ProGP236 (HisJ)
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| ProGP ID | ProGP236 (HisJ) |
| Validation Status | Characterized |
| Organism Information | |
| Organism Name | Campylobacter jejuni NCTC 11168 serotype O:2 |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria Class : Epsilonproteobacteria Orders : Campylobacterales Family : Campylobacteraceae Genus : Campylobacter Species : jejuni Subspecies : jejuni Strain : NCTC 11168 serotype O:2 |
| Taxonomic ID (NCBI) | 192222 |
| Genome Information | |
| 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 Name | Cj0734c (hisJ) |
| NCBI Gene ID | 905052 |
| GenBank Gene Sequence | NC_002163 |
| Protein Information | |
| Protein Name | HisJ |
| UniProtKB/SwissProt ID | Q46125 |
| NCBI RefSeq | YP_002344152.1 |
| EMBL-CDS | CAL34871.1 |
| 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 Location | Periplasm |
| Function | A component of the histidine uptake system. |
| Glycosylation Status | |
| Glycosylation Type | N- (Asn) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | N29 |
| Experimentally Validated Glycosite(s ) in Mature Protein | N29 |
| 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 |
| Technique(s) used for Glycosylation Detection | Immunoblot 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 Name | PglB |
| Additional Comment | Glycosylation 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). |
| Literature | |
| Year of Identification | 2005 |
| Year of Identification Month Wise | 2005.4.15 |
| Year of Validation | 2005 |
| Reference | Maita, 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 |
| Contact | Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan. |
| Reference | Nita-Lazar, M., Wacker, M., Schegg, B., Amber, S. and Aebi, M., 2005. The NXS/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation. Glycobiology, 15(4), pp.361-367. |
| Corresponding Author | Markus Aebi |
| Contact | Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology, Zürich, CH-8092 Zürich, Switzerland. |
| Reference | Scott, N.E., Parker, B.L., Connolly, A.M., Paulech, J., Edwards, A.V., Crossett, B., Falconer, L., Kolarich, D., Djordjevic, S.P., Højrup, P. and Packer, N.H., 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. Molecular & cellular proteomics, 10(2), pp.S1-S18. |
| Corresponding Author | Stuart J. Cordwell |
| Contact | School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia |