ProGP220 (Cj0200c)
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| ProGP ID | ProGP220 (Cj0200c) |
| 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 | Cj0200c |
| NCBI Gene ID | 904543 |
| GenBank Gene Sequence | NC_002163 |
| Protein Information | |
| Protein Name | Cj0200c |
| UniProtKB/SwissProt ID | Q0PBT9 |
| NCBI RefSeq | YP_002343658.1 |
| EMBL-CDS | CAL34369.1 |
| UniProtKB Sequence | >tr|Q0PBT9|Q0PBT9_CAMJE Putative periplasmic protein OS=Campylobacter jejuni GN=Cj0200c PE=1 SV=1 MKKSILFASALLASSMLFADSLKLEGTIAQIYDNNKTLLIDSIYGGQMAIKVLPNTEIEM DDCGIFGTDKDGTFKDLQVGNFLESKISYGTPATPNTQAIPVARKIEIQCYKKAY |
| Sequence length | 115 AA |
| Subcellular Location | Putative periplasmic |
| Glycosylation Status | |
| Glycosylation Type | N- (Asn) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | N35 |
| Experimentally Validated Glycosite(s ) in Mature Protein | N35 |
| Glycosite(s) Annotated Protein Sequence | >tr|Q0PBT9|Q0PBT9_CAMJE Putative periplasmic protein OS=Campylobacter jejuni GN=Cj0200c PE=1 SV=1 MKKSILFASALLASSMLFADSLKLEGTIAQIYDNN*(35)KTLLIDSIYGGQMAIKVLPNTEIEM DDCGIFGTDKDGTFKDLQVGNFLESKISYGTPATPNTQAIPVARKIEIQCYKKAY |
| Sequence Around Glycosites (21 AA) | EGTIAQIYDNNKTLLIDSIYG |
| 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 | 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 | 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 |