ProGP361 (Putative mechanosensitive ion channel family protein)

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ProGP ID ProGP361 (Putative mechanosensitive ion channel family protein)
Validation Status Characterized
Organism Information
Organism NameCampylobacter jejuni HB93-13
Domain Bacteria
Classification Phylum : Proteobacteria
Class : Epsilonproteobacteria
Orders : Campylobacterales
Family : Campylobacteraceae
Genus : Campylobacter
Species : jejuni
Subspecies : jejuni
Strain : HB93-13
Taxonomic ID (NCBI) 192222
Genome Information
GenBank NC_002163.1
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 Namecj0238
NCBI Gene ID 904565
GenBank Gene Sequence NC_002163.1.
Protein Information
Protein NamePutative mechanosensitive ion channel family protein
UniProtKB/SwissProt ID Q0PBR6
NCBI RefSeq WP_002858655.1
EMBL-CDSCAL34393.1
UniProtKB Sequence >tr|Q0PBR6|Q0PBR6_CAMJE Putative mechanosensitive ion channel family protein OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=Cj0238 PE=4 SV=1 MKKIIFSLCFFILHLGAQEFKFIDANISKEDEGIYALVEKYVDLNNQIKEFKKNNDENSS TFNGILSEFEKDKKTILAKIPDMIVGQKINEEAVARFLKAKEKLLDVQKKNINKPYIYTD ATLNLVYFNIVESFYSSLFEVEKLFKNTASSEDLIATVDKAMENLQNSSNVNLDSFKSKI TNPEELEKITLKERYISNAVDSYSEILKYLRSNADLLESNYIFSLLELQVWIDRINEAIG VSFVNIGKIVISALVLVFFISLRRFFANIVYFFLVQLFYRNKNDVDDIKVIFIENIKKPV GFLLIVYAISLCLTIATYPAPLSVNLSNFFHIVYAVLIAWLILRMLDGYGVVLVSKLAQK SGKKEVVNLIIKILYFVIIIIALLYILAQLGFNISAIIASLGIGGLAVALAAKDIIANFF ASILLLFDNSFNQGDWVEVSGIEGTVVETGLRKTTIRTFDNCLVFLPNSTIMGANIKNWS KRRMGRHVRMYLGVGYDATPEKLEQCVKDLREFLHTSDLVAHDEDSALKYGDHTTKYRQN LVSINDLEGYKNACYVALSEFADSSINIELYFYIKEIGGKDFREARQSLMLEFMRIIEKN GLTFAFPSRSIYIENLPPLDLQAKAIK
Sequence length 627 AA
Glycosylation Status
Glycosylation Type N- (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN25 and N58
Glycosite(s) Annotated Protein Sequence >tr|Q0PBR6|Q0PBR6_CAMJE Putative mechanosensitive ion channel family protein OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=Cj0238 PE=4 SV=1 MKKIIFSLCFFILHLGAQEFKFIDAN*(25)ISKEDEGIYALVEKYVDLNNQIKEFKKNNDEN*(58)SS TFNGILSEFEKDKKTILAKIPDMIVGQKINEEAVARFLKAKEKLLDVQKKNINKPYIYTD ATLNLVYFNIVESFYSSLFEVEKLFKNTASSEDLIATVDKAMENLQNSSNVNLDSFKSKI TNPEELEKITLKERYISNAVDSYSEILKYLRSNADLLESNYIFSLLELQVWIDRINEAIG VSFVNIGKIVISALVLVFFISLRRFFANIVYFFLVQLFYRNKNDVDDIKVIFIENIKKPV GFLLIVYAISLCLTIATYPAPLSVNLSNFFHIVYAVLIAWLILRMLDGYGVVLVSKLAQK SGKKEVVNLIIKILYFVIIIIALLYILAQLGFNISAIIASLGIGGLAVALAAKDIIANFF ASILLLFDNSFNQGDWVEVSGIEGTVVETGLRKTTIRTFDNCLVFLPNSTIMGANIKNWS KRRMGRHVRMYLGVGYDATPEKLEQCVKDLREFLHTSDLVAHDEDSALKYGDHTTKYRQN LVSINDLEGYKNACYVALSEFADSSINIELYFYIKEIGGKDFREARQSLMLEFMRIIEKN GLTFAFPSRSIYIENLPPLDLQAKAIK
Sequence Around Glycosites (21 AA) GAQEFKFIDANISKEDEGIYA
IKEFKKNNDENSSTFNGILSE
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Technique(s) used for Glycosylation DetectionZIC-HILIC enrichment
Technique(s) used for Glycosylated Residue(s) Detection Reversed Phase LC-Tandem CID/HCD-MS
Glycan Information
Glycan Annotation Heptasaccharide GalNAc- α1,4-GalNAc- α1,4-(Glcβ1,3)-GalNAc- α1,4-GalNAc- α1,4-GalNAc- α1,3-Bac-β1 where Bac is bacillosamine (2,4-diacetamido-2,4,6-trideoxyglucopyranose)
BCSDB ID 20059
GlyTouCan G38348FF
Technique(s) used for Glycan Identification Reversed Phase LC-Tandem CID/HCD-MS
Literature
Year of Identification2011
Year of Identification Month Wise2011.2.10
Year of Validation 2011
ReferenceScott, 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
ContactSchool of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia