39300]









[GN:YJFR]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 40.1 KD PROTEIN IN AIDB-SGAT INTERGENIC REGION]









[SP:P39300]


SPX2086
2086
4747
136
408
430
3.30E-54
[LN:YJFR_ECOLI]
136









[AC:P39300]









[GN:YJFR]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 40.1 KD PROTEIN IN AIDB-SGAT INTERGENIC REGION]









[SP:P39300]


SPX2087
2087
4748
558
1674
178
6.30E-20
“[GI:4512373]
144









[LN:AB011837]









[AC:AB011837]









[GN:yjdC]









[OR:Bacillus halodurans]









[SR:Bacillus halodurans (strain:C-125) DNA, clone_lib:lambda no.9]”


SPX2088
2088
4749
235
705
489
3.20E-93
[GI:5616307]
123









[LN:AF160811]









[AC:AF160811]









[PN:L-ribulose 5-phosphate 4-epimerase]









[GN:araD]









[OR:Bacillus stearothermophilus]


SPX2089
2089
4750
288
864
777
3.20E-106
“[LN:SGBU_HAEIN]
153









[AC:P44990]









[GN:SGBU:HI1026]









[OR:Haemophilus influenzae]









[EC:5.-.-.-]









[DE:PUTATIVE HEXULOSE-6-PHOSPHATE ISOMERASE, (HUMPI)]









[SP:P44990]”


SPX2090
2090
4751
222
666
349
1.00E-70
[LN:SGAH_ECOLI]
132









[AC:P39304]









[GN:SGAH]









[OR:Escherichia coli]









[EC:4.1.2.-]









[DE:3-HEXULOSE 6-PHOSPHATE FORMALDEHYDE LYASE)]









[SP:P39304]


SPX2091
2091
4752
162
486
266
1.10E-45
[LN:PTXA_ECOLI]
104









[AC:P39303]









[GN:SGAA]









[OR:Escherichia coli]









[EC:2.7.1.69]









[DE:(EC 2.7.1.69)]









[SP:P39303]


SPX2092
2092
4753
94
282
111
6.80E-22
[LN:PTXB_ECOLI]
104









[AC:P39302]









[GN:SGAB]









[OR:Escherichia coli]









[EC:2.7.1.69]









[DE:(EC 2.7.1.69)]









[SP:P39302]


SPX2093
2093
4754
509
1527
275
5.90E-99
[LN:SGAT_ECOLI]
108









[AC:P39301]









[GN:SGAT]









[OR:Escherichia coli]









[DE:PUTATIVE TRANSPORT PROTEIN SGAT]









[SP:P39301]


SPX2094
2094
4755
208
624
210
1.10E-38
“[GI:6681651]
183









[LN:AB016077]









[AC:AB016077]









[PN:sakacin A production response regulator]









[GN:sapR]









[OR:Streptococcus mutans]









[SR:Streptococcus mutans (strain:MT8148) DNA, clone:pYT570]”


SPX2095
2095
4756
329
987
145
1.90E-24
[LN:JAG_BACSU]
116









[AC:Q01620]









[GN:JAG]









[OR:Bacillus subtilis]









[DE:JAG PROTEIN (SPOIIIJ ASSOCIATED PROTEIN)]









[SP:Q01620]


SPX2096
2096
4757
277
831
357
1.00E-51
[LN:SP3J_BACSU]
122









[AC:Q01625]









[GN:SPOIIIJ]









[OR:Bacillus subtilis]









[DE:STAGE III SPORULATION PROTEIN J PRECURSOR]









[SP:Q01625]


SPX2097
2097
4758
124
372
173
3.10E-31
“[GI:5672645]
137









[LN:AB013492]









[AC:AB013492]









[GN:rnpA]









[OR:Bacillus halodurans]









[SR:Bacillus halodurans (strain:C-125) DNA, clone:ALBAC001]”


SPX2098
2098
4759
397
1191
822
1.30E-149
“[LN:ACKA_BACSU]
122









[AC:P37877]









[GN:ACKA]









[OR:Bacillus subtilis]









[EC:2.7.2.1]









[DE:ACETATE KINASE, (ACETOKINASE)]









[SP:P37877]”


SPX2099
2099
4760
318
954
297
4.70E-44
[LN:YTXK_BACSU]
137









[AC:P37876]









[GN:YTXK]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 37.4 KD PROTEIN IN ACKA-SSPA INTERGENIC REGION]









[SP:P37876]


SPX2100
2100
4761
196
588
132
2.90E-10
[LN:H70323]
90









[AC:H70323]









[PN:hypothetical protein aq_262]









[GN:aq_262]









[OR:Aquifex aeolicus]


SPX2101
2101
4762
138
414


NO-HIT
6


SPX2102
2102
4763
169
507
157
1.60E-30
[GI:3287181]
89









[LN:LLC3107]









[AC:Y15043]









[GN:orf150]









[OR:Lactococcus lactis subsp. cremoris]


SPX2103
2103
4764
101
303
123
9.50E-12
[GI:3287182]
115









[LN:LLC3107]









[AC:Y15043]









[PN:hypothetical protein]









[GN:orf128]









[OR:Lactococcus lactis subsp. cremoris]


SPX2104
2104
4765
135
405
626
3.00E-81
[GI:3211751]
104









[LN:AF052207]









[AC:AF052207]









[PN:competence protein]









[GN:cglD]









[OR:Streptococcus pneumoniae]


SPX2105
2105
4766
109
327
512
5.80E-66
[GI:3211750]
104









[LN:AF052207]









[AC:AF052207]









[PN:competence protein]









[GN:cglC]









[OR:Streptococcus pneumoniae]


SPX2106
2106
4767
348
1044
1440
3.30E-199
[GI:3211749]
104









[LN:AF052207]









[AC:AF052207]









[PN:competence protein]









[GN:cglB]









[OR:Streptococcus pneumoniae]


SPX2107
2107
4768
314
942
1592
4.30E-217
[GI:3211748]
104









[LN:AF052207]









[AC:AF052207]









[PN:competence protein]









[GN:cglA]









[OR:Streptococcus pneumoniae]


SPX2108
2108
4769
124
372
468
9.20E-61
[GI:2058543]
100









[LN:SGU81957]









[AC:U81957]









[PN:putative DNA binding protein]









[OR:Streptococcus gordonii]


SPX2109
2109
4770
353
1059
639
1.60E-125
[LN:T36961]
179









[AC:T36961]









[PN:probable zinc-containing dehydrogenase]









[GN:SCJ1.28c]









[CL:alcohol dehydrogenase:long-chain alcohol dehydrogenase homology]









[OR:Streptomyces coelicolor]


SPX2110
2110
4771
142
426


NO-HIT
6


SPX2111
2111
4772
384
1152
819
3.90E-108
[GI:6683552]
118









[LN:AB024532]









[AC:AB024532]









[GN:SA8A11-1]









[OR:Enterococcus seriolicida]









[SR:Enterococcus seriolicida DNA]


SPX2112
2112
4773
606
1818
173
2.40E-27
[LN:C69975]
90









[AC:C69975]









[PN:acyltransferase homolog yrhL]









[GN:yrhL]









[OR:Bacillus subtilis]


SPX2113
2113
4774
381
1143
1469
3.70E-200
[LN:TGT_BACSU]
134









[AC:O32053]









[GN:TGT]









[OR:Bacillus subtilis]









[EC:2.4.2.29]









[DE:TRANSGLYCOSYLASE) (GUANINE INSERTION ENZYME)]









[SP:O32053]


SPX2114
2114
4775
286
858
90
9.00E-05
[LN:S32215]
76









[AC:S32215]









[PN:hypothetical protein 1]









[OR:Bacillus megaterium]


SPX2115
2115
4776
215
645
769
1.20E-104
[LN:PCP_STRPY]
149









[AC:Q01328]









[GN:PCP]









[OR:Streptococcus pyogenes]









[EC:3.4.19.3]









[DE:PEPTIDASE) (PYROGLUTAMYL-PEPTIDASE I) (PGP-I) (PYRASE)]









[SP:Q01328]


SPX2116
2116
4777
90
270


NO-HIT
6


SPX2117
2117
4778
120
360
221
1.90E-43
“[LN:YTRP_LACLA]
155









[AC:Q02009]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[DE:HYPOTHETICAL 13.3 KD PROTEIN IN TRPE 5′REGION]









[SP:Q02009]”


SPX2118
2118
4779
142
426
163
3.50E-17
[LN:D69783]
139









[AC:D69783]









[PN:transcription regulator MarR family homolog ydgJ]









[GN:ydgJ]









[CL:regulatory protein mprA]









[OR:Bacillus subtilis]


SPX2119
2119
4780
69
207
107
2.10E-10
[GI:1914870]
81









[LN:SPZ82001]









[AC:Z82001]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX2120
2120
4781
371
1113
382
8.00E-79
[GI:517204]
65









[LN:SPU09352]









[AC:U09352]









[OR:Streptococcus pyogenes]


SPX2121
2121
4782
207
621
153
7.60E-14
[LN:A57362]
81









[AC:A57362]









[PN:gyrb protein]









[GN:gyrb]









[OR:Streptococcus pneumoniae]


SPX2122
2122
4783
427
1281
216
1.10E-45
[LN:H72331]
139









[AC:H72331]









[PN:conserved hypothetical protein]









[GN:TM0815]









[CL:conserved hypothetical protein HI1612]









[OR:Thermotoga maritima]


SPX2123
2123
4784
495
1485
412
4.80E-66
[LN:B64532]
96









[AC:B64532]









[PN:threonine synthase]









[CL:threonine synthase]









[OR:Helicobacter pylori]


SPX2124
2124
4785
426
1278
70
0.00014
“[LN:T05142]
158









[AC:T05142:S60128:S45018]









[PN:gamma-glutamylcysteine synthetase:protein F7H19.290]









[OR:Arabidopsis thaliana]









[SR:, mouse-ear cress]









[EC:6.3.2.2]”


SPX2125
2125
4786
59
177
100
1.30E-08
[LN:C64671]
81









[AC:C64671]









[PN:hypothetical protein HP1211]









[OR:Helicobacter pylori]


SPX2126
2126
4787
61
183
81
9.30E-05
[LN:E72688]
143









[AC:E72688]









[PN:hypothetical protein APE0925]









[GN:APE0925]









[CL:Aeropyrum pernix hypothetical protein APE0925]









[OR:Aeropyrum pernix]


SPX2127
2127
4788
78
234
143
4.90E-15
[LN:F71245]
95









[AC:F71245]









[PN:hypothetical protein PHS004]









[GN:PHS004]









[OR:Pyrococcus horikoshii]


SPX2128
2128
4789
82
246
247
1.10E-29
[LN:F81737]
131









[AC:F81737]









[PN:hypothetical protein TC0129 [imported]]









[GN:TC0129]









[OR:Chlamydia muridarum:Chlamydia trachomatis MoPn]


SPX2129
2129
4790
52
156
80
3.00E-05
[LN:D75542]
90









[AC:D75542]









[PN:hypothetical protein]









[GN:DR0254]









[OR:Deinococcus radiodurans]


SPX2130
2130
4791
105
315


NO-HIT
6


SPX2131
2131
4792
146
438
486
1.80E-62
[GI:517210]
65









[LN:SPU11799]









[AC:U11799]









[OR:Streptococcus pyogenes]


SPX2132
2132
4793
354
1062
824
6.40E-132
[GI:1915907]
95









[LN:LLPEPPGEN]









[AC:Y08842]









[PN:aminopeptidase P]









[GN:pepP]









[OR:Lactococcus lactis]


SPX2133
2133
4794
944
2832
2029
0
[LN:UVRA_BACSU]
104









[AC:O34863]









[GN:UVRA]









[OR:Bacillus subtilis]









[DE:EXCINUCLEASE ABC SUBUNIT A]









[SP:O34863]


SPX2134
2134
4795
315
945
236
1.50E-26
[LN:A75272]
140









[AC:A75272]









[PN:probable transport protein]









[GN:DR2463]









[CL:magnesium and cobalt transport protein]









[OR:Deinococcus radiodurans]


SPX2135
2135
4796
68
204


NO-HIT
6


SPX2136
2136
4797
213
639


NO-HIT
6


SPX2137
2137
4798
51
153
123
1.60E-12
[GI:1914870]
81









[LN:SPZ82001]









[AC:Z82001]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX2138
2138
4799
344
1032
86
1.10E-19
[LN:E75325]
91









[AC:E75325]









[PN:probable mccF protein]









[GN:DR2000]









[OR:Deinococcus radiodurans]


SPX2139
2139
4800
226
678
66
3.80E-08
[GI:6470197]
77









[LN:AF188935]









[AC:AF188935]









[PN:pXO2-46]









[OR:Bacillus anthracis]


SPX2140
2140
4801
188
564
465
3.30E-63
[LN:3MGA_HAEIN]
121









[AC:P44321]









[GN:TAG:HI0654]









[OR:Haemophilus influenzae]









[EC:3.2.2.20]









[DE:GLYCOSIDASE) (TAG)]









[SP:P44321]


SPX2141
2141
4802
186
558


NO-HIT
6


SPX2142
2142
4803
198
594
235
1.00E-38
[LN:RUVA_BACSU]
122









[AC:O05392]









[GN:RUVA]









[OR:Bacillus subtilis]









[DE:PROBABLE HOLLIDAY JUNCTION DNA HELICASE RUVA]









[SP:O05392]


SPX2143
2143
4804
70
210


NO-HIT
6


SPX2144
2144
4805
367
1101
888
6.00E-128
“[LN:RIBD_ACTPL]
177









[AC:P50853]









[GN:RIBD:RIBG]









[OR:Actinobacillus pleuropneumoniae]









[SR:,Haemophilus pleuropneumoniae]









[EC:3.5.4.-]









[DE:RIBOFLAVIN-SPECIFIC DEAMINASE,]









[SP:P50853]”


SPX2145
2145
4806
212
636
601
1.70E-81
“[LN:RISA_ACTPL]
179









[AC:P50854]









[GN:RIBE:RIBB]









[OR:Actinobacillus pleuropneumoniae]









[SR:,Haemophilus pleuropneumoniae]









[EC:2.5.1.9]









[DE:RIBOFLAVIN SYNTHASE ALPHA CHAIN,]









[SP:P50854]”


SPX2146
2146
4807
412
1236
1266
1.80E-170
“[LN:GCH2_ACTPL]
153









[AC:P50855]









[GN:RIBA]









[OR:Actinobacillus pleuropneumoniae]









[SR:,Haemophilus pleuropneumoniae]









[EC:3.5.4.25]









[DE:SYNTHASE)]]









[SP:P50855]”


SPX2147
2147
4808
156
468
546
1.30E-70
“[LN:RISB_ACTPL]
194









[AC:P50856]









[GN:RIBH]









[OR:Actinobacillus pleuropneumoniae]









[SR:,Haemophilus pleuropneumoniae]









[EC:2.5.1.9]









[DE:(LUMAZINE SYNTHASE) (RIBOFLAVIN SYNTHASE BETA CHAIN)]









[SP:P50856]”


SPX2148
2148
4809
650
1950
3286
0
[LN:HEXB_STRPN]
117









[AC:P14160]









[GN:HEXB]









[OR:Streptococcus pneumoniae]









[DE:DNA MISMATCH REPAIR PROTEIN HEXB]









[SP:P14160]


SPX2149
2149
4810
84
252


NO-HIT
6


SPX2150
2150
4811
97
291


NO-HIT
6


SPX2151
2151
4812
61
183
122
1.10E-12
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX2152
2152
4813
174
522
231
9.30E-27
“[GI:1196936]
144









[LN:STRHEXB]









[AC:M29686]









[PN:unknown protein]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (clone: pSP(8,41).) DNA]”


SPX2153
2153
4814
153
459


NO-HIT
6


SPX2154
2154
4815
126
378
333
1.60E-40
[GI:517210]
65









[LN:SPU11799]









[AC:U11799]









[OR:Streptococcus pyogenes]


SPX2155
2155
4816
211
633
762
7.90E-101
[GI:517210]
65









[LN:SPU11799]









[AC:U11799]









[OR:Streptococcus pyogenes]


SPX2156
2156
4817
201
603
499
7.70E-65
[LN:C81084]
109









[AC:C81084]









[PN:hypothetical protein NMB1426 [imported]]









[GN:NMB1426]









[OR:Neisseria meningitidis]


SPX2157
2157
4818
64
192


NO-HIT
6


SPX2158
2158
4819
218
654
461
2.50E-67
[LN:C81084]
109









[AC:C81084]









[PN:hypothetical protein NMB1426 [imported]]









[GN:NMB1426]









[OR:Neisseria meningitidis]


SPX2159
2159
4820
201
603
353
3.50E-53
[GI:6782392]
125









[LN:SDY18363]









[AC:Y18363]









[PN:ribonucleotide reductase-like (Nrd-like)]









[GN:nrd]









[OR:Streptococcus dysgalactiae]


SPX2160
2160
4821
194
582


NO-HIT
6


SPX2161
2161
4822
429
1287
2176
6.20E-298
[GI:5830536]
104









[LN:SPAJ6396]









[AC:AJ006396]









[PN:response regulator]









[GN:rr07]









[OR:Streptococcus pneumoniae]


SPX2162
2162
4823
568
1704
1183
7.00E-160
[GI:5830535]
102









[LN:SPAJ6396]









[AC:AJ006396]









[PN:histidine kinase]









[GN:hk07]









[OR:Streptococcus pneumoniae]


SPX2163
2163
4824
205
615


NO-HIT
6


SPX2164
2164
4825
190
570


NO-HIT
6


SPX2165
2165
4826
231
693
395
1.90E-87
[GI:6165406]
91









[LN:LLA012388]









[AC:AJ012388]









[PN:hypothetical protein]









[OR:Lactococcus lactis]


SPX2166
2166
4827
354
1062
616
4.50E-130
[GI:6165405]
91









[LN:LLA012388]









[AC:AJ012388]









[PN:hypothetical protein]









[OR:Lactococcus lactis]


SPX2167
2167
4828
73
219
94
8.50E-07
[LN:G72536]
92









[AC:G72536]









[PN:hypothetical protein APE1580]









[GN:APE1580]









[OR:Aeropyrum pernix]


SPX2168
2168
4829
458
1374
219
7.10E-53
[LN:E75327]
99









[AC:E75327]









[PN:ArgE/DapE/Acy1 family protein]









[GN:DR2017]









[OR:Deinococcus radiodurans]


SPX2169
2169
4830
285
855
319
1.50E-63
[GI:6165404]
91









[LN:LLA012388]









[AC:AJ012388]









[PN:hypothetical protein]









[OR:Lactococcus lactis]


SPX2170
2170
4831
66
198


NO-HIT
6


SPX2171
2171
4832
184
552
109
1.10E-12
[LN:YXEM_BACSU]
110









[AC:P54952]









[GN:YXEM:LP9E]









[OR:Bacillus subtilis]









[DE:INTERGENIC REGION PRECURSOR]









[SP:P54952]


SPX2172
2172
4833
62
186


NO-HIT
6


SPX2173
2173
4834
225
675
129
5.60E-10
[LN:G75494]
121









[AC:G75494]









[PN:AzlC family protein]









[GN:DR0633]









[CL:hypothetical protein b2682]









[OR:Deinococcus radiodurans]


SPX2174
2174
4835
137
411
328
2.80E-41
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX2175
2175
4836
80
240


NO-HIT
6


SPX2176
2176
4837
75
225


NO-HIT
6


SPX2177
2177
4838
410
1230
80
2.70E-10
[GI:3582221]
114









[LN:AE001272]









[AC:AE001272]









[PN:conserved hypothetical protein]









[GN:ORF00049]









[OR:Lactococcus lactis]


SPX2178
2178
4839
222
666
71
1.80E-05
[LN:E69787]
87









[AC:E69787]









[PN:hypothetical protein ydiL]









[GN:ydiL]









[OR:Bacillus subtilis]


SPX2179
2179
4840
66
198


NO-HIT
6


SPX2180
2180
4841
296
888
587
4.20E-77
[GI:4102023]
134









[LN:AF007761]









[AC:AF007761]









[PN:MutR]









[GN:mutR]









[FN:positive transcriptional regulator of mutA]









[OR:Streptococcus mutans]


SPX2181
2181
4842
69
207


NO-HIT
6


SPX2182
2182
4843
206
618
479
1.40E-72
[LN:UDG5_ECOLI]
111









[AC:Q47329]









[GN:KFID]









[OR:Escherichia coli]









[EC:1.1.1.22]









[DE:(UDP-GLCDH) (UDPGDH)]









[SP:Q47329]


SPX2183
2183
4844
252
756
86
3.90E-08
[GI:4689219]
92









[LN:AF115779]









[AC:AF115779]









[PN:unknown]









[GN:mitC]









[OR:Streptomyces lavendulae]


SPX2184
2184
4845
74
222


NO-HIT
6


SPX2185
2185
4846
115
345


NO-HIT
6


SPX2186
2186
4847
81
243


NO-HIT
6


SPX2187
2187
4848
539
1617
294
1.70E-34
“[LN:D72267]
180









[AC:D72267]









[PN:ABC transporter, ATP-binding protein]









[GN:TM1328]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Thermotoga maritima]”


SPX2188
2188
4849
318
954
137
5.90E-20
[LN:B75096]
144









[AC:B75096]









[PN:glycosyl transferase PAB0772]









[GN:PAB0772]









[CL:Neisseria meningitidis glycosyl transferase A]









[OR:Pyrococcus abyssi]


SPX2189
2189
4850
175
525
179
6.60E-17
[GI:1276880]
90









[LN:STU40830]









[AC:U40830]









[PN:EpsG]









[GN:epsG]









[OR:Streptococcus thermophilus]


SPX2190
2190
4851
188
564


NO-HIT
6


SPX2191
2191
4852
107
321
187
3.70E-21
[GI:4200438]
96









[LN:AF026471]









[AC:AF026471]









[PN:putative transposase]









[OR:Streptococcus pneumoniae]


SPX2192
2192
4853
88
264
196
2.60E-23
[GI:5019553]
97









[LN:SPN239004]









[AC:AJ239004]









[PN:putative transposase]









[OR:Streptococcus pneumoniae]


SPX2193
2193
4854
355
1065
893
8.00E-121
[GI:2804700]
87









[LN:AF030361]









[AC:AF030361]









[PN:transposase]









[OR:Streptococcus pneumoniae]


SPX2194
2194
4855
129
387
490
2.90E-65
[GI:663279]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX2195
2195
4856
71
213
119
2.60E-10
[GI:2198546]
78









[LN:SPCPS14E]









[AC:X85787]









[GN:tasA]









[OR:Streptococcus pneumoniae]


SPX2196
2196
4857
337
1011
913
6.50E-132
[LN:YDIE_BACSU]
138









[AC:O05518]









[GN:YDIE]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 36.8 KD PROTEIN IN PHOB-GROES INTERGENIC REGION]









[SP:O05518]


SPX2197
2197
4858
146
438
92
1.00E-09
[LN:E69786]
190









[AC:E69786]









[PN:ribosomal-protein-alanine N-acetyltransfer homolog ydiD]









[GN:ydiD]









[CL:Escherichia coli ribosomal-protein-alanine N-acetyltransferase rimI]









[OR:Bacillus subtilis]


SPX2198
2198
4859
228
684
303
1.40E-53
[GI:3341437]
101









[LN:EFY17797]









[AC:Y17797]









[PN:hypothetical protein]









[GN:ydiC]









[OR:Enterococcus faecalis]


SPX2199
2199
4860
62
186


NO-HIT
6


SPX2200
2200
4861
77
231


NO-HIT
6


SPX2201
2201
4862
78
234
78
2.50E-10
[LN:D69871]
87









[AC:D69871]









[PN:hypothetical protein ykzG]









[GN:ykzG]









[OR:Bacillus subtilis]


SPX2202
2202
4863
560
1680
1841
6.00E-251
[LN:YKQC_BACSU]
137









[AC:Q45493]









[GN:YKQC]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 61.5 KD PROTEIN IN ADEC-PDHA INTERGENIC REGION]









[SP:Q45493]


SPX2203
2203
4864
121
363


NO-HIT
6


SPX2204
2204
4865
638
1914
1698
2.50E-282
“[LN:GIDA_LACLC]
171









[AC:O32806]









[GN:GIDA]









[OR:Lactococcus lactis]









[SR:,subspcremoris:Streptococcus cremoris]









[DE:GLUCOSE INHIBITED DIVISION PROTEIN A (FRAGMENT)]









[SP:O32806]”


SPX2205
2205
4866
158
474


NO-HIT
6


SPX2206
2206
4867
161
483
73
2.50E-06
[LN:F75354]
95









[AC:F75354]









[PN:MutT/nudix family protein]









[GN:DR1776]









[OR:Deinococcus radiodurans]


SPX2207
2207
4868
392
1176
578
1.10E-170
[LN:TRMU_BACSU]
105









[AC:O35020]









[GN:TRMU]









[OR:Bacillus subtilis]









[EC:2.1.1.61]









[DE:(EC 2.1.1.61)]









[SP:O35020]


SPX2208
2208
4869
60
180


NO-HIT
6


SPX2209
2209
4870
66
198


NO-HIT
6


SPX2210
2210
4871
551
1653
1324
7.00E-210
[LN:A41971]
169









[AC:A41971:A60282:A33134]









[PN:surface protein pspA precursor:pneumococcal surface protein A]









[GN:pspA]









[CL:cpl repeat homology]









[OR:Streptococcus pneumoniae]


SPX2211
2211
4872
79
237
98
1.60E-06
[GI:311109]
169









[LN:YSCISCLRP]









[AC:L16900]









[PN:intrastrand crosslink recognition protein]









[GN:Ixr1]









[OR:Saccharomyces cerevisiae]









[SR:Saccharomyces cerevisiae (strain ) DNA]


SPX2212
2212
4873
64
192
77
0.00063
[LN:B72392]
86









[AC:B72392]









[PN:hypothetical protein]









[GN:TM0315]









[OR:Thermotoga maritima]


SPX2213
2213
4874
103
309
87
0.0009
[GI:7292943]
106









[LN:AE003494]









[AC:AE003494:AE002593]









[GN:CG11075]









[OR:Drosophila melanogaster]









[SR:fruit fly]


SPX2214
2214
4875
106
318


NO-HIT
6


SPX2215
2215
4876
103
309
459
8.20E-56
[GI:6752385]
90









[LN:AF071807]









[AC:AF071807]









[PN:PspA]









[GN:pspA]









[OR:Streptococcus pneumoniae]


SPX2216
2216
4877
93
279


NO-HIT
6


SPX2217
2217
4878
100
300


NO-HIT
6


SPX2218
2218
4879
71
213


NO-HIT
6


SPX2219
2219
4880
253
759


NO-HIT
6


SPX2220
2220
4881
129
387


NO-HIT
6


SPX2221
2221
4882
301
903


NO-HIT
6


SPX2222
2222
4883
61
183


NO-HIT
6


SPX2223
2223
4884
125
375


NO-HIT
6


SPX2224
2224
4885
62
186


NO-HIT
6


SPX2225
2225
4886
227
681


NO-HIT
6


SPX2226
2226
4887
76
228


NO-HIT
6


SPX2227
2227
4888
319
957
1739
3.00E-234
“[LN:ALYS_BPHB3]
162









[AC:P32762]









[GN:HBL]









[OR:Streptococcus pneumoniae phage HB-3]









[EC:3.5.1.28]









[DE:LYTIC AMIDASE, (N-ACETYLMURAMOYL-L-ALANINE AMIDASE)]









[SP:P32762]”


SPX2228
2228
4889
111
333


NO-HIT
6


SPX2229
2229
4890
139
417
97
1.20E-08
[LN:VG14_BPB03]
110









[AC:Q37895]









[GN:14]









[OR:Bacteriophage B103]









[DE:LYSIS PROTEIN (LATE PROTEIN GP14)]









[SP:Q37895]


SPX2230
2230
4891
117
351


NO-HIT
6


SPX2231
2231
4892
68
204


NO-HIT
6


SPX2232
2232
4893
2120
6360
154
1.40E-22
[GI:4530154]
134









[LN:AF085222]









[AC:AF085222]









[PN:putative tail-host specificity protein]









[OR:Streptococcus thermophilus bacteriophage DT1]


