lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the translocation and assembly module (TAM), which facilitates the insertion and assembly of specific beta-barrel proteins into the outer membrane. Promotes the assembly and secretion across the outer membrane of a subset of autotransporters, such as Ag43. Involved in the assembly of the outer membrane usher protein FimD. In vitro, when TAM is reconstituted into preformed liposomes, it can promote the assembly of several outer membrane proteins, including OmpA, EspP, Ag43 and FadL. TamA is sufficient to catalyze a low level of outer membrane protein (OMP) assembly, but both TamA and TamB are required for efficient OMP assembly. TamA must bind to the beta signal of client proteins to promote their assembly. Has anion selective channel-forming ability, but the physiological relevance of this activity is unclear.
Subcellular Localization:
Cell outer membrane.
Domain:
Contains 3 N-terminal periplasmic polypeptide transport-associated (POTRA) domains and a C-terminal 16-stranded beta-barrel transmembrane region. The 3 POTRA domains seem to form a rigid body (unlike BamA where the 5 POTRA domains are able to move independently). Upon substrate binding (Ag43, AC P39180) the 3 POTRA domains move away from the inner surface of the outer membrane by about 30 Angstroms, which would deform either the outer membrane or TamB and may provide force to reset TAM. POTRA1 is required for interaction with TamB. Deletion of POTRA1 decreases Ag43 binding to this protein, whereas deletion of POTRA1 and 2 obviates binding to Ag43. The beta-barrel is closed on the extracellular face by loop 6 (residues 456-495), while the C-terminal beta-strand forms an inward kink which may act as a gate for substrate access from the periplasm. This kink weakens the beta-strand pair between the first and last strands which may contribute to gating and substrate translocation; Possesses a dynamic lateral gate, which may provide a different environment for substrate engagement when compared to BamA, explaining how TAM may be more effective than the BAM complex in the folding of certain substrate proteins.
Sequence:
MRYIRQLCCVSLLCLSGSAVAANVRLQVEGLSGQLEKNVRAQLSTIESDEVTPDRRFRARVDDAIREGLKALGYYQPTIEFDLRPPPKKGRQVLIAKVTPGVPVLIGGTDVVLRGGARTDKDYLKLLDTRPAIGTVLNQGDYENFKKSLTSIALRKGYFDSEFTKAQLGIALGLHKAFWDIDYNSGERYRFGHVTFEGSQIRDEYLQNLVPFKEGDEYESKDLAELNRRLSATGWFNSVVVAPQFDKARETKVLPLTGVVSPRTENTIETGVGYSTDVGPRVKATWKKPWMNSYGHSLTTSTSISAPEQTLDFSYKMPLLKNPLEQYYLVQGGFKRTDLNDTESDSTTLVASRYWDLSSGWQRAINLRWSLDHFTQGEITNTTMLFYPGVMISRTRSRGGLMPTWGDSQRYSIDYSNTAWGSDVDFSVFQAQNVWIRTLYDRHRFVTRGTLGWIETGDFDKVPPDLRFFAGGDRSIRGYKYKSIAPKYANGDLKGASKLITGSLEYQYNVTGKWWGAVFVDSGEAVSDIRRSDFKTGTGVGVRWESPVGPIKLDFAVPVADKDEHGLQFYIGLGPEL
The following text describes a protein:
Function:
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MADQSPADQTPPSSGMQSLSVDSQPPSSSSTPQMSLEEKFKIIRSVGEECIQEDELLNLLNHKPEPICYDGFEPSGRMHIAQGVMKAINVNKLTSAGCRVKIWIADWFAQLNNKMGGDLKKIKVVGQYLIEIWKAVGMDLNEKVEFLWSSDEINSRASEYWPLVMDIARRNKLPRIMRCCQIMGRSEQDELSAAQILYPCMQCADIFFLKADICQLGMDQRKVNVLAREYCVDIKRKNKPIILSHHMLPGLQQGQEKMSKSDPSSSIFMEDEEAEVNVKIKKAYCPPKIVKGNPCLEYIKYIIFPWFNEFRVERNADNGGDKTYKDFEELVSDYESGGLHPGDLKPALSKALNKILQPVRDHFNKDAKAKDLLKRVKSYRVTK
The following text describes a protein:
Function:
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein.
Sequence:
MENRYIHFGIVLGLIAAISAGLLGGVNDFTSKVIAENTLKIVNEARKEVLPEATSFKEDEAKEADGMQYIPGFNDAGEVIGYVASVTEAGYGGDINFVVGIDKDAKVTGLNVVTSSETPGLGAKINGKEWQEHWIGKDSTYEFNKSVDAFAGATISPSAVYRGVIRALNTYQNEVSK
The following text describes a protein:
Function:
Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways.
Subcellular Localization:
Chromosome, telomere. Cytoplasm, cytoskeleton, spindle. Nucleus.
Sequence:
MGRGLAGACLARNMKMEEAETSTIPKRKKPKPCLPPISAVEAEAEAVAAGWMLDFACRCLCRHFCEENWAEFERSRDLALTIIKGLNKIEIHRMKTVCLCQLLAYIGEGKSIDPHTKSDQRLSPLENAYLVWTSFLKVQSKHEKLHEEIKRLIQIQAVAVYMEKGYFNKATEVVQRLFPESLTNEPLRMKLSAITKEKDPYHRFLLHFDFRLLLEKIKSYVTVFLNEESNNFLIKEATKEVESRCAGKNMVPIEFDKLIEEKKEKYFEMTQRSDQQSYSLADEASFFNTEQVKPSLKQRNRKQNVLQKKEDLQNSEISSESWLPPVKKKQRWSSKEDEKLKDGVQKFGVGNWNKILQHYDFKERTNVMLKDRWRTMVRSGMV
The following text describes a protein:
Function:
CzcA and CzcB together would act in zinc efflux nearly as effectively as the complete czc efflux system (CzcABC). The CzcB protein is thought to funnel zinc cations to the CzcA transport protein.
Sequence:
MNKKAIIIGLILALALGGGVAYRLTHSTTGGGEKAEQKEAGHKDEKGGHDEGKEEKEKKEEHDEHGEEKLVKMSAEVQKQSGVVVAPAKKQRLAGVISATGKVEANADRIAHVSPRIPGKIVAVRSSLGDSVAAGQVLVTLDSVELGEALNRYHQSRTKLALAQSNMDRIKVLVDKKIAARKEILQAETDYKTAQTELHTDEERLSLYGINLSDLKSDNHKKPLLPVRSPIGGVITEKHAIVGELSDPSKSLYTVADLSSVWVLVDIHEKDLAKVRRGQAATVIVGAFPDKKFRGRITYLADLVDEATRTVKARVEVPNPGRKLKPEMFATVELAIAADAPPVLAVPEEAVLELDGKKVIFVAEKETEFEPRVVELGRTVGGMVEVVSGLKEGERYATKGAFTLKSELKKEELEDDEH
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Miscellaneous:
MISCELLANEOUS: Present with 2900 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1.
Sequence:
MFPYLTRMNLSIKMGGLTLKESSPNAFLNNTTIARRFKHEYAPRFKIVQKKQKGRVPVRTGGSIKGSTLQFGKYGLRLKSEGIRISAQQLKEADNAIMRYVRPLNNGHLWRRLCTNVAVCIKGNETRMGKGKGGFDHWMVRVPTGKILFEINGDDLHEKVAREAFRKAGTKLPGVYEFVSLDSLVRVGLHSFKNPKDDPVKNFYDENAKKPSKKYLNILKSQEPQYKLFRGR
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that promotes the ubiquitination of various substrates. In turn, participates in the regulation of many biological processes including cell cycle, apoptosis, osteoclastogenesis as well as innate or adaptive immunity. Acts as negative regulator of NF-kappa-B-dependent transcription by promoting the ubiquitination and stabilization of the NF-kappa-B inhibitor TNFAIP3. May promote the ubiquitination of TRAF6 as well. Also acts as a negative regulator of T-cell activation. Inhibits cellular dsRNA responses and interferon production by targeting MAVS component for proteasomal degradation. Ubiquitinates the CDK inhibitor CDKN1A leading to its degradationand probably also CDKN1B and CDKN1C. This activity stimulates cell cycle G1-to-S phase transition and suppresses cellular senescence. May play a role in spermatogenesis (By similarity). Inhibits classical swine fever virus replication by mediating 'K27'-linked ubiquitination of viral NS4B and inducing its degradation via the proteasome.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAAQPQDREGGAQLAGPAAEADPLGRFTCPVCLEVYEKPVQVPCGHVFCSACLQECLKPKKPVCGVCRSTLAPGVRAVELERQIESTETSCHGCRKNFFLSKIRAHVATCSKYQNYIMEGVKATTKDASLQPRNVPNRYTFPCPYCPEKNFDQEGLVEHCKLVHSTDTKSVVCPICASMPWGDPNYRSANFIEHIQRRHQFSYDTFVDYDVDEEDMMNQVLQRSLLDQ
The following text describes a protein:
Function:
Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism.
