Latest update: September 24, 2018


ProGT10 (PglB)

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ProGT ID ProGT10 (PglB)
ProGT Pathway
Organism Information
Organism NameCampylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Clinical ImplicationPathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Campylobacteraceae
Order: Campylobacterales
Class: Epsilonproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)192222
Genome Sequence(s)
Gene BankAL111168
EMBLAL111168
Gene Information
Gene NamepglB
NCBI Gene ID905417
Protein information
Protein NamePglB 
UniProtKB/ SwissProt IDQ0P9C8
NCBI Ref SeqYP_002344519.1
UniProtKB Sequence>sp|Q0P9C8|PGLB_CAMJE Undecaprenyl-diphosphooligosaccharide--protein glycotransferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=pglB PE=1 SV=1 MLKKEYLKNPYLVLFAMIVLAYVFSVFCRFYWVWWASEFNEYFFNNQLMIISNDGYAFAE GARDMIAGFHQPNDLSYYGSSLSTLTYWLYKITPFSFESIILYMSTFLSSLVVIPIILLA NEYKRPLMGFVAALLASVANSYYNRTMSGYYDTDMLVIVLPMFILFFMVRMILKKDFFSL IALPLFIGIYLWWYPSSYTLNVALIGLFLIYTLIFHRKEKIFYIAVILSSLTLSNIAWFY QSAIIVILFALFALEQKRLNFMIIGILGSATLIFLILSGGVDPILYQLKFYIFRSDESAN LTQGFMYFNVNQTIQEVENVDFSEFMRRISGSEIVFLFSLFGFVWLLRKHKSMIMALPIL VLGFLALKGGLRFTIYSVPVMALGFGFLLSEFKAILVKKYSQLTSNVCIVFATILTLAPV FIHIYNYKAPTVFSQNEASLLNQLKNIANREDYVVTWWDYGYPVRYYSDVKTLVDGGKHL GKDNFFPSFSLSKDEQAAANMARLSVEYTEKSFYAPQNDILKSDILQAMMKDYNQSNVDL FLASLSKPDFKIDTPKTRDIYLYMPARMSLIFSTVASFSFINLDTGVLDKPFTFSTAYPL DVKNGEIYLSNGVVLSDDFRSFKIGDNVVSVNSIVEINSIKQGEYKITPIDDKAQFYIFY LKDSAIPYAQFILMDKTMFNSAYVQMFFLGNYDKNLFDLVINSRDAKVFKLKI
EMBL CDSCAL35243.1
Sequence length713 AA
Subcellular LocationMembrane (Integral component of membrane)
Function in Native Organism 1) The PglB is OSTase which transfer an heptasaccharide to N of D/E-N-X-T/S consensus sequence of the protein in Campylobacter jejuni.
String192222.Cj1126c.
Potential Application1) PglB can be used to create artificial glycopeptides because it has relaxed substrate specificity of accepting peptide substrates over the full-length protein.
2) PglB can transfer undecaprenyl pyrophosphate-linked saccharides of various lengths (2?7 saccharides) adds to the promise of using PglB in the synthesis of diverse glycopeptide products.
Additional Information1) PglB requires an acetamido group at the C-2.
2) R331 of C.lari and R328 of C.jejuni form a salt bridge with acidic amino acid.
3) PglB can transfer several structurally different O-antigen saccharides to protein.
Acceptor Subtrate Information
Acceptor Substrate name CgpA
ProGPdb ID ProGP218
Acceptor Substrate name Cj0114
ProGPdb ID ProGP219
Acceptor Substrate name Cj0200c
ProGPdb ID ProGP220
Acceptor Substrate name Cj1496c
ProGPdb ID ProGP221
Acceptor Substrate name PEB3
ProGPdb ID ProGP222
Acceptor Substrate name ZnuA
ProGPdb ID ProGP223
Acceptor Substrate name AcrA
ProGPdb ID ProGP218
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 for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada.
Corresponding Author Szymanski, C.M.
ContactsInstitute for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada.
Reference Glover, K. J., Weerapana, E., Numao, S., & Imperiali, B. (2005). Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni. Chemistry & biology, 12(12), 1311-1316.

Authors Glover, K. J., Weerapana, E., Numao, S., & Imperiali, B.
Research groupsDepartment of Chemistry and Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.
Corresponding Author Imperiali, B.
ContactsDepartment of Chemistry and Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.
Reference Kowarik, M., Young, N.M., Numao, S., Schulz, B.L., Hug, I., Callewaert, N., Mills, D.C., Watson, D.C., Hernandez, M., Kelly, J.F. & Wacker, M. (2006). Definition of the bacterial N?glycosylation site consensus sequence. The EMBO journal, 25(9), 1957-1966.

Authors Kowarik, M., Young, N.M., Numao, S., Schulz, B.L., Hug, I., Callewaert, N., Mills, D.C., Watson, D.C., Hernandez, M., Kelly, J.F. & Wacker, M.
Research groups Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, Switzerland
Corresponding Author Wacker, M.
Contacts Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, Switzerland
Reference Ihssen, J., Kowarik, M., Wiesli, L., Reiss, R., Wacker, M., & Thöny-Meyer, L. (2012). Structural insights from random mutagenesis of Campylobacter jejuni oligosaccharyltransferase PglB. BMC biotechnology, 12(1), 67.

Authors Ihssen, J., Kowarik, M., Wiesli, L., Reiss, R., Wacker, M., & Thöny-Meyer, L.
Research groupsEmpa, Swiss Federal Laboratories for Materials Science and Technology, Laboratory for Biomaterials, CH-9014, St, Gallen, Switzerland.
Corresponding Author Thöny-Meyer, L.
ContactsEmpa, Swiss Federal Laboratories for Materials Science and Technology, Laboratory for Biomaterials, CH-9014, St, Gallen, Switzerland.
Reference Jaffee, M. B., & Imperiali, B. (2013). Optimized protocol for expression and purification of membrane-bound PglB, a bacterial oligosaccharyl transferase. Protein expression and purification, 89(2), 241-250.

Authors Jaffee, M. B., & Imperiali, B.
Research groupsDepartment of Biology and Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge
Corresponding Author Imperiali, B.
ContactsDepartment of Biology and Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge
Reference Ollis, A. A., Zhang, S., Fisher, A. C., & DeLisa, M. P. (2014). Engineered oligosaccharyltransferases with greatly relaxed acceptor-site specificity. Nature chemical biology, 10(10), 816.

Authors Ollis, A. A., Zhang, S., Fisher, A. C., & DeLisa, M. P.
Research groups1 School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, New York, USA. 2 Proteomics and Mass Spectrometry Core Facility, Cornell University, Ithaca, New York, USA. 3 Glycobia Inc., Ithaca, New York, USA.
Corresponding Author DeLisa, M. P.
Contacts School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, New York, USA