ProGP257

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ProGP ID ProGP257
Validation Status Characterized
Organism Information
Organism NameCampylobacter jejuni NCTC 11168
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 NameCj0365c (CmeABC operon)
NCBI Gene ID 904688
GenBank Gene Sequence NC_002163.1. 
Protein Information
Protein NameCmeC
UniProtKB/SwissProt ID Q0PBE5
NCBI RefSeq YP_002343802.1
EMBL-CDSCAL34515.1
UniProtKB Sequence >tr|Q0PBE5|Q0PBE5_CAMJE Outer membrane channel protein CmeC (Multidrug efflux system CmeABC) OS=Campylobacter jejuni GN=cmeC PE=4 SV=1 MNKIISISAIASFTLLISACSLSPNLNIPEANYSIDNKLGALSWEKENNSSITKNWWKDF DDENLNKVVDLALKNNNDLKLAFIHMEQAAAQLGIDFSSLLPKFDGSASGSRAKTAINAP SNRTGEVSYGNDFKMGLNLSYEIDLWGKYRDTYRASKSGFKASEYDYEAARLSVISNTVQ TYFNLVNAYENENALKEAYKSAKEIYRINDEKFQVGAVGEYELAQARANLESMALQYNEA KLNKENYLKALKILTSNDLNDILYKNQSYQVFNLKEFDIPTGISSTILLQRPDIGSSLEK LTQQNYLVGVARTAFLPSLSLTGLLGFESGDLDTLVKGGSKTWNIGGNFTLPIFHWGEIY QNVNLAKLNKDEAFVNYQNTLITAFGEIRYALVARKTIRLQYDNAQASEQSYKRIYEIAK ERYDIGEMSLQDYLEARQNWLNAAVAFNNIKYSYANSIVDVIKAFGGGFEQSEDTSKNIK EESKNLDMSFRE
Sequence length 492 AA
Subcellular LocationOuter membrane
Function Outer membrane component of a multidrug efflux pump (RND superfamily) involved in antibiotic resistance.
Glycosylation Status
Glycosylation Type N- (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN49
Glycosite(s) Annotated Protein Sequence >tr|Q0PBE5|Q0PBE5_CAMJE Outer membrane channel protein CmeC (Multidrug efflux system CmeABC) OS=Campylobacter jejuni GN=cmeC PE=4 SV=1 MNKIISISAIASFTLLISACSLSPNLNIPEANYSIDNKLGALSWEKENNSSITKN*(49)WWKDF DDENLNKVVDLALKNNNDLKLAFIHMEQAAAQLGIDFSSLLPKFDGSASGSRAKTAINAP SNRTGEVSYGNDFKMGLNLSYEIDLWGKYRDTYRASKSGFKASEYDYEAARLSVISNTVQ TYFNLVNAYENENALKEAYKSAKEIYRINDEKFQVGAVGEYELAQARANLESMALQYNEA KLNKENYLKALKILTSNDLNDILYKNQSYQVFNLKEFDIPTGISSTILLQRPDIGSSLEK LTQQNYLVGVARTAFLPSLSLTGLLGFESGDLDTLVKGGSKTWNIGGNFTLPIFHWGEIY QNVNLAKLNKDEAFVNYQNTLITAFGEIRYALVARKTIRLQYDNAQASEQSYKRIYEIAK ERYDIGEMSLQDYLEARQNWLNAAVAFNNIKYSYANSIVDVIKAFGGGFEQSEDTSKNIK EESKNLDMSFRE
Sequence Around Glycosites (21 AA) LGALSWEKENNSSITKNWWKD
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionZIC-HILIC enrichment
Technique(s) used for Glycosylated Residue(s) Detection Reversed Phase LC-Tandem CID/HCD-MS and CID/ETD-MS
Glycan Information
Glycan Annotation Heptasaccharide GalNAc- α1,4-GalNAc- α1,4-(Glc β1,3)-GalNAc- α1,4-GalNAc- α1,4-GalNAc- α1,3-Bac- β1 where Bac is bacillosamine (2,4-diacetamido-2,4,6-trideoxyglucopyranose)
BCSDB ID20059
Technique(s) used for Glycan Identification Reversed Phase LC-Tandem CID/HCD-MS
Literature
Year of Identification2007
Year of Identification Month Wise2007.09
Year of Validation 2011
ReferenceGuerry, P., Ewing, C.P., Schoenhofen, I.C. and Logan, S.M. (2007) Protein glycosylation in Campylobacter jejuni: partial suppression of pglF by mutation of pseC. J Bacteriol, 189, 6731-6733. [PubMed: 17631632]
Author Logan, S.M.
Research GroupEnteric Diseases Department, Naval Medical Research Center, 503 Robert Grant Ave., Silver Spring, MD 20910, USA
Corresponding Author Guerry, P., Ewing, C.P., Schoenhofen, I.C. Logan, S.M.
ContactEnteric Diseases Department, Naval Medical Research Center, 503 Robert Grant Ave., Silver Spring, MD 20910, USA
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