Latest update: September 24, 2018


ProGT9 (PglB)

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ProGT ID ProGT9 (PglB)
ProGT Pathway
Organism Information
Organism NameCampylobacter Jejuni 81-176
Clinical ImplicationPathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Campylobacteraceae
Order: Campylobacterales
Class: Epsilonproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)354242
Genome Information
Gene BankCP000538
EMBLCP000538
Gene Information
Gene NamepglB
Protein information
Protein NamePglB 
UniProtKB/ SwissProt IDA0A0H3P9U9
NCBI Ref SeqWP_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 CDSEAQ72203.1.
Sequence length713 AA
Subcellular LocationMembrane (Integral component of membrane)
String354242.Cjejjejuni_010100005965.
Potential Application1) 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 Information1) 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 TypeN- (Asn) linked 
CAZY FamilyGT66
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferEn bloc
Acceptor specificity Sequon_1Asp/Glu- Asn-Xaa-Ser/Thr
Donor TypeLipid linked sugars
Donor SpecificityUndPP-GalNAc- 1,4-GalNAc- 1,4-(Glc 1,3)-Gal-NAc- 1,4- GalNAc- 1,4-GalNAc- 1,3-Bac
Accessory GT IDProGT9.1
Glycan Information
Glycan transferredHeptasaccharide (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_strategiesIn 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 Validation2002 
Reference Young, N.M., Brisson, J.R., Kelly, J., Watson, D.C., Tessier, L., Lanthier, P.H., Jarrell, H.C., Cadotte, N., Michael, F.S., Aberg, E. & Szymanski, C.M. (2002). N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli. Science, 298(5599), 1790-1793.

Authors Young, N.M., Brisson, J.R., Kelly, J., Watson, D.C., Tessier, L., Lanthier, P.H., Jarrell, H.C., Cadotte, N., Michael, F.S., Aberg, E. & Szymanski, C.M.
Research groupsInstitute of Microbiology, Department of Biology, Swiss Federal Institute of Technology, Zürich, CH-8092 Zürich, Switzerland.
Corresponding Author Szymanski, C.M.
ContactsInstitute of Microbiology, Department of Biology, Swiss Federal Institute of Technology, Zürich, CH-8092 Zürich, Switzerland.
Reference Larsen, J. C., Szymanski, C., & Guerry, P. (2004). N-linked protein glycosylation is required for full competence in Campylobacter jejuni 81-176. Journal of bacteriology, 186(19), 6508-6514

Authors Larsen, J. C., Szymanski, C., & Guerry, P.
Research groupsDepartment of Microbiology and Immunology, F. Edward Hebert School of Medicine, Uniformed Services University of the Health Sciences, Bethesda, Maryland, USA
Corresponding Author Guerry, P.
ContactsDepartment of Microbiology and Immunology, F. Edward Hebert School of Medicine, Uniformed Services University of the Health Sciences, Bethesda, Maryland, USA
Reference Li, L., Woodward, R., Ding, Y., Liu, X.W., Yi, W., Bhatt, V.S., Chen, M., Zhang, L.W. & Wang, P. G. (2010). Overexpression and topology of bacterial oligosaccharyltransferase PglB. Biochemical and biophysical research communications, 394(4), 1069-1074.

Authors Li, L., Woodward, R., Ding, Y., Liu, X.W., Yi, W., Bhatt, V.S., Chen, M., Zhang, L.W. & Wang, P. G.
Research groupsNational Glycoengineering Research Center and The State Key Laboratory of Microbial Technology, School of Life Sciences, Shandong University, Shandong 250100, China.
Corresponding Author Wang, P. G.
ContactsNational Glycoengineering Research Center and The State Key Laboratory of Microbial Technology, School of Life Sciences, Shandong University, Shandong 250100, China.
Reference Ihssen, J., Haas, J., Kowarik, M., Wiesli, L., Wacker, M., Schwede, T., & Thöny-Meyer, L. (2015). Increased efficiency of Campylobacter jejuni N-oligosaccharyltransferase PglB by structure-guided engineering. Open biology, 5(4), 140227.

Authors Ihssen, J., Haas, J., Kowarik, M., Wiesli, L., Wacker, M., Schwede, T., & Thöny-Meyer, L.
Research groups1 Laboratory for Biointerfaces, Empa, Swiss Federal Laboratories for Materials Science and Technology, St Gallen 9014, Switzerland. 2 Biozentrum, University of Basel, Klingelbergstrasse 50/70, Basel 4056, Switzerland SIB Swiss Institute of Bioinformatics, Klingelbergstrasse 50/70, Basel 4056, Switzerland. 3 GlycoVaxyn AG, Schlieren 8952, Switzerland. 4 Laboratory for Biointerfaces, Empa, Swiss Federal Laboratories for Materials Science and Technology, St Gallen 9014, Switzerland
Corresponding Author Thöny-Meyer, L.
ContactsLaboratory for Biointerfaces, Empa, Swiss Federal Laboratories for Materials Science and Technology, St Gallen 9014, Switzerland.