ProGP223

Home -> ProGPdb -> Search ProGP -> Display data

ProGP ID ProGP223
Validation Status Characterized
Organism Information
Organism NameCampylobacter jejuni NCTC 11168 serotype O:2
Domain Bacteria
Classification Family: Campylobacteraceae
Order: Campylobacterales
Class: Epsilonproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 192222
Genome Sequence(s)
GenBank AL111168.1
EMBL AL111168
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 NameCj0289c
NCBI Gene ID 904613
GenBank Gene Sequence 904613
Protein Information
Protein NamePEB3
UniProtKB/SwissProt ID Q0PBL7
NCBI RefSeq YP_002343730.1
EMBL-CDSCAL34442.1
UniProtKB Sequence >tr|Q0PBL7|Q0PBL7_CAMJE Major antigenic peptide PEB3 OS=Campylobacter jejuni GN=peb3 PE=1 SV=1 MKKIITLFGACALAFSMANADVNLYGPGGPHTALKDIANKYSEKTGVKVNVNFGPQATWF EKAKKDADILFGASDQSALAIASDFGKDFNVSKIKPLYFREAIILTQKGNPLKIKGLKDL ANKKVRIVVPEGAGKSNTSGTGVWEDMIGRTQDIKTIQNFRNNIVAFVPNSGSARKLFAQ DQADAWITWIDWSKSNPDIGTAVAIEKDLVVYRTFNVIAKEGASKETQDFIAYLSSKEAK EIFKKYGWRE
Sequence length 250 AA
Subcellular LocationSurface
Function Functions as an adhesin ; also a transport protein that may function in utilization of 3-phosphoglycerate or other phosphate-containing molecules from the host.
Protein Structure
PDB ID 2HXW
Glycosylation Status
Glycosylation Type N (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN90
Experimentally Validated Glycosite(s ) in Mature ProteinN90
Glycosite(s) Annotated Protein Sequence >tr|Q0PBL7|Q0PBL7_CAMJE Major antigenic peptide PEB3 OS=Campylobacter jejuni GN=peb3 PE=1 SV=1 MKKIITLFGACALAFSMANADVNLYGPGGPHTALKDIANKYSEKTGVKVNVNFGPQATWF EKAKKDADILFGASDQSALAIASDFGKDFN*(90)VSKIKPLYFREAIILTQKGNPLKIKGLKDL ANKKVRIVVPEGAGKSNTSGTGVWEDMIGRTQDIKTIQNFRNNIVAFVPNSGSARKLFAQ DQADAWITWIDWSKSNPDIGTAVAIEKDLVVYRTFNVIAKEGASKETQDFIAYLSSKEAK EIFKKYGWRE
Sequence Around Glycosites (21 AA) AIASDFGKDFNVSKIKPLYFR
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionSBA (soybean agglutinin) lectin-agarose affinity chromatography
Technique(s) used for Glycosylated Residue(s) Detection CapLC-MS/MS (capillary liquid chromatography-tandem mass spectrometry)
Glycan Information
Glycan Annotation Linkage: Bac-Asn.
1406 Da heptasaccharide composed of GalNAc-α1,4-GalNAc-α1,4-[Glcβ1,3-]GalNAc-α1,4-GalNAc-α1,4-GalNAc-α1,3-Bac-β1,N-Asn-Xaa, where Bac is bacillosamine, 2,4-diacetamido-2,4,6-trideoxyglucopyranose.
BCSDB ID23625
Technique(s) used for Glycan Identification 1H, 13C NMR spectroscopy- one dimensional TOCSY (total correlation spectroscopy) and NOESY (nuclear Overhauser effect spectroscopy); HMBC (heteronuclear multiple bond coherence), HMQC (heteronuclear multiple quantum correlation) spectra.
Protein Glycosylation linked (PGL) gene(s)
OST Gene NamePglB
OST ProGT IDProGT7
Characterized Accessory Gene(s)PglA, PglJ, PglH, PglI, PglC are glycosyltransferases involved in the heptasaccharide assembly. PglFED are the bacillosamine biosynthetic enzymes. PglK is a flippase.
Accessory Gene(s)Progt IDProGT8.1-ProGT8.9
Literature
Additional CommentSequon feature: The consensus sequence for the C jejuni PglB is D/E-X'-N-X"-S/T (where X' and X" stand for any amino acid except proline) which is glycosylated when located in flexible, exposed structural elements. Tripeptide sequence NLT too has been found to be modified in vitro.
Year of Identification2002
Year of Identification Month Wise2002.11.29
Year of Validation 2002
ReferenceScott NE, Parker BL, Connolly AM, Paulech J, Edwards AV, Crossett B, Falconer L, Kolarich D, Djordjevic SP, Højrup P, Packer NH, Larsen MR, Cordwell SJ. (2011) Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni. Mol Cell Proteomics. 2011 Feb;10(2):M000031-MCP201.
AuthorScott NE, Parker BL, Connolly AM, Paulech J, Edwards AV, Crossett B, Falconer L, Kolarich D, Djordjevic SP, Højrup P, Packer NH, Larsen MR, Cordwell SJ
Research GroupSchool of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia
Corresponding Author Cordwell SJ
ContactSchool of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia
Reference Young, N.M., Brisson, J.R., Kelly, J., Watson, D.C., Tessier, L., Lanthier, P.H., Jarrell, H.C., Cadotte, N., St Michael, F., Aberg, E. et al. (2002) Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni. J Biol Chem, 277, 42530-42539. [PubMed: 12186869]
Author Young, N.M., Brisson, J.R., Kelly, J., Watson, D.C., Tessier, L., Lanthier, P.H., Jarrell, H.C., Cadotte, N., St Michael, F., Aberg, E. et al.
Research GroupInstitute for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada. young@nrc.ca
Corresponding Author Young, N.M,St Michael,
ContactInstitute for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada. young@nrc.ca
Reference Olivier, N.B., Chen, M.M., Behr, J.R. and Imperiali, B. (2006) In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system. Biochemistry, 45, 13659-13669. [PubMed: 17087520]
Author Imperiali, B.
Research GroupDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.
Corresponding Author Olivier, N.B., Chen, M.M., Behr, J.R. Imperiali, B.
ContactDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.
Reference1) Maita, 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 GroupInstitute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, Switzerland.
Corresponding Author Kohda, D
ContactInstitute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, Switzerland.
Reference Rangarajan, E.S., Bhatia, S., Watson, D.C., Munger, C., Cygler, M., Matte, A. and Young, N.M. (2007) Structural context for protein N-glycosylation in bacteria: The structure of PEB3, an adhesin from Campylobacter jejuni. Protein Sci, 16, 990-995. [PubMed: 17456748]
Author Rangarajan, E.S., Bhatia, S., Watson, D.C., Munger, C., Cygler, M., Matte, A. Young, N.M.
Research GroupDepartment of Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada.
Corresponding Author Young, N.M.
ContactDepartment of Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada.
Reference Rangarajan, E.S., Bhatia, S., Watson, D.C., Munger, C., Cygler, M., Matte, A. and Young, N.M. (2007) Structural context for protein N-glycosylation in bacteria: The structure of PEB3, an adhesin from Campylobacter jejuni. Protein Sci, 16, 990-995. [PubMed: 17456748]
Author Rangarajan, E.S., Bhatia, S., Watson, D.C., Munger, C., Cygler, M., Matte, A. Young, N.M.
Research GroupDepartment of Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada.
Corresponding Author Young, N.M.
ContactDepartment of Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada.
Reference Linton, D., Allan, E., Karlyshev, A.V., Cronshaw, A.D. and Wren, B.W. (2002) Identification of N-acetylgalactosamine-containing glycoproteins PEB3 and CgpA in Campylobacter jejuni. Mol Microbiol, 43, 497-508. [PubMed: 11985725]
Author Linton, D., Allan, E., Karlyshev, A.V., Cronshaw, A.D. Wren, B.W.
Research GroupDepartment of Infectious and Tropical Diseases,
Corresponding Author Wren, B.W.
ContactDepartment of Infectious and Tropical Diseases,