ProGP231 (VirB10 protein)

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ProGP ID ProGP231 (VirB10 protein)
Validation Status Characterized
Organism Information
Organism NameCampylobacter jejuni serotype O:23/36 (strain 81-176)
Domain Bacteria
Classification Family: Campylobacteraceae
Order: Campylobacterales
Class: Epsilonproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 354242
Genome Information
GenBank CP000550.1
EMBL CP000550
Organism Additional Information Campylobacter jejuni is a microaerophilic, Gram-negative, human pathogen that is the major cause of bacterial food-borne diarrhoea (gastroenteritis). It is most frequently responsible for a form of post-infection neuromuscular paralysis known as Guillain Barre' syndrome. It also leads to an immunoproliferative small intestine disease that is a rare malignant lymphoma of the intestine. Motility is essential for pathogenicity.
Gene Information
Gene NameCjp3 (CJJ81176_pVir0003)
NCBI Gene ID 1343085
GenBank Gene Sequence NC_005012
Protein Information
Protein NameVirB10 protein
UniProtKB/SwissProt ID Q9KIS0
NCBI RefSeq NP_863300.1
EMBL-CDSEAQ71778.1
UniProtKB Sequence >tr|Q9KIS0|Q9KIS0_CAMJJ VirB10 OS=Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) GN=virB10 PE=4 SV=1 MKKSFLSLSLATILLSNNLFAEDIFDQTSEENVSKNISKKDNQSQNLLNKEDLDYLFKNS DTKFPVTDYIYKGGFKEPNEDIKIHSEEKPKKEEDNNITKLAKIEEKKQELIQKNQQIAK EIHQDNISSQERKIKKLIRDSILADRGNTQIYFQENSSKYGVDGFSNQKSIDVSTNEHRL YRMIRAGRLIPALLTSAISSDLQGIVTAQIEQDIYASMGNAVLIPRGSKAIGFYKNDNKI GQNRLEIQWREIITPQGVNILLTNALASDNMGMAGAVGSVNNKYLERYGMPYALSTISNV LLLSIASKAGNNNYAQEVYSQSKNDVSTIVDDIIQQQSQIKPTIEIKSGSRIFIVPTNHM WFAKPKNNEVLIQYFQDN
Sequence length 378 AA
Subcellular LocationPeriplasmic or on surface
Function Type IV secretion (TFSS) homolog. The TFSS genes present on pVir have been proposed to encode proteins that form a functional secretion channel that appears to affect both intestinal epithelial cell invasion and natural competence.
Glycosylation Status
Glycosylation Type N- (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN32, N97
Experimentally Validated Glycosite(s ) in Mature ProteinN32, N97
Glycosite(s) Annotated Protein Sequence >tr|Q9KIS0|Q9KIS0_CAMJJ VirB10 OS=Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) GN=virB10 PE=4 SV=1 MKKSFLSLSLATILLSNNLFAEDIFDQTSEEN*(32)VSKNISKKDNQSQNLLNKEDLDYLFKNS DTKFPVTDYIYKGGFKEPNEDIKIHSEEKPKKEEDNN*(97)ITKLAKIEEKKQELIQKNQQIAK EIHQDNISSQERKIKKLIRDSILADRGNTQIYFQENSSKYGVDGFSNQKSIDVSTNEHRL YRMIRAGRLIPALLTSAISSDLQGIVTAQIEQDIYASMGNAVLIPRGSKAIGFYKNDNKI GQNRLEIQWREIITPQGVNILLTNALASDNMGMAGAVGSVNNKYLERYGMPYALSTISNV LLLSIASKAGNNNYAQEVYSQSKNDVSTIVDDIIQQQSQIKPTIEIKSGSRIFIVPTNHM WFAKPKNNEVLIQYFQDN
Sequence Around Glycosites (21 AA) EDIFDQTSEENVSKNISKKDN
EEKPKKEEDNNITKLAKIEEK
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Technique(s) used for Glycosylation DetectionMass shift detected on SDS-polyacrylamide gel and SBA (soybean agglutinin) lectin-agarose affinity chromatography
Technique(s) used for Glycosylated Residue(s) Detection Site-directed mutagenesis
Protein Glycosylation- Implication Glycosylation of VirB10 at N97, but not at N32, is essential for wild-type (full) levels of competence. VirB10 is not detected in the pgl mutants. It reflects instability of the nonglycosylated protein, perhaps a result of an inability to interact with other TFSS proteins.
Glycan Information
Glycan Annotation Terminal α1,3-linked GalNAc.
Protein Glycosylation linked (PGL) gene(s)
OST Gene NamePglB
OST ProGT IDProGT9 (PglB)
Literature
ReferenceMaita, N., Nyirenda, J., Igura, M., Kamishikiryo, J. and Kohda, D., 2010. Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases 2. Journal of Biological Chemistry, 285(7), pp.4941-4950.
Corresponding Author Daisuke Kohda
ContactDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan.
ReferenceLarsen, J.C., Szymanski, C. and Guerry, P., 2004. N-linked protein glycosylation is required for full competence in Campylobacter jejuni 81-176. Journal of bacteriology, 186(19), pp.6508-6514.
Corresponding Author Patricia Guerry
ContactNRC-Institute for Biological Sciences, Ottawa, Canada.
ReferenceMaita, N., Nyirenda, J., Igura, M., Kamishikiryo, J. and Kohda, D. (2010) Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases. J Biol Chem, 285, 4941-4950. [PubMed: 20007322]
Author Maita, N., Nyirenda, J., Igura, M., Kamishikiryo, J. and Kohda, D.
Research GroupDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan.
Corresponding Author Kohda, D.
ContactDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan.
Reference Larsen, J.C., Szymanski, C. and Guerry, P. (2004) N-linked protein glycosylation is required for full competence in Campylobacter jejuni 81-176. J Bacteriol, 186, 6508-6514. [PubMed: 15375132]
Author Larsen, J.C., Szymanski, C. Guerry, P.
Research GroupDepartment of Microbiology and Immunology, F. Edward Hebert School of Medicine, Uniformed Services University of the Health Sciences, Bethesda, Maryland, USA.
Corresponding Author Guerry, P.
ContactDepartment of Microbiology and Immunology, F. Edward Hebert School of Medicine, Uniformed Services University of the Health Sciences, Bethesda, Maryland, USA.