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 | Phylum : Proteobacteria Class : Epsilonproteobacteria Orders : Campylobacterales Family : Campylobacteraceae Genus : Campylobacter Species : jejuni Subspecies : jejuni Strain : NCTC 11168 serotype O:2 |
| 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 |
| 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 ID | ProGT10.1, ProGT10.2, Pro |
| Additional Comment | Sequon 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. |
| Literature | |
| Year of Identification | 2002 |
| Year of Identification Month Wise | 2002.11.29 |
| Year of Validation | 2002 |
| 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 |