ProGP385 (Cj0983 (Putative lipoprotein))

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ProGP ID ProGP385 (Cj0983 (Putative lipoprotein))
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 NamejlpA
NCBI Gene ID 905274.
GenBank Gene Sequence NC_002163.1.
Protein Information
Protein NameCj0983 (Putative lipoprotein)
UniProtKB/SwissProt ID P45492
NCBI RefSeq WP_010891898.1
EMBL-CDSCAL35101.1.
UniProtKB Sequence >sp|P45492|Y983_CAMJE Uncharacterized lipoprotein Cj0983 OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=Cj0983 PE=3 SV=2 MKKGIFLSIGIAVLFSACGNSIDEKTVKKYENQLNQTVKQEIASLSQDSGIKIEFSDFKC NADGDFIACLSPNFKTLTKDNNDEYQELFQAKNIKIRSNEIYKGKANASISIKEYYNDLF KNQKSIQSNLVFEDFKLGEKVVSDINASLFQQDPKISSFINKLSSDSYTLSFDNSINKQE NNYLDNLDIKFYNAKLNFNTNLNINLKEDLLNYLDSKGIKFNTQTLVMDKQAINELLNIA NYEQASDFSNTIQKYIILNNFKIDSTLKTEGVFSSYIATAKENLQTLKAQSQNEEQALIF DKALAILNNITQNDDYKLNLDLKFKNIPVSDYSTQGIDSIEKLSINNQDATEALKIILPF IMFSMLMGGASF
Sequence length 372 AA
Glycosylation Status
Glycosylation Type N- (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN107 and N146
Glycosite(s) Annotated Protein Sequence >sp|P45492|Y983_CAMJE Uncharacterized lipoprotein Cj0983 OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=Cj0983 PE=3 SV=2 MKKGIFLSIGIAVLFSACGNSIDEKTVKKYENQLNQTVKQEIASLSQDSGIKIEFSDFKC NADGDFIACLSPNFKTLTKDNNDEYQELFQAKNIKIRSNEIYKGKAN*(107)ASISIKEYYNDLF KNQKSIQSNLVFEDFKLGEKVVSDIN*(146)ASLFQQDPKISSFINKLSSDSYTLSFDNSINKQE NNYLDNLDIKFYNAKLNFNTNLNINLKEDLLNYLDSKGIKFNTQTLVMDKQAINELLNIA NYEQASDFSNTIQKYIILNNFKIDSTLKTEGVFSSYIATAKENLQTLKAQSQNEEQALIF DKALAILNNITQNDDYKLNLDLKFKNIPVSDYSTQGIDSIEKLSINNQDATEALKIILPF IMFSMLMGGASF
Sequence Around Glycosites (21 AA) RSNEIYKGKANASISIKEYYN
KLGEKVVSDINASLFQQDPKI
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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-(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 Identification2011
Year of Identification Month Wise2011.2.10
Year of Validation 2011
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