Sequence:
MSVPSLMAMIRHSFDKDVDQVLFQGNSYVKKIILNRPQKLNCINHHMISEMTKKLKVYEIDPEVKVVVLKGNGKAFCAGGDVVASYIYMVAGHWSYGANTYKKKLILDYAVATYGKPVVALIDGIVMGAGAGLSMHGAFKIVTENTVFAMPETAIGHFVDVGASHFLSRLPGFLGEYLGLTGTTIRGEGMVACGLATHFVLSKDLHLVESALDEVTSSDTNKISKIISKFEHKPNVKQDDVYSRLEIINKCFSRKTVEEILSSLEIEAGNRADKWVLEAIKSMKAGSPISLKISLKSIREGRMQALDQCLAREYNIFCHIMRRTVSIDFFEGIRAKFLDKDENPKWEPARLELVSDEMVGQYFSRVDEDDWETLQLPARSSSVDIMRPRL
The following text describes a protein:
Function:
Component of an integrin containing attachment complex, which is required for muscle development and maintenance. Probable regulator of cell-extracellular matrix adhesion. Required during initial muscle assembly to form dense bodies and M-lines.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Cytoplasm, myofibril, sarcomere, M line. Note=Colocalizes with pat-3/beta-integrin in body wall muscles. Requires unc-52/perlecan and pat-3 to be localized to the muscle cell membrane. Colocalizes with cpna-1 in M line and dense bodies.
Domain:
The FERM domain is not correctly detected by PROSITE or Pfam techniques because it contains the insertion of a PH domain.
Sequence:
MAHLVEGTSIIDGKWQLPILVTDLNIQRSISVLGNLNVGGLMLELVSECDVERDWSDHALWWPEKRRWLQHTRSTLDQNGITAETQLEFTPMHKEARIQLPDMQMIDARVDFSVNSFKATKKLCRDLGIRYSEELSLKRYIPPEDLRRGTSDADNMNGPLSMRPGEESVGPMTLRKAAPIFASQSNLDMRRRGQSPALSQSGHIFNAHEMGTLPRHGTLPRGVSPSPGAYNDTMRRTPIMPSISFSEGLENEQFDDALIHSPRLAPSRDTPVFRPQNYVEKAAINRGWLDSSRSLMEQGIFEGDIILLRFKFMNFFDLNPKYDPVRINQLYEQAKWSILLDEFDHTEEEATLFAALQLQATLQRDSPEPEENNKDDVDILLDELEQNLDAAALNRRSDLTQVPELADYLKYMKPKKLAAFKGFKRAFFSFRDLYLSYHQSSSDVNSAPLGHFSLKGCEVSQDVSVGQQKYHIKLLLPTAEGMIDFILKCDSEHQYARWMAACRLASRGKSMADSSYQQEVESIKNLLKMQSGNGNENGNSNTASRKAAAVKLPNDFNVDEYISSKYVRRARSKQQIQQRVSDAHGNVRQLTATEAKLQYIRAWQALPEHGIHYFIVRFRNARKAELVAVAVNRLAKLNMDNGESLKTWRFANMKKWHVNWEIRHLKIQFEDEDIEFKPLSADCKVVHEFIGGYIFLSMRSKEHSQNLDEELFHKLTGGWA
The following text describes a protein:
Function:
Voltage-gated ATP nucleotide uniporter that can also transport the purine nucleotides ADP and GTP. Uses the membrane potential as the driving force to control ATP accumulation in lysosomes and secretory vesicles. By controlling ATP storage in lysosomes, regulates ATP-dependent proteins of these organelles. Also indirectly regulates the exocytosis of ATP through its import into lysosomes in astrocytes and secretory vesicles such as adrenal chromaffin granules, mucin granules and synaptic vesicles.
Subcellular Localization:
Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein.