SPX2233
2233
4894
79
237


NO-HIT
6


SPX2234
2234
4895
117
351


NO-HIT
6


SPX2235
2235
4896
1218
3654
236
2.10E-30
[GI:2392838]
76









[LN:AF011378]









[AC:AF011378]









[PN:unknown]









[OR:Bacteriophage sk1]


SPX2236
2236
4897
187
561
106
2.00E-07
[GI:5305335]
104









[LN:AF071081]









[AC:AF071081]









[PN:proline-rich mucin homolog]









[OR:Mycobacterium tuberculosis]


SPX2237
2237
4898
70
210


NO-HIT
6


SPX2238
2238
4899
73
219


NO-HIT
6


SPX2239
2239
4900
127
381


NO-HIT
6


SPX2240
2240
4901
138
414


NO-HIT
6


SPX2241
2241
4902
123
369
77
0.00049
[LN:T13522]
132









[AC:T13522]









[PN:hypothetical protein 33]









[CL:Bacillus phage phi-105 hypothetical protein 33]









[OR:Bacillus phage phi-105]


SPX2242
2242
4903
172
516
71
7.90E-06
[LN:T42287]
65









[AC:T42287]









[PN:hypothetical protein]









[OR:phage SPP1]


SPX2243
2243
4904
61
183


NO-HIT
6


SPX2244
2244
4905
113
339


NO-HIT
6


SPX2245
2245
4906
104
312


NO-HIT
6


SPX2246
2246
4907
63
189


NO-HIT
6


SPX2247
2247
4908
61
183
73
0.0003
[LN:F75258]
90









[AC:F75258]









[PN:hypothetical protein]









[GN:DR2560]









[OR:Deinococcus radiodurans]


SPX2248
2248
4909
282
846
226
2.60E-48
[GI:1369939]
92









[LN:BTP9011]









[AC:X84706]









[PN:major head protein]









[GN:mhp]









[OR:Bacteriophage B1]


SPX2249
2249
4910
195
585


NO-HIT
6


SPX2250
2250
4911
86
258


NO-HIT
6


SPX2251
2251
4912
76
228


NO-HIT
6


SPX2252
2252
4913
468
1404
80
1.20E-06
[LN:T13317]
87









[AC:T13317]









[PN:hypothetical protein 28]









[OR:Streptococcus phage phi-O1205]


SPX2253
2253
4914
490
1470
154
3.40E-39
[LN:T13620]
90









[AC:T13620]









[PN:hypothetical protein gp502]









[OR:Streptococcus phage phi-Sfi11]


SPX2254
2254
4915
433
1299
330
6.80E-48
[LN:TERL_BPSPP]
105









[AC:P54308]









[GN:2]









[OR:Bacteriophage SPP1]









[DE:TERMINASE LARGE SUBUNIT (G2P)]









[SP:P54308]


SPX2255
2255
4916
160
480
215
2.30E-32
[GI:4680607]
105









[LN:AF125198]









[AC:AF125198]









[PN:terminase small subunit]









[GN:TS1]









[OR:bacteriophage phi-FC1]


SPX2256
2256
4917
135
405
154
4.60E-16
[GI:4530181]
103









[LN:AF085222]









[AC:AF085222]









[PN:unknown]









[OR:Streptococcus thermophilus bacteriophage DT1]


SPX2257
2257
4918
124
372


NO-HIT
6


SPX2258
2258
4919
146
438
115
1.00E-14
[GI:5001708]
80









[LN:AF109874]









[AC:AF109874]









[PN:unknown]









[OR:Bacteriophage Tuc2009]


SPX2259
2259
4920
153
459


NO-HIT
6


SPX2260
2260
4921
87
261
109
9.50E-12
[GI:4530179]
103









[LN:AF085222]









[AC:AF085222]









[PN:unknown]









[OR:Streptococcus thermophilus bacteriophage DT1]


SPX2261
2261
4922
232
696
203
1.70E-24
[LN:T13308]
87









[AC:T13308]









[PN:hypothetical protein 19]









[OR:Streptococcus phage phi-O1205]


SPX2262
2262
4923
450
1350
358
1.30E-46
[GI:2689558]
63









[LN:U93688]









[AC:U93688]









[OR:Staphylococcus aureus]


SPX2263
2263
4924
274
822
470
7.10E-87
[LN:T13301]
87









[AC:T13301]









[PN:hypothetical protein 12]









[OR:Streptococcus phage phi-O1205]


SPX2264
2264
4925
78
234


NO-HIT
6


SPX2265
2265
4926
66
198


NO-HIT
6


SPX2266
2266
4927
169
507


NO-HIT
6


SPX2267
2267
4928
276
828


NO-HIT
6


SPX2268
2268
4929
106
318


NO-HIT
6


SPX2269
2269
4930
398
1194


NO-HIT
6


SPX2270
2270
4931
163
489


NO-HIT
6


SPX2271
2271
4932
120
360


NO-HIT
6


SPX2272
2272
4933
161
483
256
2.10E-45
[GI:2352435]
92









[LN:AF004379]









[AC:AF004379]









[OR:Streptococcus thermophilus bacteriophage Sfi21]


SPX2273
2273
4934
258
774


NO-HIT
6


SPX2274
2274
4935
77
231


NO-HIT
6


SPX2275
2275
4936
114
342


NO-HIT
6


SPX2276
2276
4937
63
189


NO-HIT
6


SPX2277
2277
4938
87
261


NO-HIT
6


SPX2278
2278
4939
91
273


NO-HIT
6


SPX2279
2279
4940
80
240


NO-HIT
6


SPX2280
2280
4941
64
192


NO-HIT
6


SPX2281
2281
4942
68
204


NO-HIT
6


SPX2282
2282
4943
67
201


NO-HIT
6


SPX2283
2283
4944
72
216
101
3.70E-09
[LN:Y272_METJA]
132









[AC:Q57720]









[GN:MJ0272]









[OR:Methanococcus jannaschii]









[DE:HYPOTHETICAL TRANSCRIPTIONAL REGULATOR MJ0272]









[SP:Q57720]


SPX2284
2284
4945
68
204


NO-HIT
6


SPX2285
2285
4946
230
690


NO-HIT
6


SPX2286
2286
4947
264
792
112
4.00E-15
[LN:T13264]
82









[AC:T13264]









[PN:repressor protein]









[OR:Lactococcus lactis phage BK5-T]


SPX2287
2287
4948
317
951
102
5.00E-09
[LN:F59095]
94









[AC:F59095]









[PN:hypothetical protein pXO1-38]









[GN:pXO1-38]









[OR:Bacillus anthracis]


SPX2288
2288
4949
58
174


NO-HIT
6


SPX2289
2289
4950
376
1128
212
3.50E-43
[GI:2689564]
87









[LN:U93688]









[AC:U93688]









[PN:integrase]









[GN:int]









[OR:Staphylococcus aureus]


SPX2290
2290
4951
62
186


NO-HIT
6


SPX2291
2291
4952
353
1059
81
0.00071
[LN:AF147045]
138









[AC:AF147045]









[PN:cytochrome c oxidase subunit 1]









[GN:COI]









[OR:Mitochondrion Dolichoderus lutosus]









[SR:Dolichoderus lutosus]


SPX2292
2292
4953
64
192


NO-HIT
6


SPX2293
2293
4954
71
213


NO-HIT
6


SPX2294
2294
4955
81
243


NO-HIT
6


SPX2295
2295
4956
149
447


NO-HIT
6


SPX2296
2296
4957
60
180


NO-HIT
6


SPX2297
2297
4958
117
351
137
3.30E-14
[GI:4760910]
86









[LN:AF099088]









[AC:AF099088]









[PN:EntT]









[GN:entT]









[OR:Enterococcus faecium]


SPX2298
2298
4959
288
864
117
4.70E-08
[GI:4102023]
134









[LN:AF007761]









[AC:AF007761]









[PN:MutR]









[GN:mutR]









[FN:positive transcriptional regulator of mutA]









[OR:Streptococcus mutans]


SPX2299
2299
4960
125
375


NO-HIT
6


SPX2300
2300
4961
76
228


NO-HIT
6


SPX2301
2301
4962
127
381


NO-HIT
6


SPX2302
2302
4963
75
225


NO-HIT
6


SPX2303
2303
4964
70
210


NO-HIT
6


SPX2304
2304
4965
68
204


NO-HIT
6


SPX2305
2305
4966
288
864
117
4.70E-08
[GI:4102023]
134









[LN:AF007761]









[AC:AF007761]









[PN:MutR]









[GN:mutR]









[FN:positive transcriptional regulator of mutA]









[OR:Streptococcus mutans]


SPX2306
2306
4967
173
519
840
6.50E-114
[GI:663278]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX2307
2307
4968
122
366


NO-HIT
6


SPX2308
2308
4969
96
288
279
1.60E-35
[GI:663279]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX2309
2309
4970
256
768
1235
1.10E-172
[GI:663279]
138









[LN:STRCOMAA]









[AC:M36180:L15190]









[PN:transposase]









[OR:Streptococcus pneumoniae]









[SR:Streptococcus pneumoniae (strain RX1) DNA]


SPX2310
2310
4971
157
471
375
6.90E-56
[LN:ASSY_BACSU]
98









[AC:O34347]









[GN:ARGG]









[OR:Bacillus subtilis]









[EC:6.3.4.5]









[DE:LIGASE)]









[SP:O34347]


SPX2311
2311
4972
266
798
200
6.10E-32
“[LN:B72357]
181









[AC:B72357]









[PN:amino acid ABC transporter, periplasmic amino acid-binding protein]









[GN:TM0593]









[CL:lysine-arginine-ornithine-binding protein]









[OR:Thermotoga maritima]”


SPX2312
2312
4973
214
642
420
1.80E-51
[LN:F81408]
125









[AC:F81408]









[PN:ABC-type transmembrane transport protein Cj0607 [imported]]









[GN:Cj0607]









[OR:Campylobacter jejuni]


SPX2313
2313
4974
59
177
80
1.80E-07
[LN:F72598]
92









[AC:F72598]









[PN:hypothetical protein APE1254]









[GN:APE1254]









[OR:Aeropyrum pernix]


SPX2314
2314
4975
439
1317


NO-HIT
6


SPX2315
2315
4976
371
1113


NO-HIT
6


SPX2316
2316
4977
72
216


NO-HIT
6


SPX2317
2317
4978
84
252


NO-HIT
6


SPX2318
2318
4979
288
864
117
4.70E-08
[GI:4102023]
134









[LN:AF007761]









[AC:AF007761]









[PN:MutR]









[GN:mutR]









[FN:positive transcriptional regulator of mutA]









[OR:Streptococcus mutans]


SPX2319
2319
4980
196
588
300
1.00E-34
[GI:1619598]
108









[LN:LGAPFA]









[AC:Y08498]









[PN:aggregation promoting protein]









[GN:apfA]









[OR:Lactobacillus gasseri]


SPX2320
2320
4981
97
291


NO-HIT
6


SPX2321
2321
4982
224
672
276
8.70E-69
[LN:SDHB_BACSU]
115









[AC:O34635]









[GN:YLOW]









[OR:Bacillus subtilis]









[EC:4.2.1.13]









[DE:DEAMINASE) (SDH) (L-SD)]









[SP:O34635]


SPX2322
2322
4983
291
873
877
9.00E-119
[LN:SDHA_BACSU]
115









[AC:O34607]









[GN:YLPA]









[OR:Bacillus subtilis]









[EC:4.2.1.13]









[DE:DEAMINASE) (SDH) (L-SD)]









[SP:O34607]


SPX2323
2323
4984
178
534


NO-HIT
6


SPX2324
2324
4985
211
633
123
1.50E-15
[GI:7576264]
95









[LN:ECH277403]









[AC:AJ277403]









[PN:IndB protein]









[GN:indB]









[OR:Erwinia chrysanthemi]


SPX2325
2325
4986
72
216


NO-HIT
6


SPX2326
2326
4987
617
1851
1006
3.00E-136
[GI:6601348]
86









[LN:AF155805]









[AC:AF155805]









[PN:Cps9E]









[GN:cps9E]









[OR:Streptococcus suis]


SPX2327
2327
4988
84
252
135
6.70E-14
[LN:S28486]
72









[AC:S28486]









[PN:hypothetical protein 2]









[OR:Vibrio cholerae]


SPX2328
2328
4989
392
1176
123
7.20E-25
[LN:T44514]
93









[AC:T44514]









[PN:hypothetical protein 6P [imported]]









[OR:Plesiomonas shigelloides]


SPX2329
2329
4990
102
306


NO-HIT
6


SPX2330
2330
4991
249
747
142
5.40E-29
[LN:YYCB_BACSU]
137









[AC:P37482]









[GN:YYCB]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 43.2 KD PROTEIN IN DNAC-RPLI INTERGENIC REGION]









[SP:P37482]


SPX2331
2331
4992
143
429
143
9.10E-15
[LN:PQ0016]
80









[AC:PQ0016]









[PN:hypothetical 9K protein]









[OR:Lactobacillus confusus]


SPX2332
2332
4993
109
327
102
4.10E-07
[LN:D75250]
100









[AC:D75250]









[PN:conserved hypothetical protein]









[GN:DR2629]









[OR:Deinococcus radiodurans]


SPX2333
2333
4994
198
594


NO-HIT
6


SPX2334
2334
4995
304
912


NO-HIT
6


SPX2335
2335
4996
123
369


NO-HIT
6


SPX2336
2336
4997
355
1065
118
3.00E-07
[LN:T18283]
82









[AC:T18283]









[PN:hypothetical protein G5]









[OR:Dictyostelium discoideum]


SPX2337
2337
4998
318
954


NO-HIT
6


SPX2338
2338
4999
329
987
925
1.60E-165
[GI:2565150]
89









[LN:LLU92974]









[AC:U92974:M90760:M90761]









[PN:unknown]









[OR:Lactococcus lactis]


SPX2339
2339
5000
69
207


NO-HIT
6


SPX2340
2340
5001
515
1545


NO-HIT
6


SPX2341
2341
5002
134
402


NO-HIT
6


SPX2342
2342
5003
308
924
389
1.50E-61
[GI:1483212]
104









[LN:ATCELD]









[AC:Z77855]









[PN:sugar-binding transport protein]









[OR:Anaerocellum thermophilum]


SPX2343
2343
5004
320
960
601
9.60E-95
[GI:1483211]
104









[LN:ATCELD]









[AC:Z77855]









[PN:sugar-binding transport protein]









[OR:Anaerocellum thermophilum]


SPX2344
2344
5005
70
210


NO-HIT
6


SPX2345
2345
5006
120
360


NO-HIT
6


SPX2346
2346
5007
116
348
577
5.80E-76
[GI:4200438]
96









[LN:AF026471]









[AC:AF026471]









[PN:putative transposase]









[OR:Streptococcus pneumoniae]


SPX2347
2347
5008
177
531
299
3.70E-73
[LN:A37146]
182









[AC:A37146:A44901:S11354:C69699:I39962]









[PN:ribosomal protein S4:ribosomal protein BS4 (rpsD)]









[GN:rpsD]









[CL:Escherichia coli ribosomal protein S4]









[OR:Bacillus subtilis]


SPX2348
2348
5009
359
1077
1709
2.00E-231
[GI:5830539]
102









[LN:SPAJ6397]









[AC:AJ006397]









[PN:histidine kinase]









[GN:hk08]









[OR:Streptococcus pneumoniae]


SPX2349
2349
5010
233
699
1196
1.40E-161
[GI:5830538]
104









[LN:SPAJ6397]









[AC:AJ006397]









[PN:response regulator]









[GN:rr08]









[OR:Streptococcus pneumoniae]


SPX2350
2350
5011
124
372


NO-HIT
6


SPX2351
2351
5012
891
2673
106
0.00022
[GI:7293562]
105









[LN:AE003511]









[AC:AE003511:AE002593]









[GN:CG7874]









[OR:Drosophila melanogaster]









[SR:fruit fly]


SPX2352
2352
5013
190
570


NO-HIT
6


SPX2353
2353
5014
137
411


NO-HIT
6


SPX2354
2354
5015
179
537
199
2.70E-20
[GI:3550634]
151









[LN:SPAJ6986]









[AC:AJ006986]









[PN:glycosyl transferase]









[GN:cap33fH]









[FN:synthesis of capsular polysaccharide]









[OR:Streptococcus pneumoniae]


SPX2355
2355
5016
222
666
346
1.00E-42
[LN:YKQB_BACSU]
144









[AC:P39760]









[GN:YKQB]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 24.3 KD PROTEIN IN KINC-ADEC INTERGENIC REGION (ORF4)]









[SP:P39760]


SPX2356
2356
5017
460
1380
339
7.90E-94
[LN:G75367]
99









[AC:G75367]









[PN:potassium uptake protein KtrB]









[GN:DR1668]









[OR:Deinococcus radiodurans]


SPX2357
2357
5018
62
186
162
1.60E-17
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX2358
2358
5019
255
765
75
8.50E-08
[LN:D72516]
143









[AC:D72516]









[PN:probable uridine phosphorylase APE2105]









[GN:APE2105]









[CL:purine-nucleoside phosphorylase pnp]









[OR:Aeropyrum pernix]


SPX2359
2359
5020
63
189
91
8.80E-06
“[GI:6332762]
194









[LN:AB033763]









[AC:AB033763:AB014419:AB014429:AB014439]









[PN:hypothetical protein]









[OR:Staphylococcus aureus]









[SR:Staphylococcus aureus (strain:NCTC10442) DNA, clone_lib:Lambda das]”


SPX2360
2360
5021
99
297
153
6.00E-20
[LN:YQHL_BACSU]
141









[AC:P54510]









[GN:YQHL]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 14.6 KD PROTEIN IN GCVT-SPOIIIAA INTERGENIC REGION]









[SP:P54510]


SPX2361
2361
5022
121
363


NO-HIT
6


SPX2362
2362
5023
98
294
194
1.30E-21
“[GI:6332750]
194









[LN:AB033763]









[AC:AB033763:AB014419:AB014429:AB014439]









[PN:hypothetical protein]









[OR:Staphylococcus aureus]









[SR:Staphylococcus aureus (strain:NCTC10442) DNA, clone_lib:Lambda das]”


SPX2363
2363
5024
82
246
167
8.40E-17
[LN:A75356]
100









[AC:A75356]









[PN:conserved hypothetical protein]









[GN:DR1764]









[OR:Deinococcus radiodurans]


SPX2364
2364
5025
132
396
175
2.80E-26
[LN:T44495]
90









[AC:T44495]









[PN:hypothetical protein YFIE [imported]]









[OR:Bacillus halodurans]


SPX2365
2365
5026
346
1038
219
2.60E-44
[GI:6562808]
119









[LN:SC4A7]









[AC:AL133423]









[PN:putative aldose 1-epimerase]









[GN:SC4A7.35]









[OR:Streptomyces coelicolor A3(2)]


SPX2366
2366
5027
153
459


NO-HIT
6


SPX2367
2367
5028
389
1167
473
3.90E-95
[LN:AGAS_ECOLI]
89









[AC:P42907]









[GN:AGAS]









[OR:Escherichia coli]









[DE:AGAS PROTEIN]









[SP:P42907]


SPX2368
2368
5029
83
249
77
6.20E-05
[GI:1914870]
81









[LN:SPZ82001]









[AC:Z82001]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX2369
2369
5030
135
405
103
3.80E-13
[GI:5669855]
128









[LN:AF130465]









[AC:AF130465]









[PN:mannose-specific phosphotransferase system]









[GN:manL]









[OR:Streptococcus salivarius]


SPX2370
2370
5031
277
831
144
4.90E-34
“[LN:PTPD_ECOLI]
102









[AC:P42911]









[GN:AGAD]









[OR:Escherichia coli]









[DE:ENZYME II, D COMPONENT)]









[SP:P42911]”


SPX2371
2371
5032
302
906
128
6.60E-16
[GI:1732200]
115









[LN:VFU65015]









[AC:U65015]









[PN:PTS permease for mannose subunit IIPMan]









[GN:manY]









[OR:Vibrio furnissii]


SPX2372
2372
5033
159
477
298
2.50E-36
[GI:6690421]
105









[LN:AF129168]









[AC:AF129168]









[PN:EIIB sorbose-PTS homolog]









[GN:sorB]









[OR:Lactobacillus casei]


SPX2373
2373
5034
509
1527
265
3.30E-90
“[LN:JC5618]
134









[AC:JC5618]









[PN:beta-galactosidase,:lactase]









[GN:bgaC]









[CL:beta-galactosidase bga]









[OR:Bacillus circulans]









[EC:3.2.1.23]”


SPX2374
2374
5035
131
393
358
5.70E-44
“[LN:JC5618]
134









[AC:JC5618]









[PN:beta-galactosidase,:lactase]









[GN:bgaC]









[CL:beta-galactosidase bga]









[OR:Bacillus circulans]









[EC:3.2.1.23]”


SPX2375
2375
5036
239
717
142
7.80E-15
[LN:F69750]
144









[AC:F69750]









[PN:transcription regulator GntR family homolog ybgA]









[GN:ybgA]









[CL:transcription regulator GntR]









[OR:Bacillus subtilis]


SPX2376
2376
5037
1304
3912
6324
0
“[LN:STRH_STRPN]
139









[AC:P49610]









[GN:STRH]









[OR:Streptococcus pneumoniae]









[EC:3.2.1.52]









[DE:BETA-N-ACETYLHEXOSAMINIDASE PRECURSOR,]









[SP:P49610]”


SPX2377
2377
5038
130
390


NO-HIT
6


SPX2378
2378
5039
433
1299
1678
1.40E-227
[LN:PUR8_BACSU]
140









[AC:P12047]









[GN:PURB:PURE]









[OR:Bacillus subtilis]









[EC:4.3.2.2]









[DE:(GLUTAMYL-TRNA SYNTHETASE REGULATORY FACTOR)]









[SP:P12047]


SPX2379
2379
5040
76
228


NO-HIT
6


SPX2380
2380
5041
384
1152
286
1.70E-65
[GI:5051462]
155









[LN:NME242842]









[AC:AJ242842]









[PN:putative phosphoribosylaminoimidazole]









[GN:purK]









[FN:purine nucleotide synthesis]









[OR:Neisseria meningitidis]


SPX2381
2381
5042
155
465
515
5.30E-66
[GI:3892884]
75









[LN:LLJ000883]









[AC:AJ000883]









[GN:purE]









[OR:Lactococcus lactis]


SPX2382
2382
5043
421
1263
589
2.10E-157
[GI:3892883]
75









[LN:LLJ000883]









[AC:AJ000883]









[GN:purD]









[OR:Lactococcus lactis]


SPX2383
2383
5044
227
681


NO-HIT
6


SPX2384
2384
5045
523
1569
881
2.30E-213
[LN:PUR9_BACSU]
130









[AC:P12048]









[GN:PURH:PURHJ]









[OR:Bacillus subtilis]









[EC:2.1.2.3:3.5.4.10]









[DE:(IMP SYNTHETASE) (ATIC)]]









[SP:P12048]


SPX2385
2385
5046
170
510
136
9.10E-15
“[LN:VANZ_ENTFC]
123









[AC:Q06242]









[GN:VANZ]









[OR:Enterococcus faecium]









[SR:,Streptococcus faecium]









[DE:VANZ PROTEIN]









[SP:Q06242]”


SPX2386
2386
5047
116
348


NO-HIT
6


SPX2387
2387
5048
182
546
553
2.20E-72
[GI:6446399]
115









[LN:SPU70775]









[AC:U70775]









[PN:phosphoribosylglycinamide formyltransferase]









[OR:Streptococcus pyogenes]


SPX2388
2388
5049
341
1023
1084
7.20E-148
[GI:3150047]
140









[LN:AF016634]









[AC:AF016634]









[PN:phosphoribosylformylglycinamide cyclo-ligase]









[GN:pur5]









[OR:Lactococcus lactis subsp. cremoris]


SPX2389
2389
5050
481
1443
1727
7.50E-248
[GI:4097534]
122









[LN:LLU64311]









[AC:U64311]









[PN:phosphoribosylpyrophosphate amidotransferase]









[GN:purF]









[OR:Lactococcus lactis]


SPX2390
2390
5051
1243
3729
149
3.00E-49
“[LN:C69492]
217









[AC:C69492]









[PN:phosphoribosylformylglycinamidine synthase, component II:formylglycinamide ribotide amidotransferase:phosphoribosylformylglycinamidine synthetase]









[OR:Archaeoglobus fulgidus]









[EC:6.3.5.3]”


SPX2391
2391
5052
45
135


NO-HIT
6


SPX2392
2392
5053
204
612
875
9.90E-117
[LN:PUR7_STRPN]
117









[AC:Q07296]









[GN:PURC]









[OR:Streptococcus pneumoniae]









[EC:6.3.2.6]









[DE:(SAICAR SYNTHETASE)]









[SP:Q07296]


SPX2393
2393
5054
124
372
175
1.90E-17
“[LN:H75412]
160









[AC:H75412]









[PN:spermidine/putrescine ABC transporter, periplasmic spermidine/putrescine-binding protein]









[GN:DR1305]









[OR:Deinococcus radiodurans]”


SPX2394
2394
5055
431
1293
2159
2.90E-302
[GI:2804700]
87









[LN:AF030361]









[AC:AF030361]









[PN:transposase]









[OR:Streptococcus pneumoniae]


SPX2395
2395
5056
86
258


NO-HIT
6


SPX2396
2396
5057
166
498
300
8.70E-37
[LN:YEBR_ECOLI]
163









[AC:P76270:O07976:O07978]









[GN:YEBR]









[OR:Escherichia coli]









[DE:HYPOTHETICAL 20.3 KD PROTEIN IN PRC-PPHA INTERGENIC REGION]









[SP:P76270:O07976:O07978]


SPX2397
2397
5058
552
1656
749
7.10E-135
“[LN:S13786]
245









[AC:S13786:S00745:S66049:B69618]









[PN:DNA-directed DNA polymerase, III chain dnaX:DNA polymerase III (gamma and tau subunits) dnaX]









[GN:dnaX:dnaZX]









[CL:DNA-directed DNA polymerase III gamma chain]









[OR:Bacillus subtilis]









[EC:2.7.7.7]”


SPX2398
2398
5059
65
195


NO-HIT
6


SPX2399
2399
5060
257
771
948
1.70E-125
[LN:V296_BACSU]
109









[AC:P80866]









[GN:YURI]









[OR:Bacillus subtilis]









[DE:VEGETATIVE PROTEIN 296 (VEG296)]









[SP:P80866]


SPX2400
2400
5061
420
1260
583
1.90E-87
[LN:G70019]
161









[AC:G70019]









[PN:conserved hypothetical protein yurX]









[GN:yurX]









[CL:Methanobacterium thermoautotrophicum ABC transporter Ycf24]









[OR:Bacillus subtilis]


SPX2401
2401
5062
409
1227
622
8.60E-181
[LN:F70019]
105









[AC:F70019]









[PN:nifS protein homolog yurW]









[GN:yurW]









[CL:nifS protein]









[OR:Bacillus subtilis]


SPX2402
2402
5063
157
471
229
1.90E-43
[LN:E70019]
177









[AC:E70019]









[PN:nitrogen fixation protein nifU homolog yurV]









[GN:yurV]









[CL:Yeast nitrogen fixation protein:nitrogen fixation protein homology]









[OR:Bacillus subtilis]


SPX2403
2403
5064
470
1410
1721
1.20E-229
[LN:D70019]
161









[AC:D70019]









[PN:conserved hypothetical protein yurU]









[GN:yurU]









[CL:Methanobacterium thermoautotrophicum ABC transporter Ycf24]









[OR:Bacillus subtilis]


SPX2404
2404
5065
65
195


NO-HIT
6


SPX2405
2405
5066
62
186
112
8.10E-11
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX2406
2406
5067
414
1242
2059
6.00E-276
“[GI:1620468]
105









[LN:SPDACAO]









[AC:X99400]









[PN:D,D-carboxypeptidase]









[GN:dacA]









[OR:Streptococcus pneumoniae]”


SPX2407
2407
5068
370
1110
1807
5.00E-255
[GI:1620467]
89









[LN:SPDACAO]









[AC:X99400]









[PN:membrane protein]









[OR:Streptococcus pneumoniae]


SPX2408
2408
5069
73
219


NO-HIT
6


SPX2409
2409
5070
67
201


NO-HIT
6


SPX2410
2410
5071
247
741
258
7.40E-41
[LN:B69627]
138









[AC:B69627]









