The following text describes a protein:
Function:
Major human immunogenic protein, detected in patients recovering from meningitidis. Autotransporter with a secreted protease domain involved in processing other autotransporter proteins including App, IgA, LbpB and NHBA (By similarity). Probably autoprocesses to release the about 70 kDa passenger domain (Probable). Both cell surface protein (Neisserial autotransporter lipoprotein NalP) and the passenger domain cleave human (host) complement factor C3, generating a shorter alpha chain and a longer beta chain than normal. Uptake of a passenger domain fragment (residues 101-784) by human cells increases cell metabolic activity; the serine protease activity is required for this increase; [NalP passenger domain]: Cleaves human (host) complement factor C3, generating a shorter alpha chain and a longer beta chain than normal. Does not act on mouse or rabbit C3. Cleavage causes C3b degradation by human CFI and CFH, and thus decreases deposition of C3b on the bacteria surface and probably facilitates complement escape; Plays a role in extracellular-DNA (eDNA) mediated biofilm formation. In some strains (including cc32 strain MC58) eDNA stimulates biofilm formation. When NalP is not expressed (and no longer processes NHBA or IgA) biofilm formation increases.
Miscellaneous:
MISCELLANEOUS: Probably a phase variable gene because of slipped-strand mispairing of a polycytidine tract in the coding sequence.
Subcellular Localization:
[Neisserial autotransporter lipoprotein NalP]: Cell outer membrane; Lipid-anchor. Cell surface. Note=The 112 kDa precursor is associated with the cell outer membrane, the passenger domain is secreted; [NalP passenger domain]: Secreted. Host cytoplasm, host perinuclear region. Note=The 68-70 kDa passenger form is secreted. A fragment of the passenger domain (residues 101-784) is taken up by human brain microvascular endothelial cells as well as some other cells; [NalP translocator]: Cell outer membrane. Note=An approximately 30 kDa form is detected in whole cells; this is probably the beta-barrel translocation domain integrated in the outer membrane.
Domain:
The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Insertion of the C-terminal translocator domain in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface, with subsequent lipid-anchoring to the cell outer membrane and eventual release of the passenger domain; The translocator domain forms a 12-stranded beta-barrel with a 10 X 12.5 Angstrom channel.
Sequence:
MRTTPTFPTKTFKPTAMALAVATTLSACLGGGGGGTSAPDFNAGGTGIGSNSRATTAKSAAVSYAGIKNEMCKDRSMLCAGRDDVAVTDRDAKINAPPPNLHTGDFPNPNDAYKNLINLKPAIEAGYTGRGVEVGIVDTGESVGSISFPELYGRKEHGYNENYKNYTAYMRKEAPEDGGGKDIEASFDDEAVIETEAKPTDIRHVKEIGHIDLVSHIIGGRSVDGRPAGGIAPDATLHIMNTNDETKNEMMVAAIRNAWVKLGERGVRIVNNSFGTTSRAGTADLFQIANSEEQYRQALLDYSGGDKTDEGIRLMQQSDYGNLSYHIRNKNMLFIFSTGNDAQAQPNTYALLPFYEKDAQKGIITVAGVDRSGEKFKREMYGEPGTEPLEYGSNHCGITAMWCLSAPYEASVRFTRTNPIQIAGTSFSAPIVTGTAALLLQKYPWMSNDNLRTTLLTTAQDIGAVGVDSKFGWGLLDAGKAMNGPASFPFGDFTADTKGTSDIAYSFRNDISGTGGLIKKGGSQLQLHGNNTYTGKTIIEGGSLVLYGNNKSDMRVETKGALIYNGAASGGSLNSDGIVYLADTDQSGANETVHIKGSLQLDGKGTLYTRLGKLLKVDGTAIIGGKLYMSARGKGAGYLNSTGRRVPFLSAAKIGQDYSFFTNIETDGGLLASLDSVEKTAGSEGDTLSYYVRRGNAARTASAAAHSAPAGLKHAVEQGGSNLENLMVELDASESSATPETVETAAADRTDMPGIRPYGATFRAAAAVQHANAADGVRIFNSLAATVYADSTAAHADMQGRRLKAVSDGLDHNGTGLRVIAQTQQDGGTWEQGGVEGKMRGSTQTVGIAAKTGENTTAAATLGMGRSTWSENSANAKTDSISLFAGIRHDAGDIGYLKGLFSYGRYKNSISRSTGADEHAEGSVNGTLMQLGALGGVNVPFAATGDLTVEGGLRYDLLKQDAFAEKGSALGWSGNSLTEGTLVGLAGLKLSQPLSDKAVLFATAGVERDLNGRDYTVTGGFTGATAATGKTGARNMPHTRLVAGLGADVEFGNGWNGLARYSYAGSKQYGNHSGRVGVGYRF