ProGP508 (Mip (Probable FKBP-type peptidyl-prolyl cis-trans isomerase FkpA))
Home -> ProGPdb -> Search ProGP -> Display data
| ProGP ID | ProGP508 (Mip (Probable FKBP-type peptidyl-prolyl cis-trans isomerase FkpA)) |
| Validation Status | Uncharacterized |
| Organism Information | |
| Organism Name | Neisseria meningitidis C311 and MC58 |
| Domain | Bacteria |
| Classification | Family: Neisseriaceae Order: Neisseriales Class: Betaproteobacteria Division or phylum: "Proteobacteria" |
| Taxonomic ID (NCBI) | 491 |
| Genome Information | |
| GenBank | AE002098.2 |
| EMBL | AE002098 |
| Organism Additional Information | Neisseria meningitidis (Gram-negative bacterium) is the causative agent of cerebrospinal meningitis. Sometimes, it crosses the epithelium using its pili to enter the bloodstream. After rapid proliferation, this leads to septicemia. It also crosses the blood-brain barrier to proliferate in the brain. |
| Gene Information | |
| Gene Name | mip (NMB_1567) or fkpA |
| Protein Information | |
| Protein Name | Mip (Probable FKBP-type peptidyl-prolyl cis-trans isomerase FkpA) |
| UniProtKB/SwissProt ID | Q9JYI8 |
| NCBI RefSeq | NP_274574.1 |
| EMBL-CDS | AAF41921.2 |
| UniProtKB Sequence | >sp|Q9JYI8|FKBA_NEIMB Probable FKBP-type peptidyl-prolyl cis-trans isomerase FkpA OS=Neisseria meningitidis serogroup B (strain MC58) GN=fkpA PE=1 SV=1 MNTIFKISALTLSAALALSACGKKEAAPASASEPAAASSAQGDTSSIGSTMQQASYAMGV DIGRSLKQMKEQGAEIDLKVFTEAMQAVYDGKEIKMTEEQAQEVMMKFLQEQQAKAVEKH KADAKANKEKGEAFLKENAAKDGVKTTASGLQYKITKQGEGKQPTKDDIVTVEYEGRLID GTVFDSSKANGGPVTFPLSQVIPGWTEGVQLLKEGGEATFYIPSNLAYREQGAGDKIGPN ATLVFDVKLVKIGAPENAPAKQPAQVDIKKVN |
| Sequence length | 272 AA |
| Subcellular Location | Membrane |
| Function | Macrophage Infectivity Potentiator Protein. PPIases (peptidyl-prolyl cis-trans isomerases) function primarily to assist the folding and structuring of unfolded and partially folded polypeptide chains and proteins. (EC:5.2.1.8) The MIP protein of N. meningitidis is able to induce cross-strain bactericidal antibodies. Therefore, it is a potential antigen to be included in defined serogroup B meningococcal vaccines. |
| Glycosylation Status | |
| Glycosylation Type | O- (Ser/Thr) linked |
| Technique(s) used for Glycosylation Detection | Mass Spectrometry |
| Literature | |
| Year of Identification | 2015 |
| Year of Identification Month Wise | 2015.5.1 |
| Reference | Schulz, B.L., Jen, F.E., Power, P.M., Jones, C.E., Fox, K.L., Ku, S.C., Blanchfield, J.T. and Jennings, M.P., 2013. Identification of bacterial protein O-oligosaccharyltransferases and their glycoprotein substrates. PloS one, 8(5), p.e62768. |
| Corresponding Author | Michael P Jennings |
| Contact | School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia. |
| Reference | Hung, M.C., Salim, O., Williams, J.N., Heckels, J.E. and Christodoulides, M., 2011. The Neisseria meningitidis macrophage infectivity potentiator protein induces cross-strain serum bactericidal activity and is a potential serogroup B vaccine candidate. Infection and immunity, 79(9), pp.3784-3791. |
| Corresponding Author | Myron Christodoulides |
| Contact | Neisseria Research Laboratory, Molecular Microbiology, Division of Infection, Inflammation and Immunity, Sir Henry Wellcome Research Laboratories, MP814, University of Southampton Medical School, Southampton SO16 6YD, United Kingdom. |
| Reference | Schulz BL, Jen FE, Power PM, Jones CE, Fox KL, Ku SC, Blanchfield JT, Jennings MP. (2013)Identification of bacterial protein O-oligosaccharyltransferases and their glycoprotein substrates. PLoS One, 8(5): e62768. [PubMed: 23658772] |
| Author | Benjamin L. Schulz, Freda E. C. Jen, Peter M. Power, Christopher E. Jones, Kate L. Fox, Shan C. Ku, Joanne T. Blanchfield, and Michael P. Jennings |
| Research Group | School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia. |
| Corresponding Author | Michael P. Jennings |
| Contact | School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia. |
| Reference | Hung MC, Salim O, Williams JN, Heckels JE, Christodoulides M. (2011) The Neisseria meningitidis macrophage infectivity potentiator protein induces cross-strain serum bactericidal activity and is a potential serogroup B vaccine candidate. Infect Immun., 79(9), 3784–3791. [PubMed: 21708989] |
| Author | Miao-Chiu Hung, Omar Salim, Jeannette N. Williams, John E. Heckels, and Myron Christodoulides |
| Research Group | Neisseria Research Laboratory, Molecular Microbiology, Division of Infection, Inflammation and Immunity, Sir Henry Wellcome Research Laboratories, MP814, University of Southampton Medical School, Southampton SO16 6YD, United Kingdom. |
| Corresponding Author | Myron Christodoulides |
| Contact | Neisseria Research Laboratory, Molecular Microbiology, Division of Infection, Inflammation and Immunity, Sir Henry Wellcome Research Laboratories, MP814, University of Southampton Medical School, Southampton SO16 6YD, United Kingdom. |