ProGP220

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ProGP ID ProGP220
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 NameCj0114
NCBI Gene ID 904445
GenBank Gene Sequence 904445
Protein Information
Protein NameCj0114
UniProtKB/SwissProt ID Q0PC23
NCBI RefSeq YP_002343574.1
EMBL-CDSCAL34285.1
UniProtKB Sequence >tr|Q0PC23|Q0PC23_CAMJE Putative periplasmic protein OS=Campylobacter jejuni GN=Cj0114 PE=3 SV=1 MKKIFTVALLGATLLYAESSAFGAGDITSNSSYGLTSNEKLFKEKLDNLNNENIQTNARI NEINERIEGLQSTLEGINSQYAKSNSRLSQVEENNQNIENNFTSEIQKLKAYVEESRKIQ EANNKQVKKVLAELSSLVDAINANYVSKNELNDANLSVKTITPSVVVSTTDSNSTIENNN TQNTQDDKAKQIDESWKKKKNNEILELAIKDVDKNAFEDSKAKLNFLITKQYKPARANFW LGEIEYKQKNYNNAIVYYKKSSSLSTKGDYFPKLLYHTAISLDKTGDTKTANGFYKALKT NYPNSPEAKASPNRK
Sequence length 315 AA
Subcellular LocationPutative periplasmic
Glycosylation Status
Glycosylation Type N- (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN101
Experimentally Validated Glycosite(s ) in Mature ProteinN101
Glycosite(s) Annotated Protein Sequence >tr|Q0PC23|Q0PC23_CAMJE Putative periplasmic protein OS=Campylobacter jejuni GN=Cj0114 PE=3 SV=1 MKKIFTVALLGATLLYAESSAFGAGDITSNSSYGLTSNEKLFKEKLDNLNNENIQTNARI NEINERIEGLQSTLEGINSQYAKSNSRLSQVEENNQNIENN*(101)FTSEIQKLKAYVEESRKIQ EANNKQVKKVLAELSSLVDAINANYVSKNELNDANLSVKTITPSVVVSTTDSNSTIENNN TQNTQDDKAKQIDESWKKKKNNEILELAIKDVDKNAFEDSKAKLNFLITKQYKPARANFW LGEIEYKQKNYNNAIVYYKKSSSLSTKGDYFPKLLYHTAISLDKTGDTKTANGFYKALKT NYPNSPEAKASPNRK
Sequence Around Glycosites (21 AA) VEENNQNIENNFTSEIQKLKA
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
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.
Literature
Year of Identification2002
Year of Identification Month Wise2002.11.29
Year of Validation 2002
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 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.
ReferenceOlivier, 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 GroupDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.
Corresponding Author Imperiali, B.
ContactDepartment 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., 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.
Corresponding Author Aberg, E.
ContactInstitute for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada.
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