ProGP323 (JlpA (42-45 kDa antigen))

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ProGP ID ProGP323 (JlpA (42-45 kDa antigen))
Validation Status Characterized
Organism Information
Organism NameCampylobacter jejuni serotype O:23/36 (strain 81-176) /JHH1
Domain Bacteria
Classification Phylum : Proteobacteria
Class : Epsilonproteobacteria
Orders : Campylobacterales
Family : Campylobacteraceae
Genus : Campylobacter
Species : jejuni
Subspecies : jejuni
Strain : 81-176
Taxonomic ID (NCBI) 354242
Genome Information
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)
GenBank Gene Sequence NC_008787.1
Protein Information
Protein NameJlpA (42-45 kDa antigen)
UniProtKB/SwissProt ID A0A0H3P9U7
NCBI RefSeq WP_009882608.1
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-. 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
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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 IDProGT9
Predicted Accessory Gene(s)Putative glycosyltransferases involved are PglA, PglC, PglD, PglE, PglF, PglG.
Accessory Gene(s)Progt IDProGT9.1,ProGT9.2
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.
Literature
Year of Identification2009
Year of Identification Month Wise2009.1
Year of Validation 2009
ReferenceMaita, N., Nyirenda, J., Igura, M., Kamishikiryo, J. and Kohda, D., 2010. Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases 2. Journal of Biological Chemistry, 285(7), pp.4941-4950.
Corresponding Author Daisuke Kohda
ContactDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan.
ReferenceScott, 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. Journal of proteome research, 8(10), pp.4654-4664.
Corresponding Author Stuart J Cordwell
ContactSchool of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia
ReferenceSzymanski, C.M., Burr, D.H. and Guerry, P., 2002. Campylobacter protein glycosylation affects host cell interactions. Infection and immunity, 70(4), pp.2242-2244.
Corresponding Author Christine M Szymanski
ContactEnteric Diseases Program, Naval Medical Research Center, Silver Spring, Marland 20910-7500, USA.