Sequence:
SRKEKKIWIIIFFIAGAMLYASRTAMPVCAVSVSQEFNWTKTQTGLALSAFFWGYVTTQVVGGHLADKHGGEYTISISLAGWSFLTLMTPYVIRLGPPTAALMHAVIMRIFTGCFQGRFYYPSMSSLFSRKVSEFDRAFSYSFATSGSHIGTLFSGIIGSLMNDYLGWPLTFITIGILSFLHFLVYHYFVVSLRRVKLAQISSSSLSSSSWAHTHTRIFKMMTMTTNRAIVIGNFCSGWMFFILLSWLPTYFQETFPDAKGWVYNTIPWLFCPPSQWFGGWLADHLIYKGFSTTFVRKFIQSLAFLGSALFLVLMGHFDSYYFALFCLTGAINFSCFHHSGISVNVQDIAPTYAGAVFGFQNMAGAVPGFLGVYVTGYILEVSKSWTVVFNLTSVILLVGWFVFIMFGTGKKVI
The following text describes a protein:
Function:
Required for pre-mRNA splicing as component of the activated spliceosome. Component of the U5 small nuclear ribonucleoprotein (snRNP) complex and the U4/U6-U5 tri-snRNP complex, building blocks of the spliceosome. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs.
Subcellular Localization:
Nucleus.
Sequence:
MIEQQKRKAPGGPVPGPVPGPAPGPGAGSAPGAAPGPTPGPDLPLVPSAAKRPRHDPPAAGGGGGQPSTGALLQSGPPRCSSLQAPIMLLSGHEGEVYCCKFHPGGNTLASAGFDRLILLWNVYGDCDNYATLKGHSGAVMELHYNTDGSMLFSASTDKTVAVWDSETGERVKRLKGHTSFVNSCYPARRGPQLVCTGSDDGTVKLWDIRKKAAVQTFQNTYQVLAVTFNDTSDQIISGGIDNDIKVWDLRQNKLTYTMRGHADSVTGLSLSSEGSYLLSNAMDNTVRIWDVRPFAPKERCVKIFQGNVHNFEKNLLRCSWSPDGSKIAGGSADRFVYVWDTTSRRILYKLPGHAGSVNELAFHPEEPISKYSPNQVIWGNRFRAGCMLVFHKTAQILLVAQTPSIKELGERSPLQPGAKPWAEQWGSTCGPG
The following text describes a protein:
Function:
Required for replication-independent chromatin assembly and for the periodic repression of histone gene transcription during the cell cycle.
Subcellular Localization:
Nucleus.
Sequence:
MQILKIPWFGHKTENKTVECYAVTINKDGTRLASGGLDGNVKIWDLTTINVFYKMADQPHKSKKDSTSTKLEESLPDKSLRRPLCSMSRHNGVVTSLKFSPDGRWLASGSDDKICLIWEKDNTQIAKSFGTDEHDLEHWTVRKRLVAHDNDIQDICWSPDGNLLVTVGLDRSVIIWNALTFEKIKRYDIHQSMVKGIVFDPANKFFATASDDRTVRIFRYYKKLNEYNNYEFQMEHVVVDPFKKSPLTSYFRRMSWSPDGQHIAVPNATNGPVPSVAIINRGNWGSDISLIGHEAPVEVCSFSPTLFQIADTPANEEIKFQTVVATGGQDRTLAIWSTCNSRPIVVCSDIVDSSITDICWSPDGETLYFSCLDGSITGVKFGARELGQPVKEDLIDQQLNRYGADRESTILPESVEQLQLEEQSKDSRAISIRRMMPIQEAKPEQTPPISTPASAAIDIERLRKQTVTMTKSGKKRVAPLLVSTSAAPKNVLQKPLEKKRRTKSSSKISQAAYLLPKMGVQTTVHGIKKKAESMSNDTEVEENNDNDDIGENVMANTNSVSDAALKRQRNRRKRKLMELKYPSSFKYISNLPEGLFNNHTLQNIEINKIYKAHSKHKDISAEISSSTAVEIDEDLVFSVVFRVFDHMRKENEVLGQTSGRIRTTIEVRNGKPWDDDISDRDFDDATKVIVTEEGNDKREYCLFFPFRVQHVLPIILNDVLKYYVLCSFHGSVQIISADTGSYRCPTFELGESVVTMRHSQGYMLVLTSSGLFYSWDLKAMKVTMTGISIAAILNNYEIGGKIVVSPIVRGLEINPQDGSPLVLLDMTNDIYGYSIDLQCWVKTVDSWYYGVGADKDLDVVLTGLVKKSKMSYEEDKVTEKIFTYKFDSSNDLEDAMRKRGQELLDLI
The following text describes a protein:
Function:
GTPase activator for the nuclear Ras-related regulatory protein GSP1 (Ran), converting it to the putatively inactive GDP-bound state.
Miscellaneous:
MISCELLANEOUS: Present with 52200 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MATLHFVPQHEEEQVYSISGKALKLTTSDDIKPYLEELAALKTCTKLDLSGNTIGTEASEALAKCIAENTQVRESLVEVNFADLYTSRLVDEVVDSLKFLLPVLLKCPHLEIVNLSDNAFGLRTIELLEDYIAHAVNIKHLILSNNGMGPFAGERIGKALFHLAQNKKAASKPFLETFICGRNRLENGSAVYLALGLKSHSEGLKVVKLYQNGIRPKGVATLIHYGLQYLKNLEILDLQDNTFTKHASLILAKALPTWKDSLFELNLNDCLLKTAGSDEVFKVFTEVKFPNLHVLKFEYNEMAQETIEVSFLPAMEKGNLPELEKLEINGNRLDEDSDALDLLQSKFDDLEVDDFEEVDSEDEEGEDEEDEDEDEKLEEIETERLEKELLEVQVDDLAERLAETEIK
The following text describes a protein:
Function:
Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity). Has dual phospholipase and lysophospholipase activities toward diacylphospholipids. Preferentially cleaves sn-2 ester bonds over sn-1 bonds. Acts as a lipase toward glycerolipid substrates. Hydrolyzes fatty acyl chains of diacylglycerols with preference for the sn-2 position and of triacylglycerols with not positional selectivity. May also hydrolyze long chain retinyl esters such as retinyl palmitate. May contribute to digestion of dietary phospholipids, glycerolipids and retinoids, facilitating lipid absorption at the brush border.
Subcellular Localization:
Apical cell membrane; Single-pass type I membrane protein.
Sequence:
KYPKRTISLSSFFSPPQLDFENDWKLITVFLSPQDACLPCSSNQQVKSSLVREDSLPPFKYHPRVDCKAFTPLSSHSTPPREPCACSKKPSRLERAVMRWSHQNYWEKLLASGRYDTEDSFTVVLQPIFHDKDSSLFPVIGVSVLVKCSSQRDKNPKVFCECLILVGEKSLLWGRVRLPRSPWKVIPTPSHFTFYFPVHRLKPADIKVIAALGDSLTAANGAGSRASDILDVLTQYRGLSWSVGGNENISTVTTLANILREFNPSLQGFSIGTGKQTSPGAFLNQAVAGDLAEDLPAQARRLVDLMKNSFKFNFQEDWKIITIFIGGNDLCDFCSDPQVPRAFVNLVPVLEIVSLRKLYQEKKVFCPRLLLRSLCPCVVKFADNSTEIASLILLNKRYQEGTHQLIDSGKYDTREDFTVVIQPFLEKVSMPMTPEGLPDSSFFAPDCFHFHKKAHGRAASGLWNNMHQSQWSRTALRGRELCSEFSRFTCNPFAFTVHTLKPADVKVVAAIGDSLTENMGRGLLPPHLFCFTSPLPDILREFNGDLTGYAIGVGEASDHNAFLNQAVPGAKAEGLLSQVQALVQRMKDDPRVSFQRDWKIITVLIGIHDLCDYCTDSNLYSATNFVGHLQAALDMLHREVGKGNRWVAYLCNCVLTVREGSPELARIEEVTRAYQSGTRRLVESGRYDTREDFTVVLQPFFQDIKLAFLPDGRPDISFFAPNCFHPSQKFHSQLSRALWNNMVSNLHKLRPADIKVVAALGDSLTSGVLASGENRVSDPSTEGILLLSFLLSIGGDGTLETHTTLPNILKKFNPQIYGYSIGTEEGTAGFNVAVGGAKAQDMPVQARALVERMKHSLEVNLEQDWKLITLFVGGNDLCVYCKDEDTHSVEKYVQHLEQALDILSELPRVFVSVVEIMEMVGLRQIHGEKCLVPVQNFCPCFLLPQENSPELQEMKNVNRAFQSSSILMAFSQKYMQREDFAVVLQPFFQSTHIPLDNKGDADLSFFSVDCFHFSERGYSEMAIALWNNMLEPVGQKQIYNNFTYSRTKLKCPSEDHPYLFTLRNSGLPGIHFKGQQNSPWEVPFWTVLVAAVGSLTVGAGIAVLWKSRKLPSRGSDTPAGAMVTAF
The following text describes a protein:
Function:
Responsible for the C-12 hydroxylation of the macrolactone ring of erythromycin. Thus, EryK catalyzes the hydroxylation of erythromycin D (ErD) at the C-12 position to produce erythromycin C (ErC). Erythromycin B (ErB) is not a substrate for this enzyme.
