ProGP224

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ProGP ID ProGP224
Validation Status Characterized
Organism Information
Organism NameCampylobacter jejuni NCTC 11168 serotype O:2
Domain Bacteria
Classification Family: Campylobacteraceae
Order: Campylobacterales
Class: Epsilonproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 192222
Genome Sequence(s)
GenBank AL111168.1
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 NameCj0143c
NCBI Gene ID 904476
GenBank Gene Sequence 904476
Protein Information
Protein NameZnuA
UniProtKB/SwissProt ID Q0PBZ4
NCBI RefSeq YP_002343603.1
EMBL-CDSCAL34314.1
UniProtKB Sequence >tr|Q0PBZ4|Q0PBZ4_CAMJE Putative periplasmic solute binding protein for ABC transport system OS=Campylobacter jejuni GN=Cj0143c PE=3 SV=1 MKKIILFILSLGIFYTFTQAKNLEQEQNTSSNLVSVSIAPQAFFVKKIAANTLDVNVILP PNSNEHNFEFKPSTMKKLEKSDIYFTIGLEFEKVFTDKFKQNFPKLQVINMQKNIALIQT HDTHEHSHEHEHHEHGHFDPHTWLDPILVQTMALNIYDTLIQKYPQNENLYKENLDKFLA ELDSLNLQIASKLEKLKNREFVVYHPSWTYFAKRYNLTQIPVEILGKEPKSKDLQKLITL MKDKNLKVIFVQNGFPENAAKTLAKECDAKIYKIDHLSYDWENELLKTADAFSHNL
Sequence length 296 AA
Subcellular LocationPeriplasmic
Function Metallochaperone essential for C. jejuni growth in Zn-limiting media and for chick cecal colonization.
Glycosylation Status
Glycosylation Type N- (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN28
Experimentally Validated Glycosite(s ) in Mature ProteinN28
Glycosite(s) Annotated Protein Sequence >tr|Q0PBZ4|Q0PBZ4_CAMJE Putative periplasmic solute binding protein for ABC transport system OS=Campylobacter jejuni GN=Cj0143c PE=3 SV=1 MKKIILFILSLGIFYTFTQAKNLEQEQN*(28)TSSNLVSVSIAPQAFFVKKIAANTLDVNVILP PNSNEHNFEFKPSTMKKLEKSDIYFTIGLEFEKVFTDKFKQNFPKLQVINMQKNIALIQT HDTHEHSHEHEHHEHGHFDPHTWLDPILVQTMALNIYDTLIQKYPQNENLYKENLDKFLA ELDSLNLQIASKLEKLKNREFVVYHPSWTYFAKRYNLTQIPVEILGKEPKSKDLQKLITL MKDKNLKVIFVQNGFPENAAKTLAKECDAKIYKIDHLSYDWENELLKTADAFSHNL
Sequence Around Glycosites (21 AA) TQAKNLEQEQNTSSNLVSVSI
Technique(s) used for Glycosylation DetectionSBA (soybean agglutinin) lectin-agarose affinity chromatography
Technique(s) used for Glycosylated Residue(s) Detection Site-directed mutagenesis
Glycan Information
Glycan Annotation Linkage: Bac-Asn.
1406 Da heptasaccharide composed of GalNAc-α1,4-GalNAc-α1,4-[Glcβ1,3-]GalNAc-α1,4-GalNAc-α1,4-GalNAc-α1,3-Bac-β1,N-Asn-Xaa, where Bac is bacillosamine, 2,4-diacetamido-2,4,6-trideoxyglucopyranose.
BCSDB ID23625
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 IDProGT7
Characterized Accessory Gene(s)PglA, PglJ, PglH, PglI, PglC are glycosyltransferases involved in the heptasaccharide assembly. PglFED are the bacillosamine biosynthetic enzymes. PglK is a flippase.
Accessory Gene(s)Progt IDProGT8.1-ProGT8.9
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 Identification2002
Year of Identification Month Wise2002.11.29
Year of Validation 2009
ReferenceMaita, 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.
ReferenceDavis, L.M., Kakuda, T. and DiRita, V.J. (2009) A Campylobacter jejuni znuA orthologue is essential for growth in low-zinc environments and chick colonization. J Bacteriol, 191, 1631-1640. [PubMed: 19103921]
AuthorDavis LM1, Kakuda T, DiRita VJ.
Research GroupDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, 48109, USA
Corresponding Author DiRita VJ.
ContactDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, 48109, USA
ReferenceOlivier, N.B., Chen, M.M., Behr, J.R. and Imperiali, B. (2006) In vitro biosynthesis of UDP-N,N-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system. Biochemistry, 45, 13659-13669. [PubMed: 17087520]
Author Olivier, N.B., Chen, M.M., Behr, J.R. Imperiali, B.
Research GroupDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.
ContactDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.
ReferenceYoung, N.M., Brisson, J.R., Kelly, J., Watson, D.C., Tessier, L., Lanthier, P.H., Jarrell, H.C., Cadotte, N., St Michael, F., Aberg, E. et al. (2002) Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni. J Biol Chem, 277, 42530-42539. [PubMed: 12186869]
Author Young, N.M., Brisson, J.R., Kelly, J., Watson, D.C., Tessier, L., Lanthier, P.H., Jarrell, H.C., Cadotte, N., St Michael, F., Aberg, E. et al.
Research GroupInstitute for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada. young@nrc.ca
Corresponding Author N. Martin Young
ContactInstitute for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada. young@nrc.ca
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. 2011 Feb;10(2):M000031-MCP201.
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