ProGP237

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ProGP ID ProGP237
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 NameCj0734c (hisJ)
NCBI Gene ID 905052
GenBank Gene Sequence 905052
Protein Information
Protein NameHisJ
UniProtKB/SwissProt ID Q46125
NCBI RefSeq YP_002344152.1
EMBL-CDSCAL34871.1
UniProtKB Sequence >sp|Q46125|HISJ_CAMJE Histidine-binding protein OS=Campylobacter jejuni GN=hisJ PE=1 SV=1 MKKFLTAFLVAFTGLFLVACQNTKTENNASNEANTTLTLKVGTAPNYKPFNFKQDSKLTG FDTDLIEEIAKKNGIEIVWVETNFDGLIPALKSGKIDMIASAMSATDERRQSVDFTKPYY MSKNLYLKLKNNDSLQTKNDLEGKKIGVQLGTLQENTAKAIKNAQVQSNKDLNIAVLALK NNKIDAIVADQDTAKGFLAENPELVSFYQETDGGEGFSFAFDKNKQKDIIEIFNKGIDEA KTDGFYDTLIKKYELE
Sequence length 256 AA
Subcellular LocationPeriplasm
Function A component of the histidine uptake system.
Glycosylation Status
Glycosylation Type N (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN29
Experimentally Validated Glycosite(s ) in Mature ProteinN29
Glycosite(s) Annotated Protein Sequence >sp|Q46125|HISJ_CAMJE Histidine-binding protein OS=Campylobacter jejuni GN=hisJ PE=1 SV=1 MKKFLTAFLVAFTGLFLGACSDSKNKESN*(29)ASVELKVGTAPNYKPFNFKQDSKLTG FDTDLIEEIAKKNGIEIVWVETNFDGLIPALKSGKIDMIASAMSATDERRQSVDFTKPYY MSKNLYLKLKNNDSLQTKNDLEGKKIGVQLGTLQENTAKAIKNAQVQSNKDLNIAVLALK NNKIDAIVADQDTAKGFLAENPELVSFYQETDGGEGFSFAFDKNKQKDIIEIFNKGIDEA KTDGFYDTLIKKYELE
Sequence Around Glycosites (21 AA) ACSDSKNKESNASVELKVGTA
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionImmunoblot analysis using glycosylation-specific R12 antiserum, SBA (soybean agglutinin) lectin-agarose affinity chromatography, Slow/ aberrant migration on SDS-PAGE
Technique(s) used for Glycosylated Residue(s) Detection Site-directed mutagenesis (N28L)
Protein Glycosylation linked (PGL) gene(s)
OST Gene NamePglB
Literature
Additional CommentGlycosylation at sequon 28-N-A-S-30 and not at the other potential sequon 132-N-D-S-134 in glycosylation competent recombinant E.coli strain as well as in native host strain suggests for the first time that N-X-S/T sequon is required but not sufficient in case of campylobacter/ bacterial N glycosylation. Seat of glycosylation was found to be periplasm. N127 is experimentally proved (by site directed mutagenesis) as non-glycosylated sequon.
Sequence conflict has been observed at many places. Regarding the glycosite, it is from 18V to 38T → GACSDSKNKESNASVE (21 residues).
Year of Identification2005
Year of Identification Month Wise2005.4.15
Year of Validation 2005
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
Reference Nita-Lazar, M., Wacker, M., Schegg, B., Amber, S. and Aebi, M. (2005) The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation. Glycobiology, 15, 361-367. [PubMed: 15574802]
Author Nita-Lazar, M., Wacker, M., Schegg, B., Amber, S. Aebi, M.
Research GroupInstitute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, CH-8093 Zürich, Switzerland.
Corresponding Author Aebi, M.
ContactInstitute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, CH-8093 Zürich, Switzerland.
Reference Nita-Lazar, M., Wacker, M., Schegg, B., Amber, S. and Aebi, M. (2005) The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation. Glycobiology, 15, 361-367. [PubMed: 15574802]
Author Nita-Lazar, M., Wacker, M., Schegg, B., Amber, S. Aebi, M.
Research GroupInstitute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, CH-8093 Zürich, Switzerland.
Corresponding Author Aebi, M.
ContactInstitute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, CH-8093 Zürich, Switzerland.
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.