Sequence:
MTTIDEVPGMADETALLDWLGTMREKQPVWQDRYGVWHVFRHADVQTVLRDTATFSSDPTRVIEGASPTPGMIHEIDPPEHRALRKVVSSAFTPRTISDLEPRIRDVTRSLLADAGESFDLVDVLAFPLPVTIVAELLGLPPMDHEQFGDWSGALVDIQMDDPTDPALAERIADVLNPLTAYLKARCAERRADPGDDLISRLVLAEVDGRALDDEEAANFSTALLLAGHITTTVLLGNIVRTLDEHPAHWDAAAEDPGRIPAIVEEVLRYRPPFPQMQRTTTKATEVAGVPIPADVMVNTWVLSANRDSDAHDDPDRFDPSRKSGGAAQLSFGHGVHFCLGAPLARLENRVALEEIIARFGRLTVDRDDERLRHFEQIVLGTRHLPVLAGSSPRQSA
The following text describes a protein:
Function:
Catalyzes the formation of 2'O-methylated cytidine (Cm32) at position 32 in tRNA.
Subcellular Localization:
Cytoplasm.
Sequence:
MIIMISVILVNPKYSGNVGSIARVMMNFGFEELRIVGDKSIINNEAYMMAVHAREILDNAKFYNTFDEAIGDLDFVIATSGARGGDRNLKRVPITPKELADKILEVKGNIGIVFGREDDGLRNEEIDKCDLLVSIPTSEKYPIMNLSHAVAVILYEIYTKKVRNKFLDINMREASKEDKELLIRKFNEFIDKNEKIPEHKKELCKIIFKRLVNRAFISGKEAWTLMSAFK
The following text describes a protein:
Function:
Mediates sugar transport across membranes.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MPSETDDFLLSNYTEKINMTTSLGQTILPYLSFTALSSTVAFFLCGLQICHRIKTRGSSEGTSPAPFLLSFLSCGLFIQYGLLKDDDVITYCNGIGCFLQACYLMYFYYMTRNRRFLNKVISIELGIIGIVVYWVAHSTNSHLTKTTYVGNYCIFLNICSVAAPLFDIGKVVRNKSSESLPLPLCVACFVVCLQWMFYGYIVDDIVILVPNVIATVISILQLSLFIIYPGAPAGVLPQKYEHI
The following text describes a protein:
Function:
Structural component of the gap junctions.
Subcellular Localization:
Cell junction, gap junction. Cell membrane; Multi-pass membrane protein.