[PN:transcription repressor of fructose operon fruR]









[GN:fruR]









[CL:regulatory protein gutR]









[OR:Bacillus subtilis]


SPX2411
2411
5072
304
912
725
2.80E-94
[LN:A69627]
123









[AC:A69627]









[PN:fructose 1-phosphate kinase fruB]









[GN:fruB]









[CL:6-phosphofructokinase 2]









[OR:Bacillus subtilis]


SPX2412
2412
5073
76
228


NO-HIT
6


SPX2413
2413
5074
651
1953
371
4.60E-168
“[LN:H69626]
246









[AC:H69626]









[PN:PTS fructose-specific enzyme IIBC component fruA]









[GN:fruA]









[CL:phosphotransferase system enzyme II, fructose-specific:phosphotransferase system mannitol-specific enzyme II factor III homology]









[OR:Bacillus subtilis]”


SPX2414
2414
5075
738
2214
934
4.10E-198
[LN:SP3E_BACSU]
126









[AC:P21458:P21459]









[GN:SPOIIIE]









[OR:Bacillus subtilis]









[DE:STAGE III SPORULATION PROTEIN E]









[SP:P21458:P21459]


SPX2415
2415
5076
84
252
82
0.00017
[GI:2257458]
153









[LN:AB000222]









[AC:AB000222]









[GN:epr]









[FN:glycylglycine endopeptidase resistance]









[OR:Staphylococcus capitis]









[SR:Staphylococcus capitis DNA]


SPX2416
2416
5077
95
285
124
7.00E-12
“[LN:A70132]
117









[AC:A70132]









[PN:cell division protein homolog]









[OR:Borrelia burgdorferi]









[SR:, Lyme disease spirochete]”


SPX2417
2417
5078
72
216


NO-HIT
6


SPX2418
2418
5079
220
660
102
0.00013
“[LN:T06029]
127









[AC:T06029]









[PN:hypothetical protein T28I19.100]









[GN:T28I19.100]









[OR:Arabidopsis thaliana]









[SR:, mouse-ear cress]”


SPX2419
2419
5080
401
1203
698
8.70E-120
“[LN:NIFS_LACDE]
131









[AC:P31672]









[OR:Lactobacillus delbrueckii]









[SR:,subspbulgaricus]









[DE:NIFS PROTEIN HOMOLOG (FRAGMENT)]









[SP:P31672]”


SPX2420
2420
5081
405
1215
982
1.40E-130
[LN:THII_BACSU]
121









[AC:O34595]









[GN:THII]









[OR:Bacillus subtilis]









[DE:PROBABLE THIAMINE BIOSYNTHESIS PROTEIN THII]









[SP:O34595]


SPX2421
2421
5082
210
630
115
3.40E-15
[LN:G75475]
100









[AC:G75475]









[PN:conserved hypothetical protein]









[GN:DR0779]









[OR:Deinococcus radiodurans]


SPX2422
2422
5083
116
348


NO-HIT
6


SPX2423
2423
5084
112
336


NO-HIT
6


SPX2424
2424
5085
144
432


NO-HIT
6


SPX2425
2425
5086
61
183


NO-HIT
6


SPX2426
2426
5087
389
1167
82
2.50E-06
[LN:T35924]
101









[AC:T35924]









[PN:hypothetical protein SC9B5.04]









[GN:SC9B5.04]









[OR:Streptomyces coelicolor]


SPX2427
2427
5088
498
1494
137
2.50E-32
[GI:1841495]
95









[LN:SEHSDRMS]









[AC:Y11005]









[PN:StySKI methylase]









[GN:hsdM]









[OR:Salmonella enterica]


SPX2428
2428
5089
374
1122
109
3.30E-14
[LN:YC18_METJA]
114









[AC:Q58615]









[GN:MJ1218]









[OR:Methanococcus jannaschii]









[DE:HYPOTHETICAL PROTEIN MJ1218]









[SP:Q58615]


SPX2429
2429
5090
79
237


NO-HIT
6


SPX2430
2430
5091
138
414


NO-HIT
6


SPX2431
2431
5092
276
828
153
1.90E-22
[LN:A75153]
164









[AC:A75153]









[PN:integrase/recombinase xerd PAB0255]









[GN:xerD-like:PAB0255]









[CL:probable site-specific integrase/recombinase XerC]









[OR:Pyrococcus abyssi]


SPX2432
2432
5093
369
1107
148
4.50E-19
[GI:3057063]
84









[LN:AF013165]









[AC:AF013165]









[PN:HsdS]









[GN:hsds]









[OR:Lactococcus lactis]


SPX2433
2433
5094
1117
3351
153
6.50E-30
“[LN:T1R_ECOLI]
139









[AC:P08956]









[GN:HSDR:HSR]









[OR:Escherichia coli]









[EC:3.1.21.3]









[DE:TYPE I RESTRICTION ENZYME ECOK I R PROTEIN,]









[SP:P08956]”


SPX2434
2434
5095
157
471
132
1.60E-24
[LN:AHRC_BACSU]
117









[AC:P17893]









[GN:AHRC]









[OR:Bacillus subtilis]









[DE:ARGININE HYDROXIMATE RESISTANCE PROTEIN]









[SP:P17893]


SPX2435
2435
5096
758
2274
1298
1.20E-249
“[LN:PEPX_LACLC]
195









[AC:P22093]









[GN:PEPX]









[OR:Lactococcus lactis]









[SR:,subspcremoris:Streptococcus cremoris]









[EC:3.4.14.11]









[DE:PEPTIDASE) (X-PROLYL-DIPEPTIDYL AMINOPEPTIDASE) (X-PDAP)]









[SP:P22093]”


SPX2436
2436
5097
1034
3102
563
5.40E-170
“[LN:DP3A_BACSU]
125









[AC:O34623]









[GN:DNAE]









[OR:Bacillus subtilis]









[EC:2.7.7.7]









[DE:DNA POLYMERASE III, ALPHA CHAIN,]









[SP:O34623]”


SPX2437
2437
5098
63
189


NO-HIT
6


SPX2438
2438
5099
336
1008
1356
2.50E-182
“[LN:K6PF_LACLA]
157









[AC:Q07636]









[GN:PFKA:PFK]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[EC:2.7.1.11]









[DE:(PHOSPHOHEXOKINASE)]









[SP:Q07636]”


SPX2439
2439
5100
236
708
1007
8.20E-134
[GI:6708108]
153









[LN:AF172173]









[AC:AF172173]









[PN:pyruvate kinase]









[GN:pyk]









[FN:conversion of phosphoenolpyruvate to pyruvate]









[OR:Streptococcus thermophilus]


SPX2440
2440
5101
305
915
1099
9.10E-150
[GI:6708108]
153









[LN:AF172173]









[AC:AF172173]









[PN:pyruvate kinase]









[GN:pyk]









[FN:conversion of phosphoenolpyruvate to pyruvate]









[OR:Streptococcus thermophilus]


SPX2441
2441
5102
74
222
137
1.60E-13
[LN:G71171]
95









[AC:G71171]









[PN:hypothetical protein PH0571]









[GN:PH0571]









[OR:Pyrococcus horikoshii]


SPX2442
2442
5103
67
201
73
3.00E-08
[LN:VINT_BPL54]
87









[AC:P20709]









[GN:INT]









[OR:Bacteriophage L54a]









[DE:INTEGRASE]









[SP:P20709]


SPX2443
2443
5104
101
303
95
3.10E-05
[GI:763050]
84









[LN:BTU21935]









[AC:U21935]









[PN:repressor protein]









[OR:Bacteriophage T270]


SPX2444
2444
5105
85
255
89
1.90E-08
[GI:509672]
128









[LN:TU2CIRPRSR]









[AC:L26219]









[PN:repressor protein]









[GN:cI]









[OR:Bacteriophage Tuc2009]









[SR:Bacteriophage Tuc2009 DNA]


SPX2445
2445
5106
291
873
393
1.90E-60
[GI:4580015]
78









[LN:AF049342]









[AC:AF049342]









[PN:unknown]









[OR:Treponema denticola]


SPX2446
2446
5107
128
384
364
3.60E-46
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX2447
2447
5108
104
312


NO-HIT
6


SPX2448
2448
5109
239
717


NO-HIT
6


SPX2449
2449
5110
132
396


NO-HIT
6


SPX2450
2450
5111
272
816
184
2.20E-58
[LN:D69759]
136









[AC:D69759]









[PN:hypothetical protein ycgQ]









[GN:ycgQ]









[CL:Bacillus subtilis hypothetical protein ycgQ]









[OR:Bacillus subtilis]


SPX2451
2451
5112
302
906
369
7.00E-86
[LN:E69759]
87









[AC:E69759]









[PN:hypothetical protein ycgR]









[GN:ycgR]









[OR:Bacillus subtilis]


SPX2452
2452
5113
710
2130
644
1.20E-222
[LN:G69773]
128









[AC:G69773]









[PN:conserved hypothetical protein ydcI]









[GN:ydcI]









[CL:hypothetical protein ydcI]









[OR:Bacillus subtilis]


SPX2453
2453
5114
150
450
256
7.80E-44
[GI:7007441]
129









[LN:AB031213]









[AC:AB031213]









[PN:YdcK]









[GN:ydcK]









[OR:Bacillus halodurans]









[SR:Bacillus halodurans (strain:C-125) DNA]


SPX2454
2454
5115
85
255
90
7.80E-11
[LN:E70043]
87









[AC:E70043]









[PN:hypothetical protein yvlC]









[GN:yvlC]









[OR:Bacillus subtilis]


SPX2455
2455
5116
64
192


NO-HIT
6


SPX2456
2456
5117
253
759
486
8.70E-81
[LN:A70001]
188









[AC:A70001]









[PN:ABC transporter (ATP-binding protein) homolog ytsC]









[GN:ytsC]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Bacillus subtilis]


SPX2457
2457
5118
75
225
76
3.20E-05
[LN:G72510]
92









[AC:G72510]









[PN:hypothetical protein APE2061]









[GN:APE2061]









[OR:Aeropyrum pernix]


SPX2458
2458
5119
663
1989
249
1.70E-50
[LN:B70001]
101









[AC:B70001]









[PN:ABC transporter (permease) homolog ytsD]









[GN:ytsD]









[OR:Bacillus subtilis]


SPX2459
2459
5120
197
591
230
2.10E-25
[LN:SPBC1683]
121









[AC:AL355920]









[PN:hypothetical protein]









[GN:SPBC1683.10c]









[OR:Schizosaccharomyces pombe]









[SR:fission yeast]


SPX2460
2460
5121
365
1095
1143
8.40E-154
[GI:517210]
65









[LN:SPU11799]









[AC:U11799]









[OR:Streptococcus pyogenes]


SPX2461
2461
5122
61
183


NO-HIT
6


SPX2462
2462
5123
492
1476
585
3.60E-138
“[LN:DCLY_BACSU]
134









[AC:P21885:P26934]









[GN:CAD]









[OR:Bacillus subtilis]









[EC:4.1.1.18]









[DE:LYSINE DECARBOXYLASE, (LDC)]









[SP:P21885:P26934]”


SPX2463
2463
5124
79
237


NO-HIT
6


SPX2464
2464
5125
176
528
83
1.20E-07
“[GI:6009430]
140









[LN:AB024946]









[AC:AB024946]









[GN:orf54]









[OR:Escherichia coli]









[SR:Escherichia coli (sub_species:enteropathogenic, strain:B171]”


SPX2465
2465
5126
287
861
439
5.40E-79
[LN:SPEE_BACSU]
99









[AC:P70998]









[GN:SPEE]









[OR:Bacillus subtilis]









[EC:2.5.1.16]









[DE:(SPDSY)]









[SP:P70998]


SPX2466
2466
5127
420
1260
1090
2.30E-187
[LN:C81435]
107









[AC:C81435]









[PN:hypothetical protein Cj0172c [imported]]









[GN:Cj0172c]









[OR:Campylobacter jejuni]


SPX2467
2467
5128
376
1128
411
7.60E-103
[LN:E75398]
104









[AC:E75398]









[PN:carboxynorspermidine decarboxylase]









[GN:DR1410]









[OR:Deinococcus radiodurans]


SPX2468
2468
5129
362
1086
530
3.80E-94
[GI:5712716]
80









[LN:AF153708]









[AC:AF153708]









[PN:unknown]









[OR:Pseudomonas sp. BG33R]


SPX2469
2469
5130
292
876
585
1.20E-110
[GI:5262946]
106









[LN:LES19104]









[AC:Y19104]









[PN:beta-alanine synthase]









[OR:Lycopersicon esculentum]









[SR:tomato]


SPX2470
2470
5131
270
810
209
6.80E-43
[LN:YXEH_BACSU]
141









[AC:P54947]









[GN:YXEH:IP1B]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 30.2 KD PROTEIN IN IDH-DEOR INTERGENIC REGION]









[SP:P54947]


SPX2471
2471
5132
74
222


NO-HIT
6


SPX2472
2472
5133
224
672
90
2.30E-09
[LN:E69787]
87









[AC:E69787]









[PN:hypothetical protein ydiL]









[GN:ydiL]









[OR:Bacillus subtilis]


SPX2473
2473
5134
303
909
229
5.80E-46
[LN:T44638]
172









[AC:T44638]









[PN:capsular polysaccharide biosynthesis protein cpsY [imported]]









[GN:cpsY]









[CL:probable transcription regulator lsyR]









[OR:Streptococcus agalactiae]


SPX2474
2474
5135
154
462
197
1.80E-31
[LN:LSPA_BACSU]
140









[AC:Q45479]









[GN:LSPA:LSP]









[OR:Bacillus subtilis]









[EC:3.4.23.36]









[DE:PEPTIDASE) (SIGNAL PEPTIDASE II) (SPASE II)]









[SP:Q45479]


SPX2475
2475
5136
296
888
888
1.80E-117
[LN:YLYB_BACSU]
158









[AC:Q45480:O31732]









[GN:YLYB]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 33.7 KD PROTEIN IN LSP-PYRR INTERGENIC REGION (ORF-X)]









[SP:Q45480:O31732]


SPX2476
2476
5137
628
1884
461
1.70E-56
[GI:1914872]
88









[LN:SPZ82001]









[AC:Z82001]









[PN:PCPA]









[GN:pcpA]









[OR:Streptococcus pneumoniae]


SPX2477
2477
5138
377
1131
1387
4.40E-185
[LN:F81125]
107









[AC:F81125]









[PN:glutamate 5-kinase NMB1069 [imported]]









[GN:NMB1069]









[OR:Neisseria meningitidis]


SPX2478
2478
5139
421
1263
1530
1.10E-204
[GI:7413448]
130









[LN:AE002457]









[AC:AE002457:AE002098]









[PN:gamma-glutamyl phosphate reductase]









[GN:NMB1068]









[OR:Neisseria meningitidis]


SPX2479
2479
5140
266
798
396
3.30E-67
“[LN:PROC_ARATH]
176









[AC:P54904]









[GN:PROC1]









[OR:Arabidopsis thaliana]









[SR:,Mouse-ear cress]









[EC:1.5.1.2]









[DE:PYRROLINE-5-CARBOXYLATE REDUCTASE, (P5CR) (P5C REDUCTASE)]









[SP:P54904]”


SPX2480
2480
5141
213
639
528
4.30E-68
“[LN:KTHY_BACSU]
125









[AC:P37537]









[GN:TMK]









[OR:Bacillus subtilis]









[EC:2.7.4.9]









[DE:THYMIDYLATE KINASE, (DTMP KINASE)]









[SP:P37537]”


SPX2481
2481
5142
84
252


NO-HIT
6


SPX2482
2482
5143
297
891
244
4.80E-37
“[LN:HOLB_BACSU]
128









[AC:P37540]









[GN:HOLB]









[OR:Bacillus subtilis]









[EC:2.7.7.7]









[DE:DNA POLYMERASE III, DELTA′SUBUNIT,]









[SP:P37540]”


SPX2483
2483
5144
106
318
103
9.60E-09
[LN:YABA_BACSU]
137









[AC:P37542]









[GN:YABA]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 14.1 KD PROTEIN IN XPAC-ABRB INTERGENIC REGION]









[SP:P37542]


SPX2484
2484
5145
290
870
618
1.60E-84
[LN:YABC_BACSU]
137









[AC:P37544]









[GN:YABC]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 33.0 KD PROTEIN IN XPAC-ABRB INTERGENIC REGION]









[SP:P37544]


SPX2485
2485
5146
182
546
362
2.50E-61
[LN:S62019]
177









[AC:S62019]









[PN:hypothetical protein YDR540c:hypothetical protein D3703.8]









[GN:YDR540c]









[CL:Saccharomyces hypothetical protein YDR540c]









[OR:Saccharomyces cerevisiae]


SPX2486
2486
5147
168
504
82
2.90E-09
[GI:6690333]
102









[LN:AF117259]









[AC:AF117259]









[PN:replication protein]









[GN:repX]









[OR:Staphylococcus aureus]


SPX2487
2487
5148
150
450
400
5.20E-51
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX2488
2488
5149
134
402
370
1.00E-54
[LN:S52544]
71









[AC:S52544]









[PN:ISL2 protein]









[OR:Lactobacillus helveticus]


SPX2489
2489
5150
91
273


NO-HIT
6


SPX2490
2490
5151
445
1335
585
1.40E-196
[LN:GID_BACSU]
87









[AC:P39815]









[GN:GID]









[OR:Bacillus subtilis]









[DE:GID PROTEIN]









[SP:P39815]


SPX2491
2491
5152
246
738
793
2.20E-104
[LN:F69708]
120









[AC:F69708]









[PN:uridylate kinase smbA]









[GN:smbA]









[CL:uridine 5′-monophosphate kinase]









[OR:Bacillus subtilis]


SPX2492
2492
5153
146
438


NO-HIT
6


SPX2493
2493
5154
186
558
545
2.50E-69
[LN:G69626]
121









[AC:G69626]









[PN:ribosome recycling factor frr]









[GN:frr]









[CL:ribosome releasing factor]









[OR:Bacillus subtilis]


SPX2494
2494
5155
139
417


NO-HIT
6


SPX2495
2495
5156
285
855
180
3.70E-45
[GI:2145404]
71









[LN:BSY09476]









[AC:Y09476]









[PN:YitL]









[OR:Bacillus subtilis]


SPX2496
2496
5157
72
216
134
1.00E-13
[LN:A69931]
87









[AC:A69931]









[PN:hypothetical protein yozE]









[GN:yozE]









[OR:Bacillus subtilis]


SPX2497
2497
5158
323
969
956
1.30E-128
[LN:PHOL_BACSU]
95









[AC:P46343]









[GN:PHOH]









[OR:Bacillus subtilis]









[DE:PHOH-LIKE PROTEIN]









[SP:P46343]


SPX2498
2498
5159
65
195


NO-HIT
6


SPX2499
2499
5160
167
501
87
0.00031
[LN:E75272]
90









[AC:E75272]









[PN:hypothetical protein]









[GN:DR2441]









[OR:Deinococcus radiodurans]


SPX2500
2500
5161
92
276
253
1.30E-28
“[LN:DHA_BACSU]
151









[AC:Q08352]









[GN:ALD:SPOVN]









[OR:Bacillus subtilis]









[EC:1.4.1.1]









[DE:ALANINE DEHYDROGENASE, (STAGE V SPORULATION PROTEIN N)]









[SP:Q08352]”


SPX2501
2501
5162
65
195
168
5.10E-17
“[LN:JE0388]
152









[AC:JE0388]









[PN:alanine dehydrogenase,]









[CL:alanine dehydrogenase:alanine dehydrogenase homology]









[OR:Enterobacter aerogenes]









[EC:1.4.1.1]”


SPX2502
2502
5163
73
219
239
3.30E-27
“[LN:S74638]
233









[AC:S74638]









[PN:alanine dehydrogenase:hypothetical protein sll1682:hypothetical protein sll1682]









[CL:alanine dehydrogenase:alanine dehydrogenase homology]









[OR:Synechocystis sp.]









[SR:PCC 6803, , PCC 6803]









[SR:PCC 6803, ]”


SPX2503
2503
5164
142
426
405
2.90E-56
“[LN:DHA_BACSU]
151









[AC:Q08352]









[GN:ALD:SPOVN]









[OR:Bacillus subtilis]









[EC:1.4.1.1]









[DE:ALANINE DEHYDROGENASE, (STAGE V SPORULATION PROTEIN N)]









[SP:Q08352]”


SPX2504
2504
5165
196
588
147
8.00E-20
[LN:C69895]
170









[AC:C69895]









[PN:conserved hypothetical protein yoaA]









[GN:yoaA]









[CL:Escherichia coli ribosomal-protein-alanine N-acetyltransferase rimJ]









[OR:Bacillus subtilis]


SPX2505
2505
5166
217
651
1062
6.40E-138
[GI:3211753]
104









[LN:AF052208]









[AC:AF052208]









[PN:competence protein]









[GN:celA]









[OR:Streptococcus pneumoniae]


SPX2506
2506
5167
459
1377
2213
0
[GI:3211754]
104









[LN:AF052208]









[AC:AF052208]









[PN:competence protein]









[GN:celB]









[OR:Streptococcus pneumoniae]


SPX2507
2507
5168
306
918
1215
1.90E-162
[GI:3211754]
104









[LN:AF052208]









[AC:AF052208]









[PN:competence protein]









[GN:celB]









[OR:Streptococcus pneumoniae]


SPX2508
2508
5169
196
588
164
1.60E-26
[LN:YYBJ_BACSU]
95









[AC:P37494]









[GN:YYBJ]









[OR:Bacillus subtilis]









[DE:INTERGENIC REGION]









[SP:P37494]


SPX2509
2509
5170
392
1176


NO-HIT
6


SPX2510
2510
5171
88
264


NO-HIT
6


SPX2511
2511
5172
196
588
589
4.10E-77
[LN:IF3_LISMO]
116









[AC:O53084]









[GN:INFC]









[OR:Listeria monocytogenes]









[DE:TRANSLATION INITIATION FACTOR IF-3]









[SP:O53084]


SPX2512
2512
5173
67
201
235
1.10E-28
[LN:R5BS35]
137









[AC:S05347]









[PN:ribosomal protein L35]









[GN:rpmI]









[CL:Escherichia coli ribosomal protein L35]









[OR:Bacillus stearothermophilus]


SPX2513
2513
5174
120
360
476
9.30E-63
[LN:RL20_BACSU]
103









[AC:P55873]









[GN:RPLT]









[OR:Bacillus subtilis]









[DE:50S RIBOSOMAL PROTEIN L20]









[SP:P55873]


SPX2514
2514
5175
127
381
130
6.20E-24
[LN:LGUL_HAEIN]
147









[AC:P44638]









[GN:GLOA:HI0323]









[OR:Haemophilus influenzae]









[EC:4.4.1.5]









[DE:(S-D-LACTOYLGLUTATHIONE METHYLGLYOXAL LYASE)]









[SP:P44638]


SPX2515
2515
5176
190
570
354
2.10E-55
[LN:YLXD_BACCL]
139









[AC:P46536]









[OR:Bacillus caldolyticus]









[DE:HYPOTHETICAL 27.6 KD PROTEIN IN PYRAB-PYRD INTERGENIC REGION (ORF2)]









[SP:P46536]


SPX2516
2516
5177
94
282
172
7.70E-23
[LN:YLXD_BACCL]
139









[AC:P46536]









[OR:Bacillus caldolyticus]









[DE:HYPOTHETICAL 27.6 KD PROTEIN IN PYRAB-PYRD INTERGENIC REGION (ORF2)]









[SP:P46536]


SPX2517
2517
5178
313
939
563
8.20E-147
“[LN:PYDB_LACLC]
159









[AC:P54322]









[GN:PYRDB]









[OR:Lactococcus lactis]









[SR:,subspcremoris:Streptococcus cremoris]









[EC:1.3.3.1]









[DE:(DHODEHASE B) (DHODB)]









[SP:P54322]”


SPX2518
2518
5179
722
2166
2390
0
[GI:4218533]
167









[LN:SPN010312]









[AC:AJ010312]









[PN:endo-beta-N-acetylglucosaminidase]









[GN:lytB]









[FN:cell wall degradation and cell separation]









[OR:Streptococcus pneumoniae]


SPX2519
2519
5180
561
1683
2767
0
[GI:6175915]
132









[LN:AF181976]









[AC:AF181976]









[PN:adherence and virulence protein A]









[GN:pavA]









[FN:adhesin]









[OR:Streptococcus pneumoniae]


SPX2520
2520
5181
77
231


NO-HIT
6


SPX2521
2521
5182
166
498
705
5.20E-92
[GI:2749950]
66









[LN:AF000954]









[AC:AF000954]









[OR:Streptococcus mutans]


SPX2522
2522
5183
132
396
507
6.90E-71
[LN:A36933]
134









[AC:A36933]









[PN:diacylglycerol kinase homolog]









[CL:Bacillus subtilis diacylglycerol kinase dgkA]









[OR:Streptococcus mutans]


SPX2523
2523
5184
300
900
1502
1.40E-204
[GI:5305399]
95









[LN:AF072811]









[AC:AF072811]









[PN:GTPase Era]









[GN:era]









[OR:Streptococcus pneumoniae]


SPX2524
2524
5185
275
825
892
1.90E-119
[LN:FPG_STRMU]
110









[AC:P55045]









[GN:MUTM:FPG]









[OR:Streptococcus mutans]









[EC:3.2.2.23]









[DE:GLYCOSYLASE)]









[SP:P55045]


SPX2525
2525
5186
61
183


NO-HIT
6


SPX2526
2526
5187
203
609
167
2.40E-32
“[LN:Y553_SYNY3]
140









[AC:Q55515]









[GN:SLR0553]









[OR:Synechocystis sp]









[SR:,strain PCC 6803]









[DE:HYPOTHETICAL 22.5 KD PROTEIN SLR0553]









[SP:Q55515]”


SPX2527
2527
5188
67
201


NO-HIT
6


SPX2528
2528
5189
400
1200
1989
9.60E-280
[GI:3820455]
118









[LN:SPN7367]









[AC:AJ007367]









[PN:multi-drug resistance efflux pump]









[GN:pmrA]









[OR:Streptococcus pneumoniae]


SPX2529
2529
5190
50
150
177
8.70E-20
“[LN:RL33_LACLA]
145









[AC:P27167]









[GN:RPMG]









[OR:Lactococcus lactis]









[SR:,subsplactis:Streptococcus lactis]









[DE:50S RIBOSOMAL PROTEIN L33]









[SP:P27167]”


SPX2530
2530
5191
78
234
82
8.20E-06
[LN:A70028]
120









[AC:A70028]









[PN:hypothetical protein yvaL]









[GN:yvaL]









[CL:protein-export protein secG]









[OR:Bacillus subtilis]


SPX2531
2531
5192
785
2355
564
4.00E-180
[LN:G70027]
144









[AC:G70027]









[PN:conserved hypothetical protein yvaJ]









[GN:yvaJ]









[CL:virulence-associated protein vacB homolog]









[OR:Bacillus subtilis]


SPX2532
2532
5193
156
468
793
1.30E-104
[GI:3211758]
88









[LN:AF052209]









[AC:AF052209]









[PN:VacB homolog]









[OR:Streptococcus pneumoniae]


SPX2533
2533
5194
287
861
1499
8.30E-203
[GI:4883699]
119









[LN:AF079807]









[AC:AF079807]









[PN:tellurite resistance protein TehB]









[GN:tehB]









[OR:Streptococcus pneumoniae]


SPX2534
2534
5195
129
387
326
5.30E-41
[GI:3211758]
88









[LN:AF052209]









[AC:AF052209]









[PN:VacB homolog]









[OR:Streptococcus pneumoniae]


SPX2535
2535
5196
74
222


NO-HIT
6


SPX2536
2536
5197
318
954
800
5.10E-182
[GI:3211759]
104









[LN:AF052209]









[AC:AF052209]









[PN:competence protein]









[GN:coiA]









[OR:Streptococcus pneumoniae]


SPX2537
2537
5198
601
1803
2159
2.10E-292
“[LN:PEPB_STRAG]
129









[AC:Q53778]









[GN:PEPB]









[OR:Streptococcus agalactiae]









[EC:3.4.24.-]









[DE:GROUP B OLIGOPEPTIDASE PEPB,]









[SP:Q53778]”


SPX2538
2538
5199
238
714
680
4.90E-90
[GI:1771204]
86









[LN:LLLVSFPEP]









[AC:X99710]









[PN:methyltransferase]









[OR:Lactococcus lactis]


SPX2539
2539
5200
314
942
189
3.10E-32
[LN:PRTM_LACPA]
121









[AC:Q02473]









[GN:PRTM]









[OR:Lactobacillus paracasei]









[DE:PROTEASE MATURATION PROTEIN PRECURSOR]









[SP:Q02473]


SPX2540
2540
5201
114
342
567
4.00E-74
[GI:1490399]
90









[LN:SPPARCETP]









[AC:Z67739]









[PN:DNA transposase]









[OR:Streptococcus pneumoniae]


SPX2541
2541
5202
191
573
422
2.30E-53
[LN:B30868]
81









[AC:B30868]









[PN:hypothetical protein 1]









[OR:Streptococcus agalactiae]


SPX2542
2542
5203
91
273


NO-HIT
6


SPX2543
2543
5204
64
192


NO-HIT
6


SPX2544
2544
5205
207
621
86
4.90E-12
“[LN:T46083]
190









[AC:T46083]









[PN:hypothetical protein T20E23.120]









[CL:Aquifex aeolicus phosphoglycerate mutase:phosphoglycerate mutase homology]









[OR:Arabidopsis thaliana]









[SR:, mouse-ear cress]”


SPX2545
2545
5206
161
483
210
1.70E-35
“[LN:EBSC_ENTFA]
115









[AC:P36922]









[OR:Enterococcus faecalis]









[SR:,Streptococcus faecalis]









[DE:EBSC PROTEIN]









[SP:P36922]”


SPX2546
2546
5207
281
843
128
6.60E-17
[LN:B72411]
96









[AC:B72411]









[PN:conserved hypothetical protein]









[GN:TM0164]









[OR:Thermotoga maritima]


SPX2547
2547
5208
263
789
102
2.10E-09
[GI:1865711]
116









[LN:BPPLYBA]









[AC:Y11477]









[PN:endolysin]









[GN:plyBa]









[FN:cell wall hydrolase]









[OR:Bacteriophage Bastille]


SPX2548
2548
5209
460
1380
1180
1.90E-156
[LN:S66080]
237









[AC:S66080:I40018:C69629:S05371:S18903]









[PN:UDP-N-acetylglucosamine pyrophosphorylase gcaD:cell division protein tms26:tms protein]









[GN:gcaD:tms26]









[CL:N-acetylglucosamine-1-phosphate uridyltransferase]









[OR:Bacillus subtilis]


SPX2549
2549
5210
182
546
167
2.40E-45
[LN:YQKG_BACSU]
137









[AC:P54570]









[GN:YQKG]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 21.0 KD PROTEIN IN GLNQ-ANSR INTERGENIC REGION]









[SP:P54570]


SPX2550
2550
5211
105
315


NO-HIT
6


SPX2551
2551
5212
231
693
477
1.60E-61
[LN:PFS_ECOLI]
110









[AC:P24247]









[GN:PFS]









[OR:Escherichia coli]









[EC:3.2.2.16:3.2.2.9]









[DE:(EC 3.2.2.9)]]









[SP:P24247]


SPX2552
2552
5213
164
492
124
1.90E-12
[GI:2769573]
79









[LN:LLCPJW565]









[AC:Y12736]









[OR:Lactococcus lactis subsp. cremoris]


SPX2553
2553
5214
197
591
137
1.00E-08
“[LN:DPO3_BACSU]
154









[AC:P13267]









[GN:POLC:DNAF:MUTI]









[OR:Bacillus subtilis]









[EC:2.7.7.7]









[DE:DNA POLYMERASE III, ALPHA CHAIN POLC-TYPE, (POLIII)]









[SP:P13267]”


SPX2554
2554
5215
257
771
105
1.40E-11
[LN:E69827]
159









[AC:E69827]









[PN:glycerophosphodiester phosphodiesterase homolog yhdW]









[GN:yhdW]









[CL:glycerophosphodiester phosphodiesterase]









[OR:Bacillus subtilis]


SPX2555
2555
5216
116
348
577
5.80E-76
[GI:4200438]
96









[LN:AF026471]









[AC:AF026471]









[PN:putative transposase]









[OR:Streptococcus pneumoniae]


SPX2556
2556
5217
47
141
186
5.40E-22
[GI:5019553]
97









[LN:SPN239004]









[AC:AJ239004]









[PN:putative transposase]









[OR:Streptococcus pneumoniae]


SPX2557
2557
5218
67
201


NO-HIT
6


SPX2558
2558
5219
211
633


NO-HIT
6


SPX2559
2559
5220
100
300
84
0.00082
[GI:1707287]
148









[LN:BBU80959]









[AC:U80959:L78251]









[PN:putative outer membrane protein]









[GN:ospFi]









[OR:Borrelia burgdorferi]









[SR:Lyme disease spirochete]


SPX2560
2560
5221
236
708
267
1.40E-53
[LN:YE54_HAEIN]
141









[AC:P44202]









[GN:HI1454]









[OR:Haemophilus influenzae]









[DE:HYPOTHETICAL CYTOCHROME C-TYPE BIOGENESIS PROTEIN HI1454]









[SP:P44202]


SPX2561
2561
5222
186
558
239
6.40E-28
[LN:YE53_HAEIN]
136









[AC:Q57127:O05062]









[GN:HI1453]









[OR:Haemophilus influenzae]









[DE:HYPOTHETICAL PROTEIN HI1453 PRECURSOR]









[SP:Q57127:O05062]


SPX2562
2562
5223
464
1392
481
1.60E-122
[LN:D69814]
120









[AC:D69814]









[PN:metabolite transporter homolog yfnA]









[GN:yfnA]









[CL:arginine permease]









[OR:Bacillus subtilis]


SPX2563
2563
5224
308
924
985
7.10E-129
[LN:T46757]
95









[AC:T46757]









[PN:lipoprotein lmb [validated]]









[GN:lmb]









[OR:Streptococcus agalactiae]


SPX2564
2564
5225
839
2517
409
3.50E-104
[LN:T46758]
90









[AC:T46758]









[PN:hypothetical protein [imported]]









[OR:Streptococcus agalactiae]


SPX2565
2565
5226
1040
3120
400
1.50E-93
[LN:T46758]
90









[AC:T46758]









[PN:hypothetical protein [imported]]









[OR:Streptococcus agalactiae]


SPX2566
2566
5227
63
189


NO-HIT
6


SPX2567
2567
5228
63
189
240
1.40E-26
[LN:T46758]
90









[AC:T46758]









[PN:hypothetical protein [imported]]









[OR:Streptococcus agalactiae]


SPX2568
2568
5229
67
201
104
3.80E-14
[LN:T46758]
90









[AC:T46758]









[PN:hypothetical protein [imported]]









[OR:Streptococcus agalactiae]


SPX2569
2569
5230
161
483
152
4.70E-20
[LN:T46758]
90









[AC:T46758]









[PN:hypothetical protein [imported]]









[OR:Streptococcus agalactiae]


SPX2570
2570
5231
80
240


NO-HIT
6


SPX2571
2571
5232
86
258


NO-HIT
6


SPX2572
2572
5233
145
435
107
6.20E-05
[GI:7228476]
121









[LN:AF163151]









[AC:AF163151]









[PN:dentin sialophosphoprotein precursor]









[GN:DSPP]









[OR:Homo sapiens]









[SR:human]


SPX2573
2573
5234
408
1224
961
7.20E-190
“[LN:PEPT_LACLC]
185









[AC:P42020]









[GN:PEPT]









[OR:Lactococcus lactis]









[SR:,subspcremoris:Streptococcus cremoris]









[EC:3.4.11.-]









[DE:PEPTIDASE T, (AMINOTRIPEPTIDASE) (TRIPEPTIDASE)]









[SP:P42020]”


SPX2574
2574
5235
365
1095
215
4.70E-41
[LN:HEMZ_BACSU]
108









[AC:P32396]









[GN:HEMH:HEMF]









[OR:Bacillus subtilis]









[EC:4.99.1.1]









[DE:SYNTHETASE)]









[SP:P32396]


SPX2575
2575
5236
126
378
149
2.80E-25
[GI:6136300]
90









[LN:AF065159]









[AC:AF065159]









[PN:MscL]









[GN:mscL]









[OR:Bradyrhizobium japonicum]


SPX2576
2576
5237
87
261


NO-HIT
6


SPX2577
2577
5238
129
387
180
3.60E-29
“[LN:T44787]
136









[AC:T44787]









[PN:glucokinase, [imported]]









[CL:glucose kinase:glucose kinase homology]









[OR:Bacillus megaterium]









[EC:2.7.1.2]”


SPX2578
2578
5239
88
264
61
0.0009
[GI:2897104]
145









[LN:AF020798]









[AC:AF020798]









[PN:putative host cell surface-exposed lipoprotein]









[OR:Streptococcus thermophilus bacteriophage TP-J34]


SPX2579
2579
5240
273
819
279
1.60E-30
“[GI:4218526]
153









[LN:SPAJ9639]









[AC:AJ009639]









[PN:1,4-beta-N-acetylmuramidase]









[GN:lytC]









[FN:lysis of cell wall peptidoglycan]









[OR:Streptococcus pneumoniae]”


SPX2580
2580
5241
510
1530
289
6.20E-30
“[GI:4218526]
153









[LN:SPAJ9639]









[AC:AJ009639]









[PN:1,4-beta-N-acetylmuramidase]









[GN:lytC]









[FN:lysis of cell wall peptidoglycan]









[OR:Streptococcus pneumoniae]”


SPX2581
2581
5242
574
1722
339
6.40E-76
“[LN:A71951]
140









[AC:A71951]









[PN:p-aminobenzoate synthetase]









[GN:pabB]









[OR:Helicobacter pylori]









[SR:strain J99, , strain J99]









[SR:strain J99, ]”


SPX2582
2582
5243
1964
5892
7027
0
[GI:6911257]
115









[LN:AF221126]









[AC:AF221126]









[PN:putative zinc metalloprotease]









[GN:zmpB]









[OR:Streptococcus pneumoniae]


SPX2583
2583
5244
78
234


NO-HIT
6


SPX2584
2584
5245
108
324
71
7.10E-06
[GI:501027]
97









[LN:TBU01849]









[AC:U01849]









[OR:Kinetoplast Trypanosoma brucei]









[SR:Trypanosoma brucei]


SPX2585
2585
5246
188
564
392
1.60E-49
[LN:YWLG_BACSU]
147









[AC:P39157]









[GN:YWLG:IPC-33D]









[OR:Bacillus subtilis]









[DE:HYPOTHETICAL 19.4 KD PROTEIN IN SPOIIR-GLYC INTERGENIC REGION]









[SP:P39157]


SPX2586
2586
5247
378
1134
1862
7.80E-253
[GI:6911256]
111









[LN:AF221126]









[AC:AF221126]









[PN:putative histidine kinase]









[GN:zmpS]









[OR:Streptococcus pneumoniae]


SPX2587
2587
5248
63
189


NO-HIT
6


SPX2588
2588
5249
186
558
898
5.90E-119
[GI:6911256]
111









[LN:AF221126]









[AC:AF221126]









[PN:putative histidine kinase]









[GN:zmpS]









[OR:Streptococcus pneumoniae]


SPX2589
2589
5250
246
738
1237
2.00E-167
[GI:6911255]
113









[LN:AF221126]









[AC:AF221126]









[PN:putative response regulator]









[GN:zmpR]









[OR:Streptococcus pneumoniae]


SPX2590
2590
5251
371
1113
1110
1.40E-147
[LN:YE55_HAEIN]
112









[AC:P45213]









[GN:HI1455]









[OR:Haemophilus influenzae]









[DE:HYPOTHETICAL PROTEIN HI1455]









[SP:P45213]


SPX2591
2591
5252
198
594
335
9.20E-41
[LN:YE53_HAEIN]
136









[AC:Q57127:O05062]









[GN:HI1453]









[OR:Haemophilus influenzae]









[DE:HYPOTHETICAL PROTEIN HI1453 PRECURSOR]









[SP:Q57127:O05062]


SPX2592
2592
5253
237
711
139
3.50E-49
[LN:YE54_HAEIN]
141









[AC:P44202]









[GN:HI1454]









[OR:Haemophilus influenzae]









[DE:HYPOTHETICAL CYTOCHROME C-TYPE BIOGENESIS PROTEIN HI1454]









[SP:P44202]


SPX2593
2593
5254
287
861
312
4.30E-47
[GI:3608389]
79









[LN:AF071085]









[AC:AF071085]









[PN:Orfde2]









[OR:Enterococcus faecalis]


SPX2594
2594
5255
685
2055
564
1.00E-82
[LN:E70040]
128









[AC:E70040]









[PN:conserved hypothetical protein yvgP]









[GN:yvgP]









[CL:hypothetical protein yvgP]









[OR:Bacillus subtilis]


SPX2595
2595
5256
64
192


NO-HIT
6


SPX2596
2596
5257
85
255


NO-HIT
6


SPX2597
2597
5258
63
189


NO-HIT
6


SPX2598
2598
5259
188
564
221
1.00E-42
[LN:E69999]
87









[AC:E69999]









[PN:hypothetical protein ytqB]









[GN:ytqB]









[OR:Bacillus subtilis]


SPX2599
2599
5260
149
447
329
6.50E-47
[LN:D69999]
165









[AC:D69999]









[PN:conserved hypothetical protein ytqA]









[GN:ytqA]









[CL:Methanococcus jannaschii conserved hypothetical protein MJ0486]









[OR:Bacillus subtilis]


SPX2600
2600
5261
84
252
209
2.10E-24
[LN:D69999]
165









[AC:D69999]









[PN:conserved hypothetical protein ytqA]









[GN:ytqA]









[CL:Methanococcus jannaschii conserved hypothetical protein MJ0486]









[OR:Bacillus subtilis]


SPX2601
2601
5262
146
438
210
2.60E-23
[LN:D69999]
165









[AC:D69999]









[PN:conserved hypothetical protein ytqA]









[GN:ytqA]









[CL:Methanococcus jannaschii conserved hypothetical protein MJ0486]









[OR:Bacillus subtilis]


SPX2602
2602
5263
120
360


NO-HIT
6


SPX2603
2603
5264
82
246
182
1.20E-19
[GI:1022726]
129









[LN:SHU35635]









[AC:U35635]









[PN:unknown]









[OR:Staphylococcus haemolyticus]









[SR:Staphylococcus haemolyticus strain=Y176]


SPX2604
2604
5265
208
624
156
1.10E-37
“[GI:6332767]
194









[LN:AB033763]









[AC:AB033763:AB014419:AB014429:AB014439]









[PN:hypothetical protein]









[OR:Staphylococcus aureus]









[SR:Staphylococcus aureus (strain:NCTC10442) DNA, clone_lib:Lambda das]”


SPX2605
2605
5266
2173
6519
309
2.70E-130
[GI:6468240]
129









[LN:SCF81]









[AC:AL133171]









[PN:putative secreted beta-galactosidase]









[GN:SCF81.25c]









[OR:Streptomyces coelicolor A3(2)]


SPX2606
2606
5267
62
186


NO-HIT
6


SPX2607
2607
5268
64
192


NO-HIT
6


SPX2608
2608
5269
144
432
184
6.10E-21
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX2609
2609
5270
262
786
92
2.70E-11
“[LN:SGCC_ECOLI]
134









[AC:P39365]









[GN:SGCC]









[OR:Escherichia coli]









[DE:PUTATIVE PHOSPHOTRANSFERASE ENZYME II, C COMPONENT SGCC]









[SP:P39365]”


SPX2610
2610
5271
231
693
231
3.70E-25
“[GI:1736815]
201









[LN:D90848]









[AC:D90848:AB001340]









[PN:PTS system, Galactitol-specific IIC component]









[GN:gatC]









[OR:Escherichia coli]









[SR:Escherichia coli (strain:K12) DNA, clone_lib:Kohara lambda minise]”


SPX2611
2611
5272
102
306


NO-HIT
6


SPX2612
2612
5273
159
477
95
5.10E-13
“[GI:4512375]
181









[LN:AB011837]









[AC:AB011837]









[PN:phosphotransferase system (PTS)]









[GN:fruA]









[OR:Bacillus halodurans]









[SR:Bacillus halodurans (strain:C-125) DNA, clone_lib:lambda no.9]”


SPX2613
2613
5274
2139
6417
10556
0
[GI:5726291]
134









[LN:AF127143]









[AC:AF127143]









[PN:cell wall-associated serine proteinase precursor]









[GN:prtA]









[OR:Streptococcus pneumoniae]


SPX2614
2614
5275
68
204
136
2.70E-14
[LN:T30285]
79









[AC:T30285]









[PN:hypothetical protein]









[OR:Streptococcus pneumoniae]


SPX2615
2615
5276
66
198


NO-HIT
6


SPX2616
2616
5277
262
786
107
2.30E-18
[GI:7635999]
136









[LN:SCE6]









[AC:AL353832]









[PN:putative integral membrane transport protein.]









[GN:SCE6.32c]









[OR:Streptomyces coelicolor A3(2)]


SPX2617
2617
5278
287
861
113
2.80E-10
[GI:7636000]
126









[LN:SCE6]









[AC:AL353832]









[PN:putative integral membrane protein.]









[GN:SCE6.33c]









[OR:Streptomyces coelicolor A3(2)]


SPX2618
2618
5279
318
954
601
1.60E-83
“[LN:G75548]
184









[AC:G75548]









[PN:ABC transporter, ATP-binding protein]









[GN:DR0205]









[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]









[OR:Deinococcus radiodurans]”


SPX2619
2619
5280
83
249


NO-HIT
6


SPX2620
2620
5281
132
396


NO-HIT
6


SPX2621
2621
5282
158
474
123
3.70E-11
[GI:1914870]
81









[LN:SPZ82001]









[AC:Z82001]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX2622
2622
5283
230
690
765
9.20E-100
[LN:RL1_BACST]
111









[AC:P04447]









[GN:RPLA]









[OR:Bacillus stearothermophilus]









[DE:50S RIBOSOMAL PROTEIN L1]









[SP:P04447]


SPX2623
2623
5284
142
426
596
4.50E-77
[LN:S38871]
133









[AC:S38871]









[PN:ribosomal protein L11]









[GN:rplK]









[CL:Escherichia coli ribosomal protein L11]









[OR:Staphylococcus carnosus]


SPX2624
2624
5285
75
225


NO-HIT
6


SPX2625
2625
5286
239
717
133
3.00E-20
[GI:2529473]
96









[LN:AF006665]









[AC:AF006665]









[PN:YokZ]









[GN:yokZ]









[FN:unknown]









[OR:Bacillus subtilis]


SPX2626
2626
5287
60
180


NO-HIT
6


SPX2627
2627
5288
170
510
103
7.80E-07
[LN:A81062]
119









[AC:A81062]









[PN:conserved hypothetical protein NMB1619 [imported]]









[GN:NMB1619]









[OR:Neisseria meningitidis]


SPX2628
2628
5289
72
216
187
1.80E-19
[LN:B71121]
142









[AC:B71121]









[PN:hypothetical protein PH0737]









[GN:PH0737]









[CL:thermophilic aminopeptidase I alpha chain]









[OR:Pyrococcus horikoshii]


SPX2629
2629
5290
199
597
306
4.10E-72
[LN:C69830]
131









[AC:C69830]









[PN:glucanase homolog yhfE]









[GN:yhfE]









[CL:thermophilic aminopeptidase I alpha chain]









[OR:Bacillus subtilis]


SPX2630
2630
5291
114
342
145
6.70E-14
[GI:2315995]
112









[LN:SAU87144]









[AC:U87144]









[PN:branched-chain amino acid carrier protein]









[OR:Staphylococcus aureus]


SPX2631
2631
5292
447
1341
391
6.60E-90
[LN:BRNQ_BACSU]
124









[AC:P94499:O07082]









[GN:BRNQ]









[OR:Bacillus subtilis]









[DE:CHAIN AMINO ACID UPTAKE CARRIER)]









[SP:P94499:O07082]


SPX2632
2632
5293
63
189
88
3.10E-06
“[LN:YC61_SYNY3]
140









[AC:P73801]









[GN:SLR1261]









[OR:Synechocystis sp]









[SR:,strain PCC 6803]









[DE:HYPOTHETICAL 19.1 KD PROTEIN SLR1261]









[SP:P73801]”


SPX2633
2633
5294
80
240
100
1.90E-17
[GI:1914870]
81









[LN:SPZ82001]









[AC:Z82001]









[PN:unknown]









[OR:Streptococcus pneumoniae]


SPX2634
2634
5295
193
579
548
7.70E-95
[GI:3212185]
140









[LN:U32707]









[AC:U32707:L42023]









[PN:H. influenzae predicted coding region HI0220.2]









[GN:HI0220.2]









[OR:Haemophilus influenzae Rd]


SPX2635
2635
5296
467
1401
646
4.20E-200
[GI:2160707]
79









[LN:LLU78036]









[AC:U78036]









[PN:dipeptidase]









[OR:Lactococcus lactis]


SPX2636
2636
5297
202
606
113
2.60E-17
“[LN:NOX_THETH]
158









[AC:Q60049:Q53306]









[GN:NOX]









[OR:Thermus aquaticus]









[SR:,subspthermophilus]









[EC:1.6.99.3]









[DE:(NADH:OXYGEN OXIDOREDUCTASE)]









[SP:Q60049:Q53306]”


SPX2637
2637
5298
80
240


NO-HIT
6


SPX2638
2638
5299
267
801
141
2.90E-22
[GI:2108229]
121









[LN:LFU97348]









[AC:U97348]









[PN:basic surface protein]









[FN:L-cystine transporter]









[OR:Lactobacillus fermentum]


SPX2639
2639
5300
278
834
106
6.20E-12
[LN:G75297]
167









[AC:G75297]









[PN:conserved hypothetical protein]









[GN:DR2233]









[CL:probable phosphoesterase MJ0912:phosphoesterase core homology]









[OR:Deinococcus radiodurans]


SPX2640
2640
5301
615
1845
1882
5.00E-256
[LN:UVRC_BACSU]
104









[AC:P14951]









[GN:UVRC]









[OR:Bacillus subtilis]









[DE:EXCINUCLEASE ABC SUBUNIT C]









[SP:P14951]


SPX2641
2641
5302
241
723


NO-HIT
6


SPX2642
2642
5303
411
1233
95
3.90E-07
[LN:SPN250764]
120









[AC:AJ250764]









[PN:MurM protein]









[GN:murM]









[FN:serine/alanine adding enzyme]









[OR:Streptococcus pneumoniae]


SPX2643
2643
5304
407
1221
2088
3.50E-283
[LN:SPN277484]
152









[AC:AJ277484]









[PN:beta-lactam resistance factor]









[GN:fibA]









[FN:putative role in peptidoglycan crosslinking]









[OR:Streptococcus pneumoniae]


SPX2644
2644
5305
260
780
482
7.10E-100
[GI:7453516]
113









[LN:AF157484]









[AC:AF157484]









[PN:tributyrin esterase]









[GN:estA]









[OR:Lactococcus lactis subsp. lactis]


SPX2645
2645
5306
554
1662
581
1.80E-136
[LN:H69884]
139









[AC:H69884]









[PN:conserved hypothetical protein ymfA]









[GN:ymfA]









[CL:conserved hypothetical protein MG139]









[OR:Bacillus subtilis]


SPX2646
2646
5307
647
1941
529
3.20E-120
[LN:H69980]
113









[AC:H69980]









[PN:single-strand DNA-specific exonuclease homolog yrvE]









[GN:yrvE]









[OR:Bacillus subtilis]


SPX2647
2647
5308
741
2223
529
8.40E-150
[LN:H69980]
113









[AC:H69980]









[PN:single-strand DNA-specific exonuclease homolog yrvE]









[GN:yrvE]









[OR:Bacillus subtilis]


SPX2648
2648
5309
253
759
527
8.90E-103
[LN:GLNQ_BACST]
132









[AC:P27675]









[GN:GLNQ]









[OR:Bacillus stearothermophilus]









[DE:GLUTAMINE TRANSPORT ATP-BINDING PROTEIN GLNQ]









[SP:P27675]


SPX2649
2649
5310
65
195
69
0.00063
[LN:E72756]
92









[AC:E72756]









[PN:hypothetical protein APE0042]









[GN:APE0042]









[OR:Aeropyrum pernix]


SPX2650
2650
5311
73
219
92
9.10E-12
[LN:G72510]
92









[AC:G72510]









[PN:hypothetical protein APE2061]









[GN:APE2061]









[OR:Aeropyrum pernix]


SPX2651
2651
5312
265
795
422
2.40E-66
[LN:PEB1_CAMJE]
131









[AC:P45678]









[GN:PEB1A]









[OR:Campylobacter jejuni]









[DE:MAJOR CELL-BINDING FACTOR PRECURSOR (CBF1) (PEB1)]









[SP:P45678]


SPX2652
2652
5313
226
678
400
3.80E-74
[LN:G81365]
144









[AC:G81365]









[PN:probable ABC-type amino-acid transporter permease protein Cj0920c [imported]]









[GN:Cj0920c]









[OR:Campylobacter jejuni]


SPX2653
2653
5314
220
660
234
2.00E-50
[LN:F69633]
145









[AC:F69633]









[PN:glutamine ABC transporter (membrane protein) glnP]









[GN:glnP]









[CL:histidine permease protein M]









[OR:Bacillus subtilis]


SPX2654
2654
5315
401
1203
78
7.00E-08
[GI:1255667]
136









[LN:PSEORF1]









[AC:D84146]









[PN:reductase]









[GN:pahA]









[OR:Pseudomonas aeruginosa]









[SR:Pseudomonas aeruginosa (strain:PaK1) DNA]


SPX2655
2655
5316
294
882
1498
3.00E-201
“[LN:ALF_STRPN]
130









[AC:O65944]









[GN:FBA]









[OR:Streptococcus pneumoniae]









[EC:4.1.2.13]









[DE:FRUCTOSE-BISPHOSPHATE ALDOLASE,]









[SP:O65944]”


SPX2656
2656
5317
443
1329
2174
1.90E-297
[GI:4583524]
133









[LN:AF140356]









[AC:AF140356]









[PN:VncS]









[GN:vncS]









[FN:putative histidine kinase/phosphatase]









[OR:Streptococcus pneumoniae]


SPX2657
2657
5318
219
657
1089
1.00E-146
[GI:4583523]
123









[LN:AF140356]









[AC:AF140356]









[PN:VncR]









[GN:vncR]









[FN:putative response regulator]









[OR:Streptococcus pneumoniae]


SPX2658
2658
5319
460
1380
2273
0
[GI:5712669]
91









[LN:AF140784]









[AC:AF140784]









[PN:Vexp3]









[GN:vex3]









[OR:Streptococcus pneumoniae]


SPX2659
2659
5320
216
648
1066
2.30E-141
[GI:5712668]
91









[LN:AF140784]









[AC:AF140784]









[PN:Vexp2]









[GN:vex2]









[OR:Streptococcus pneumoniae]


SPX2660
2660
5321
426
1278
2070
2.40E-280
[GI:5712667]
91









[LN:AF140784]









[AC:AF140784]









[PN:Vexp1]









[GN:vex1]









[OR:Streptococcus pneumoniae]


SPX2661
2661
5322
85
255


NO-HIT
6

## Claims

1. An isolated nucleic acid encoding a S. pneumoniae polypeptide comprising SEQ ID NO: 5137.

2. An isolated nucleic acid sequence comprising SEQ ID NO: 2476.

3. An isolated nucleic acid sequence selected from the group consisting of:
a) SEQ ID NO: 2476,
b) a nucleic acid sequence fully complementary to SEQ ID NO: 2476, and
c) an RNA of a) or b) wherein U is substituted for T.

4. A recombinant expression vector comprising the nucleic acid of claim 1 operably linked to a transcription regulatory element.

5. A recombinant expression vector comprising the nucleic acid of claim 2 operably linked to a transcription regulatory element.

6. A cell comprising the recombinant expression vector of claim 4.

7. A cell comprising the recombinant expression vector of claim 5.

8. A recombinant expression vector comprising the nucleic acid of claim 3 operably linked to a transcription regulatory element.

9. A cell comprising the recombinant expression vector of claim 8.