ProGP323

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ProGP ID ProGP323
Validation Status Characterized
Organism Information
Organism NameCampylobacter jejuni serotype O:23/36 (strain 81-176) /JHH1
Domain Bacteria
Classification Family: Campylobacteraceae
Order: Campylobacterales
Class: Epsilonproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 354242
Genome Sequence(s)
GenBank CP000538.1
EMBL CP000538
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 (CJJ81176_1002)
NCBI Gene ID 4682683
GenBank Gene Sequence 4682683
Protein Information
Protein NameJlpA (42-45 kDa antigen)
UniProtKB/SwissProt ID A1VZX2
NCBI RefSeq YP_001000663.1
EMBL-CDSEAQ72196.1
UniProtKB Sequence >tr|A1VZX2|A1VZX2_CAMJJ Surface-exposed lipoprotein OS=Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) GN=jlpA PE=4 SV=1 MKKGIFLSIGIAVLFSACGNSIDEKTVKKYENQLNQTVKQEIASLSQDSGIKIEFSDFKC NADGDFIACLSPNFKTLAKDNNDEYQELFQAKNIKIRSNEIYKGETNTSISIKEYYNDLF KNQKSIQSNLVFEDFKLGEKVVSDINASLFQQDPKISSFINKLSSDSYTLSFDNSINKQE NNYLDNLDIKFYNAKLNFNTNLNINLKEDLLNYLDSKGIKFNTQTLAMDEQAINELLNMV NYEQASDFSNTIQKYIILNNFKIDSTLKTEGVFSSYIATAKENLQTLKAQSQNEEQALIF DKALAILNNITQNDDYKLNLDLKFKNIPVSDYSTQGIDSIEKLSINNQDATEALKIILPF IMFSMLMGGASF
Sequence length 372 AA
Subcellular LocationSurface
Function Surface-associated lipoprotein that is antigenic. Promotes adherence to epithelial cells, potentially via interactions with surface-exposed hsp 90-α. Role in colonization of chicken.
Glycosylation Status
Glycosylation Type N (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN146, N107 or N146 only
Experimentally Validated Glycosite(s ) in Mature ProteinN146, N107 or N146 only
Glycosite(s) Annotated Protein Sequence >tr|A1VZX2|A1VZX2_CAMJJ Surface-exposed lipoprotein OS=Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) GN=jlpA PE=4 SV=1 MKKGIFLSIGIAVLFSACGNSIDEKTVKKYENQLNQTVKQEIASLSQDSGIKIEFSDFKC NADGDFIACLSPNFKTLAKDNNDEYQELFQAKNIKIRSNEIYKGETN*(107)TSISIKEYYNDLF KNQKSIQSNLVFEDFKLGEKVVSDIN*(146)ASLFQQDPKISSFINKLSSDSYTLSFDNSINKQE NNYLDNLDIKFYNAKLNFNTNLNINLKEDLLNYLDSKGIKFNTQTLAMDEQAINELLNMV NYEQASDFSNTIQKYIILNNFKIDSTLKTEGVFSSYIATAKENLQTLKAQSQNEEQALIF DKALAILNNITQNDDYKLNLDLKFKNIPVSDYSTQGIDSIEKLSINNQDATEALKIILPF IMFSMLMGGASF
Sequence Around Glycosites (21 AA) RSNEIYKGETNTSISIKEYYN
KLGEKVVSDINASLFQQDPKI
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionSBA (soybean agglutinin) affinity chromatography and detection of multiple bands on Western blot
Technique(s) used for Glycosylated Residue(s) Detection ESI/MS-MS (electrospray-ionization-tandem mass spectrometry)
Protein Glycosylation- Implication Glycosylation is not required for antigenicity.
Glycan Information
Glycan Annotation Linkage: Bac-Asn.
1406 Da heptasaccharide composed of HexNAc-HexNAc-[Hex-]HexNAc-HexNAc-HexNAc-Bac-N-Asn-Xaa, where Bac is bacillosamine, 2,4-diacetamido-2,4,6-trideoxyglucopyranose.
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 IDProGT6
Predicted Accessory Gene(s)Putative glycosyltransferases involved are PglA, PglC, PglD, PglE, PglF, PglG.
Accessory Gene(s)Progt IDProGT6.1-ProGT6.2
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 Identification2009
Year of Identification Month Wise2009.1
Year of Validation 2009
Reference Scott, N.E., Bogema, D.R., Connolly, A.M., Falconer, L., Djordjevic, S.P. and Cordwell, S.J. (2009) Mass spectrometric characterization of the surface-associated 42 kDa lipoprotein JlpA as a glycosylated antigen in strains of Campylobacter jejuni. J Proteome Res, 8, 4654-4664. [PubMed: 19689120]
Author Scott, N.E., Bogema, D.R., Connolly, A.M., Falconer, L., Djordjevic, S.P. Cordwell, S.J.
Research GroupSchool of Molecular and Microbial Biosciences, The University of Sydney, Australia 2006, NSW.
Corresponding Author Cordwell, S.J.
ContactSchool of Molecular and Microbial Biosciences, The University of Sydney, Australia 2006, NSW.
Reference Scott, N.E., Bogema, D.R., Connolly, A.M., Falconer, L., Djordjevic, S.P. and Cordwell, S.J. (2009) Mass spectrometric characterization of the surface-associated 42 kDa lipoprotein JlpA as a glycosylated antigen in strains of Campylobacter jejuni. J Proteome Res, 8, 4654-4664. [PubMed: 19689120]
Author Scott, N.E., Bogema, D.R., Connolly, A.M., Falconer, L., Djordjevic, S.P. Cordwell, S.J.
Research GroupSchool of Molecular and Microbial Biosciences, The University of Sydney, Australia 2006, NSW.
Corresponding Author Cordwell, S.J.
ContactSchool of Molecular and Microbial Biosciences, The University of Sydney, Australia 2006, NSW.
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]
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 Szymanski, C.M., Burr, D.H. and Guerry, P. (2002) Campylobacter protein glycosylation affects host cell interactions. Infect Immun, 70, 2242-2244. [Pubmed: 11895996]
Author Guerry, P.
Research GroupEnteric Diseases Program, Naval Medical Research Center, Silver Spring, Marland 20910-7500, USA.
Corresponding Author Szymanski, C.M., Burr, D.H. Guerry, P.
ContactEnteric Diseases Program, Naval Medical Research Center, Silver Spring, Marland 20910-7500, USA.