Sequence:
MVMIETFLGMAKYLSPREDDDWSDRLNYLITPNLLLAFSVLISFKQFGGRPIECMFPNKFPGSWEQYAENYCWSQDTYFVEPTQDVSLLKQEERYTPDRQLSYYQWVPFFLLLQAAFFRAPSYLWKYFSNHSGIRIHEVVEKAKDNANVEEEVREKNIGILKRHLSSALRFQANMESKRVQVHKTVTFLNFQYSSGFISWVYLFTKSLYFINVFAQLYLMNYFLGTNRHQWYGFGVVKDIVKGEPWERSGYFPRAAVCDFEVRQVANIQRYSVQCVLVINIFNEKIFVLLWFWYLILLFASTVSFIQWFVVLVFPCFSNWFVKQHLALSTLQHFNQRNSRRENADVSKFVTQYLHKDGVFVLRMVSSHAGIIFATDLVQALYEAYDFQDKNKLDQGSPVSDDLQTISTGTGSSIRQRKNKKSSRIEYKPGTPFTTTLMPEKDDIESSSTSSEEDQKRVSNGVTNI
The following text describes a protein:
Function:
Required for the biogenesis of c-type cytochromes. Possible subunit of a heme lyase.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MLPELGTFLLVLALLVALVQAVVPLAGAQRGRSAWMAVARPAALVQLALIAAAFAVLTHAFLVQDFSVRYVAENSNSLLPLIYRYSAVWGAHEGSLLLWTLVLALWTGAVAIWSRQLPAQVIARVLGVMALVSIGFLAFLLFTSNPFARLMPVPLEGADLNPLLQDPGLIIHPPMLYCGYVGFAVPFAFAIAALLEGRMDARWLRWTRPWTNIAWSMLTVGIALGSWWAYYELGWGGWWFWDPVENASFMPWLVGTALLHSQAVTGKRGSFASWTLLLAIAAFALSLLGTFLVRSGVLTSVHSFAADPSRGVFILVFLLSVVGGSLLLYVLRAPRLSQGDDPRRAFAGSSRETLLLLNNLLLACACAMVLLGTLYPLLADALGLGKLSVGPPYFGTLFLVLMAPLVALLPFGPLTRWQRDQPSRPLAMLAPWAALAVVLGVLAWFAAPQGQLKTALGVAGAAWVVLGTLRFLWTRRAAKGRKFTAEMLGMALAHTGVAVFLAGALLVESLSLQREVALAPGQQMEIGSYALHFDGLKEVRGPNYVSDRATLQVFKDDAAVGTLHAEKRRYASGGQTLTEAAIRPGPFGDLYVALGEPLGNQAWAVRVHLKPFVRWIWLGALLMALGGLVTAADRRFRRSPESLNV
The following text describes a protein:
Function:
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MGITMFKEFKALLSFFTRIPIYVEDFDFENIANYFYLIILIGYVFGIFSLILGYIFSFLLPNFLSAVLILFFIEYLNGFHHIDGLIDFGDGWMAVGDKRKKLMAMKDRYIGCGGVVFAIFFNLMAVISLSYILDINILYLLVGEVCAKLGMLSCSTFGNPLIEGTGRYFVKKADEKFLTIGIILSLPLLLIFSGIERKIVIIAIITTIITGLCMAKIAKRHFGGVNGDVLGASNEITRVVVLLSIIASIKVFSIYLLG
The following text describes a protein:
Function:
Toxic component of a type II toxin-antitoxin (TA) system. An endoribonuclease that cleaves both E.coli and M.smegmatis 23S rRNA between G2661 and A2662 in the sarcin-ricin loop (SRL, E.coli 23S rRNA numbering). The SRL sequence is highly conserved and is implicated in GTP hydrolysis by EF-Tu and EF-G. Acts on purified ribosomes but not on isolated RNA in E.coli, nor on a shortened artificial substrate. Upon expression in E.coli inhibits cell growth, colony formation and translation. Its toxic effect is neutralized by coexpression, or subsequent expression (tested over 2 hours) with cognate antitoxin VapB20.
Sequence:
MIFVDTSFWAALGNAGDARHGTAKRLWASKPPVVMTSNHVLGETWTLLNRRCGHRAAVAAAAIRLSTVVRVEHVTADLEEQAWEWLVRHDEREYSFVDATSFAVMRKKGIQNAYAFDGDFSAAGFVEVRPE
The following text describes a protein:
Function:
Transcription factor which plays an essential role in virulence by activating the transcription of iron uptake genes such as FRE7 in iron-poor environments such as the host bloodstream and internal organs. Promotes commensalism in a mouse model of gastrointestinal infection.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Interaction with SFU1 promotes cytoplasmic localization whereas interaction with SSN3 and subsequent phosphorylation promotes nuclear localization. Nuclear localization is associated with virulence.
Sequence:
MKFEKGKVRILPKPSPTPTNPQTPLPLLPAQTKPVNSKRKSAASTPGNESKKSRKSNSTASTPNSATPTSVGTPPQKTSKPTGHRPVTSCTFCRQHKIKCNASDNYPNPCERCKKMGLKCEIDPEFRPRKGSQIQSLKSDVDELKAKIEMLTKNESLLTQALNQHNLNHASQQQQSSGSQSQQQHPPNPQRALSYTSANSSPQVAFSNASPIPSVTSIQQNAPLTHENSDNSPYALNTPENIEELQPISEFILGDVTLPLNRANELHDKFMTTHLPFLPIIISRSATELYHKSQLLFWAVILTASLSEPEPKLYMSLASLIKQLAIETCWIKTPRSTHVIQALIILSIWPLPNEKVLDDCSYRFVGLAKNLSLQLGLHRGGEFIQEFSRNQVSLGPDAERWRTRSWLAVFFCEQFWSSLLGLPPSINTTDYLLENARVDKSLPKNFRCLISLSIFQCKLVNIMGISVTRPDGLLEPSNRAGSLSLLDRELERLRFKLQFEEGGPIEVYYLYIKLMICCFAFLPGTPIEDQVKYVSFAYLSATRIVTIVSKMVNDISLIELPIYIRQAVTYSVFMLFKLHLSRYLIDKYVDSARQSIVTVHRLFRNTLSSWKDLQNDISRTAKVLENLNMVLYNYPEIFLNDSENEDSSIITRMRSHLTASLFYDLVWCVHEARRRSVLDKGKRQAQPNKKILPLPFYNQITKDDFKTITTTSPNGTTITTLVPTDQAMNQAKSKSFDSSKPLEINGIPLPMLEATGSTREVLDSLPSQSLPSQAPTLQQYPMQQDQQQQEPSQQQQQKHSQQSQQYQQQQQSNQQQPHLQHQRQFQQSPPPQFSMISSTPPLQQPPFILANSPLPQTYLPKIDEMNMSPEVKQENSVAPFASQITNFFDQQTSGWFNNDNQDDDFLGWFDVNMMQEK
The following text describes a protein:
Function:
N-acetylglutamate synthase involved in arginine biosynthesis.
Subcellular Localization:
Mitochondrion.
Sequence:
MSKRMQNLIMEILQAQPSLRDSKTYLNSFAPRKPPPRQPQPTQSKPPSSDRTDTIASSSSSSSSSAQLNPPTEFPIPPNIARPGSLHNPSTTTWDPQHSISLENDPHATTATETAPLKLPKAILDSLHEQKQRTTSDTLSVRISDPILPTTSASPNATPKETSTVAIPQVTPVSDALADSHTALVKVQGPFTDRQLDSIAEGLVYLKRLGLVSVVVVDQDDWPEISADIDHDGQLVTGTDELEEQRMGDWLAAHPSPSSAKVNQAVCRSSVLGRKQERLRKRIMAETLRLADSLNRKGAMARPFPQAVVKVDAHAAAQVEAEARQLQQSQASSDVKPGDAVVAGSSSTSPTVHYGSGGEERLRPPLVSDDSLCSIRSALASDQIPVLAPYALFENERDGTLETLCVRADDVMVALARDMVVAATRPSEQAVASDVSASASASASASSTSADALAELIGGEVDMMPLRLMVINREGGIPSHARGGDPHLSINLASEYHQIKQSFVWHQTHPTALRNLDAISDCLSYMPQTSSGVLVTHRSPRSLIANLITNKAAHSPSLPHRLLANKQDVRHTPTIVRPGLPIKVIQDFDKLNLDKMCALLEASFRRKLNQHAYYERLRKSLDFAIITGDYQGAAIVTKEYAPDDDRASVEPIAYLDKFAVLPSLQGSGTVDFLWGALRDEVQGLGLLDALNDNGGRGGYGTGRDLVWKSRSNNPVNRWYYERSNGFVRIDTDAKGTGWQLFWCDAEDKLARLSGERRLSASASNLQEAAAIVHDNIQLASTFDQDTVSPYVDRGSWDNSSSSDTNGIEAYERSRRLSKPKFDSHLHRGSIRSGSAPTHLTLLPIVAPEEGGRLLRWAKCMKTIKGAWAD
The following text describes a protein:
Function:
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MVTKKSKKAWPWLWFSVLVILLDQLSKYLANHFLSLGHPVKILPFLNFTLNYNTGAAFSFLGTENGWQIIFFAAISFVVSIFLILWLSRTSRSEIMMLLGLSLIIGGALGNFIDRLRWSYVTDFIDFHIKDWHFATFNVADSAICVGVFLLIVHMLLTPSSKP