ProGP219

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ProGP ID ProGP219
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 NamecgpA (Cj1670c)
NCBI Gene ID 905945
GenBank Gene Sequence 905945
Protein Information
Protein NameCgpA
UniProtKB/SwissProt ID Q0P7V9
NCBI RefSeq YP_002345038.1
EMBL-CDSCAL35766.1
UniProtKB Sequence >tr|Q0P7V9|Q0P7V9_CAMJE Putative periplasmic protein OS=Campylobacter jejuni GN=cgpA PE=3 SV=1 MKTRILAIFFIFTSLLYADENPFKTDQNITLVAPPEFQKEEVKFNSSARILKSITFNYIN LDGSEDKIDLDVNKSIDWHDTYTISRFKSPDPSKVLDVSVTIPEKNSSKQESNSTANVEI PLQVAKIYDFISYAVYKNKIKLNTSDEMITDFSVGNPSKIVIDFRSKMISPTKNIRLSNS IFKRIDFGSHKGYYRLVIYLDGTYNYNIQKDATGYMINLL
Sequence length 220 AA
Subcellular LocationPutative periplasmic
Glycosylation Status
Glycosylation Type N (Asn) linked
Experimentally Validated Glycosite(s) in Full Length Protein(Signal peptide: 1-18) N28, N106, N113
Experimentally Validated Glycosite(s ) in Mature ProteinN10, N88, N95
Glycosite(s) Annotated Protein Sequence >tr|Q0P7V9|Q0P7V9_CAMJE Putative periplasmic protein OS=Campylobacter jejuni GN=cgpA PE=3 SV=1 MKTRILAIFFIFTSLLYADENPFKTDQN*(28)ITLVAPPEFQKEEVKFNSSARILKSITFNYIN LDGSEDKIDLDVNKSIDWHDTYTISRFKSPDPSKVLDVSVTIPEKN*(106)SSKQESN*(113)STANVEI PLQVAKIYDFISYAVYKNKIKLNTSDEMITDFSVGNPSKIVIDFRSKMISPTKNIRLSNS IFKRIDFGSHKGYYRLVIYLDGTYNYNIQKDATGYMINLL
Sequence Around Glycosites (21 AA) ADENPFKTDQNITLVAPPEFQ
LDVSVTIPEKNSSKQESNSTA
PEKNSSKQESNSTANVEIPLQ
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
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 2002
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
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]
2) 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 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.
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]
AuthorAberg, E.
Research GroupInstitute for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada. young@nrc.ca
Corresponding 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. Aberg, E.
ContactInstitute for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada. young@nrc.ca
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 GroupDepartment of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, UK. dennis.linton@lshtm.ac.uk
Corresponding Author Wren, B.W.
ContactDepartment of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, UK. dennis.linton@lshtm.ac.uk
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 GroupDepartment of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, UK
Corresponding Author Wren, B.W.
ContactDepartment of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, UK