ProGP383 (Uncharacterized metallophosphoesterase)

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ProGP ID ProGP383 (Uncharacterized metallophosphoesterase)
Validation Status Characterized
Organism Information
Organism NameCampylobacter jejuni HB93-13
Domain Bacteria
Classification Family: Campylobacteraceae
Order: "Campylobacterales"
Class: "Epsilonproteobacteria"
Division or phylum: "Proteobacteria"
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 Namecj0846
NCBI Gene ID 905145
GenBank Gene Sequence NC_002163.1.
Protein Information
Protein NameUncharacterized metallophosphoesterase
UniProtKB/SwissProt ID Q9PP77
NCBI RefSeq WP_002871823.1
EMBL-CDSCAL34974.1.
UniProtKB Sequence >sp|Q9PP77|Y846_CAMJE Uncharacterized metallophosphoesterase Cj0846 OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=Cj0846 PE=3 SV=1 MIFLIFSFIVLLIFGLANVYIYKRLIKKITLFKYFYKIFSFIFIVLFLAQAVFLIFRRDE YLSDTWYEILAMFYAPTYCLFFMTLAWDFVKLILALMGKRDKTYNLILRLIFELSLIVLS VFLIYASINNALKTPEVKSVDVEIPNLKKDLKIVMLTDIHLGKNLHENFLDKLITKVNLQ SPDMVVIVGDLIDTNPKDLKNYISKLNDFNSTYGTFYALGNHEYYHGINEVLDLLRKHTN MKILVNQNLDLGFIDIAGLGDLAGLDRGLYAPDLARIKVDLNTSKASILLTHQPKTALLY DLSDFDLVLSGHTHGGQIFPFMFLVKLQQGFVHGLYDLGEKTKLYVSSGAGFWGPSLRVF APSEIVILNLKGKK
Sequence length 374 AA
Glycosylation Status
Glycosylation Type N- (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN282
Glycosite(s) Annotated Protein Sequence >sp|Q9PP77|Y846_CAMJE Uncharacterized metallophosphoesterase Cj0846 OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=Cj0846 PE=3 SV=1 MIFLIFSFIVLLIFGLANVYIYKRLIKKITLFKYFYKIFSFIFIVLFLAQAVFLIFRRDE YLSDTWYEILAMFYAPTYCLFFMTLAWDFVKLILALMGKRDKTYNLILRLIFELSLIVLS VFLIYASINNALKTPEVKSVDVEIPNLKKDLKIVMLTDIHLGKNLHENFLDKLITKVNLQ SPDMVVIVGDLIDTNPKDLKNYISKLNDFNSTYGTFYALGNHEYYHGINEVLDLLRKHTN MKILVNQNLDLGFIDIAGLGDLAGLDRGLYAPDLARIKVDLN*(282)TSKASILLTHQPKTALLY DLSDFDLVLSGHTHGGQIFPFMFLVKLQQGFVHGLYDLGEKTKLYVSSGAGFWGPSLRVF APSEIVILNLKGKK
Sequence Around Glycosites (21 AA) PDLARIKVDLNTSKASILLTH
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-(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 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
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., 10(2):M000031-MCP201. [PubMed: 20360033]
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