ProGP222 (PEB3)
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ProGP ID | ProGP222 (PEB3) |
Validation Status | Characterized |
Organism Information | |
Organism Name | Campylobacter jejuni NCTC 11168 serotype O:2 |
Domain | Bacteria |
Classification | Family: Campylobacteraceae Order: Campylobacterales Class: Epsilonproteobacteria Division or phylum: "Proteobacteria" |
Taxonomic ID (NCBI) | 192222 |
Genome Information | |
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 Name | Cj0289c |
NCBI Gene ID | 904613 |
GenBank Gene Sequence | NC_002163 |
Protein Information | |
Protein Name | PEB3 |
UniProtKB/SwissProt ID | Q0PBL7 |
NCBI RefSeq | YP_002343730.1 |
EMBL-CDS | CAL34442.1 |
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 Location | Surface |
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 Protein | N90 |
Experimentally Validated Glycosite(s ) in Mature Protein | N90 |
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 |
Technique(s) used for Glycosylation Detection | SBA (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 ID | 23625 |
GlyTouCan | G58528CE |
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 Name | PglB |
OST ProGT ID | ProGT10 (PglB) |
Literature | |
Reference | Maita, 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 |
Contact | Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan. |
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 science, 16(5), pp.990-995. |
Corresponding Author | N Martin Young |
Contact | Institute for Biological Sciences, NRC, Ottawa, Ontario K1A 0R6, Canad |
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(45), pp.13659-13669. |
Corresponding Author | Barbara Imperiali |
Contact | Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA. |
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. Molecular microbiology, 43(2), pp.497-508. |
Corresponding Author | Dennis Linton |
Contact | Department of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, UK. |
Reference | Young, N.M., Brisson, J.R., Kelly, J., Watson, D.C., Tessier, L., Lanthier, P.H., Jarrell, H.C., Cadotte, N., Michael, F.S., Aberg, E. and Szymanski, C.M., 2002. Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni. Journal of Biological Chemistry, 277(45), pp.42530-42539. |
Corresponding Author | N Martin Young |
Contact | Institute for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada. |
Reference | Scott, N.E., Parker, B.L., Connolly, A.M., Paulech, J., Edwards, A.V., Crossett, B., Falconer, L., Kolarich, D., Djordjevic, S.P., Højrup, P. and Packer, N.H., 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. Molecular & cellular proteomics, 10(2), pp.S1-S18. |
Corresponding Author | Stuart J Cordwell |
Contact | School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia |
Reference | 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 Group | Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, Switzerland. |
Corresponding Author | Kohda, D |
Contact | Institute 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 Group | Department of Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada. |
Corresponding Author | Young, N.M. |
Contact | Department of Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada. |
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 | Olivier, N.B., Chen, M.M., Behr, J.R. Imperiali, B. |
Research Group | Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA. |
Corresponding Author | Imperiali, B. |
Contact | Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA. |
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 Group | Department of Infectious and Tropical Diseases, |
Corresponding Author | Wren, B.W. |
Contact | Department of Infectious and Tropical Diseases, |
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 Group | Institute for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada. |
Corresponding Author | Young, N.M,St Michael, |
Contact | Institute for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada. |
Reference | Scott 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, 10(2), M000031-MCP201. [PubMed: 20360033] |
Author | Scott 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 Group | School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia |
Corresponding Author | Cordwell SJ |
Contact | School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia |