Latest update: September 24, 2018


ProGT95 (CuPglB)

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ProGT ID ProGT95 (CuPglB)
Organism Information
Organism NameCampylobacter upsaliensis
Clinical ImplicationPathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Campylobacteraceae
Order: Campylobacterales
Class: Epsilonproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)306264
Genome Information
Gene BankAAFJ01000002
EMBLAAFJ01000002
Gene Information
Gene NamepglB
Protein information
Protein NameCuPglB 
Subcellular LocationMembrane (Integral component of membrane)
Additional Information1) It has relaxed substrate specificity towards negatively charged residue in the ?2 position relative to the asparagine as compare to C. jejuni PglB.
Glycosyltransferase Information
Glycosylation TypeN- (Asn) linked 
CAZY FamilyGT66
EC Number (BRENDA)2.4.99.18
Mechanism of Glycan TransferEn bloc
Acceptor specificity Sequon_1Asn-Xaa-Ser
Donor TypeLipid linked sugars
Donor SpecificityUndPP-Heptasaccharide
Glycan Information
Glycan transferredHeptasaccharide 
Method of Glycan IndentificationLC-MS
Experimental_strategiesIn vivo and In vitro 
Acceptor Subtrate Information
Acceptor Substrate name scFv13-R4 DQNAT
Acceptor Substrate name scFv13-R4 AQNAT
Acceptor Substrate name scFv13-R4 CQNAT
Acceptor Substrate name scFv13-R4 YQNAT
Acceptor Substrate name scFv13-R4 WQNAT
Acceptor Substrate name scFv13-R4 VQNAT
Acceptor Substrate name scFv13-R4 TQNAT
Acceptor Substrate name scFv13-R4 SQNAT
Acceptor Substrate name scFv13-R4 QQNAT
Acceptor Substrate name scFv13-R4 PQNAT
Acceptor Substrate name scFv13-R4 NQNAT
Acceptor Substrate name scFv13-R4 MQNAT
Acceptor Substrate name scFv13-R4 HQNAT
Acceptor Substrate name scFv13-R4 GQNAT
Acceptor Substrate name scFv13-R4 EQNAT
Acceptor Substrate name TAMRA-GDQNATAF
Litrature
Year Of Validation2015 
Reference Ollis, A.A., Chai, Y., Natarajan, A., Perregaux, E., Jaroentomeechai, T., Guarino, C., Smith, J., Zhang, S. & DeLisa, M. P. (2015). Substitute sweeteners: diverse bacterial oligosaccharyltransferases with unique N-glycosylation site preferences. Scientific reports, 5, 15237.

Authors Ollis, A.A., Chai, Y., Natarajan, A., Perregaux, E., Jaroentomeechai, T., Guarino, C., Smith, J., Zhang, S. & DeLisa, M. P.
Research groups1 School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY 14853 USA. 2 Department of Microbiology, Cornell University, Ithaca, NY 14853 USA. 3 Comparative Biomedical Sciences, Cornell University, Ithaca, NY 14853 USA. 4 Proteomics and Mass Spectrometry Core Facility, Cornell University, Ithaca, New York.
Corresponding Author DeLisa, M. P.
ContactsProteomics and Mass Spectrometry Core Facility, Cornell University, Ithaca, New York 14853.