ProGP222

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ProGP ID ProGP222
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 NameCj1496c
NCBI Gene ID 906007
GenBank Gene Sequence 906007
Protein Information
Protein NameCj1496c
UniProtKB/SwissProt ID Q0P8C1
NCBI RefSeq YP_002344876.1
EMBL-CDSCAL35603.1
UniProtKB Sequence >tr|Q0P8C1|Q0P8C1_CAMJE Putative periplasmic protein OS=Campylobacter jejuni GN=Cj1496c PE=1 SV=1 MIKKFILLVFISSVVFGAEQDCEQYFEARKAQIELQTREFDEARQSLEAYKASFEALQKE RLENLEKKEAEVNATLAKIEELKLENARLVEEQQKILNSINDKTQGRVKEIYSQMKDAAI ADVLSQMDAEDASKIMLSLESRKISGVLSKMDPKKASELTLLLKNLDNNASN
Sequence length 172 AA
Subcellular LocationPriplasm
Function Required for the attachment and/or invasion to INT-407 intestinal epithelial cells and the colonization of the chick gastrointestinal tract.
Glycosylation Status
Glycosylation Type N (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN73, N169
Experimentally Validated Glycosite(s ) in Mature ProteinN73, N169
Glycosite(s) Annotated Protein Sequence >tr|Q0P8C1|Q0P8C1_CAMJE Putative periplasmic protein OS=Campylobacter jejuni GN=Cj1496c PE=1 SV=1 MIKKFILLVFISSVVFGAEQDCEQYFEARKAQIELQTREFDEARQSLEAYKASFEALQKE RLENLEKKEAEVN*(73)ATLAKIEELKLENARLVEEQQKILNSINDKTQGRVKEIYSQMKDAAI ADVLSQMDAEDASKIMLSLESRKISGVLSKMDPKKASELTLLLKNLDNN*(169)ASN
Sequence Around Glycosites (21 AA) ENLEKKEAEVNATLAKIEELK
LTLLLKNLDNNASN
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionSBA (soybean agglutinin) lectin-agarose affinity chromatography
Technique(s) used for Glycosylated Residue(s) Detection Site-specific mutagenesis combined with Western blot analysis
Protein Glycosylation- Implication Glycans are not directly involved in the function of Cj1496c.
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 2006
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 Yurist-Doutsch, S., Magidovich, H., Ventura, V.V., Hitchen, P.G., Dell, A. and Eichler, J
Research GroupInstitute for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada. young@nrc.ca
Corresponding Author N. Martin Young
ContactInstitute for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada. young@nrc.ca
Reference Kakuda, T. and DiRita, V.J. (2006) Cj1496c encodes a Campylobacter jejuni glycoprotein that influences invasion of human epithelial cells and colonization of the chick gastrointestinal tract. Infect Immun, 74, 4715-4723. [PubMed: 16861659]
Author Kakuda, T. DiRita, V.J.
Research GroupUnit for Laboratory Animal Medicine and Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.
Corresponding Author DiRita, V.J.
ContactUnit for Laboratory Animal Medicine and Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.
Reference Kakuda, T. and DiRita, V.J. (2006) Cj1496c encodes a Campylobacter jejuni glycoprotein that influences invasion of human epithelial cells and colonization of the chick gastrointestinal tract. Infect Immun, 74, 4715-4723. [PubMed: 16861659]
Author Kakuda, T. DiRita, V.J.
Research GroupUnit for Laboratory Animal Medicine and Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA
Corresponding Author DiRita, V.J.
ContactUnit for Laboratory Animal Medicine and Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA
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.