ProGP508 (Mip (Probable FKBP-type peptidyl-prolyl cis-trans isomerase FkpA))

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ProGP ID ProGP508 (Mip (Probable FKBP-type peptidyl-prolyl cis-trans isomerase FkpA))
Validation Status Uncharacterized
Organism Information
Organism NameNeisseria 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 Namemip (NMB_1567) or fkpA
Protein Information
Protein NameMip (Probable FKBP-type peptidyl-prolyl cis-trans isomerase FkpA)
UniProtKB/SwissProt ID Q9JYI8
NCBI RefSeq NP_274574.1
EMBL-CDSAAF41921.2
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 LocationMembrane
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 DetectionMass Spectrometry
Literature
Year of Identification2015
Year of Identification Month Wise2015.5.1
ReferenceSchulz 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]
AuthorBenjamin 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 GroupSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia.
Corresponding Author Michael P. Jennings
ContactSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland, Australia.
ReferenceHung 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]
AuthorMiao-Chiu Hung, Omar Salim, Jeannette N. Williams, John E. Heckels, and Myron Christodoulides
Research GroupNeisseria 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
ContactNeisseria 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.