| Organism Information |
| Organism Name | Campylobacter Jejuni 81-176 |
| Clinical Implication | Pathogenic |
| 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 |
| Gene Bank | CP000538 |
| EMBL | CP000538 |
| Gene Information |
| Gene Name | pglB |
| Protein information |
| Protein Name | PglB |
| UniProtKB/ SwissProt ID | A0A0H3P9U9 |
| NCBI Ref Seq | WP_002853816.1 |
| UniProtKB Sequence | >tr|A0A0H3P9U9|A0A0H3P9U9_CAMJJ General glycosylation pathway protein OS=Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) GN=pglB PE=4 SV=1
MLKKEYLKNPYLVLFAMIVLAYVFSVLCRFYWIWWASEFNEYFFNNQLMIISNDGYAFAE
GARDMIAGFHQPNDLSYYGSSLSTLTYWLYKITPFSFESIILYMSTFLSSLVVIPIILLA
NEYKRPLMGFVAALLASIANSYYNRTMSGYYDTDMLVIVLPMFILFFMVRMILKKDFFSL
IALPLFIGIYLWWYPSSYTLNVALIGLFLIYTLIFHRKEKIFYIAVILSSLTLSNIAWFY
QSTIIVILFALFALEQKRLNFVIIGILASVTLIFLILSGGVDPILYQLKFYIFRSDESAN
LTQGFMYFNVNQTIQEVENVDLSEFMRRISGSEIVFLFSLFGFVWLLRKHKSMIMALPIL
VLGFLALKGGLRFTIYSVPVMALGFGFLLSEFKAILVKKYSQLTSNVCIVFATILTLAPV
FIHIYNYKAPTVFSQNEASLLNQLKNIANREDYVVTWWDYGYPVRYYSDVKTLVDGGKHL
GKDNFFPSFALSKDEQAAANMARLSVEYTEKSFYAPQNDILKTDILQAMMKDYNQSNVDL
FLASLSKPDFKIDTPKTRDIYLYMPARMSLIFSTVASFSFINLDTGVLDKPFTFSTAYPL
DVKNGEIYLSNGVVLSDDFRSFKIGDNVVSVNSIVEINSIKQGEYKITPIDDKAQFYIFY
LKDSAIPYAQFILMDKTMFNSAYVQMFFLGNYDKNLFDLVINSRDAKVFKLKI
|
| EMBL CDS | EAQ72203.1. |
| Sequence length | 713 AA |
| Subcellular Location | Membrane (Integral component of membrane) |
| String | 354242.Cjejjejuni_010100005965. |
| Potential Application | 1) Transfer of functional expression N-glycosylation system of Campylobacter jejuni in Escherichia coli could be used for the production of glycoconjugate vaccines in prokaryotic cells.
|
| Additional Information | 1) PglBCj is very relaxed specificity OST which utilizes a wide variety of the lipid-linked polysaccharide substrate.
2) PglBCj not only transfer the natural C. jejuni oligosaccharides, but also O antigen lipopolysaccharide of various Gram-negative bacteria and capsular antigen polysaccharides of Gram-positive bacteria. |
| Glycosyltransferase Information |
| Glycosylation Type | N- (Asn) linked |
| CAZY Family | GT66 |
| EC Number (BRENDA) | 2.4.1.- |
| Mechanism of Glycan Transfer | En bloc |
| Acceptor specificity Sequon_1 | Asp/Glu- Asn-Xaa-Ser/Thr |
| Donor Type | UndPP-GalNAc- 1,4-GalNAc- 1,4-(Glc 1,3)-Gal-NAc- 1,4- GalNAc- 1,4-GalNAc- 1,3-Bac |
| Donor Specificity | Lipid linked sugars |
| Accessory GT ID | ProGT9.1 |
| Glycan Information |
| Glycan transferred | Heptasaccharide (GalNAc- 1,4-GalNAc- 1,4-(Glc 1,3)-Gal-NAc- 1,4- GalNAc- 1,4-GalNAc- 1,3-Bac, where Bac is bacillosamine(2,4-diacetamido-2,4,6-trideoxygluose)) |
| Experimental_strategies | In vivo and In vitro |
| Acceptor Subtrate Information |
| Acceptor Substrate name | VirB10 protein |
| ProGPdb ID | ProGP232 |
| Acceptor Substrate name | JlpA |
| ProGPdb ID | ProGP323 |
| Litrature |
| Year Of Validation | 2002 |
| Reference | Wacker, M., Linton, D., Hitchen, P.G., Nita-Lazar, M., Haslam, S.M., North, S.J., Panico, M., Morris, H.R., Dell, A., Wren, B.W. and Aebi, M., 2002. N-linked glycosylation in Campylobacter jejuni and its functional transfer into Escherichia coli. Science, 298(5599), pp.1790-1793.
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| Corresponding Author | Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology, Zürich, CH-8092 Zürich, Switzerland.
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| Reference | Larsen, J.C., Szymanski, C. and Guerry, P., 2004. N-linked protein glycosylation is required for full competence in Campylobacter jejuni 81-176. Journal of bacteriology, 186(19), pp.6508-6514.
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| Corresponding Author | Department of Microbiology and Immunology, F. Edward Hebert School of Medicine, Uniformed Services University of the Health Sciences, Bethesda, Maryland, USA
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| Reference | Li, L., Woodward, R., Ding, Y., Liu, X.W., Yi, W., Bhatt, V.S., Chen, M., Zhang, L.W. and Wang, P.G., 2010. Overexpression and topology of bacterial oligosaccharyltransferase PglB. Biochemical and biophysical research communications, 394(4), pp.1069-1074.
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| Corresponding Author | National Glycoengineering Research Center and The State Key Laboratory of Microbial Technology, School of Life Sciences, Shandong University, Shandong 250100, China.
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| Reference | Ihssen, J., Haas, J., Kowarik, M., Wiesli, L., Wacker, M., Schwede, T. and Thöny-Meyer, L., 2015. Increased efficiency of Campylobacter jejuni N-oligosaccharyltransferase PglB by structure-guided engineering. Open biology, 5(4), p.140227.
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| Corresponding Author | Laboratory for Biointerfaces, Empa, Swiss Federal Laboratories for Materials Science and Technology, St Gallen 9014, Switzerland.
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