Latest update: September 24, 2018


ProGT52 (PglLBt)

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ProGT ID ProGT52 (PglLBt)
Organism Information
Organism NameBurkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
Clinical ImplicationNon-pathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Burkholderiaceae
Order: Burkholderiales
Class: Betaproteobacteria
Phylum: Proteobacteria
Taxonomic ID (NCBI)271848
Genome Information
Gene BankCP000086
EMBLCP000086
Gene Information
Gene NameBTH_I0650
Protein information
Protein NamePglLBt 
UniProtKB/ SwissProt IDQ2T0U3
NCBI Ref SeqWP_009892793.1
UniProtKB Sequence>tr|Q2T0U3|Q2T0U3_BURTA O-Antigen ligase family protein OS=Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264) GN=BTH_I0650 PE=4 SV=1 MPSSFLRSLSLIALAVALILPYAITNHTYPIPTFYSEFAAFALYWVLGASVVLLVKAERA RQPFAAPMALVAPLGFGAVLLAQIALLPLRLPSMNWLAMGYLLGALVAMQAGYALARANM VDVVARMIAGATIIGGVVAVACQFVQLFHLETMFSPFVVSYGVTVDRRPYGNMAQANHLA TYIAFALAGALYLVQTRRMPALAWAALSVLLSVGLALTVSRGPWLQVGVMVVAGFWMAFA QTRRDPAARRARAWVIPVVLGALFVAVNVAVRWANAHYHLGLAESAAERMRDAGQIAPRL ALWKYGLTMFREHPLLGVGWGEFPIHQFELVRRLGGVEIANNSHDIFIDLLAKSGLLGLG VLFVALVAWFVRALRAPHAESRVFGFALVGIVLMHALVEYPQQYTFFLLPVMFVIGLLET KPLRMLPGRAAFALFAALSVAGLASLYPVLRDYQRAEVLYYGTNPAEQYREQPSFLFGAW GDYGAATLLAISRDNLQAKLAAHERAIALLPGETVLRRYAVLQALDGREADALDTVERLR VFAEELHDWPVQLAALYKLLDEQPSLKSFKTALVAKYGTPAANLSADDEEDDSDE
EMBL CDSABC39069.1
Sequence length595 AA
Subcellular LocationMembrane (Integral component of membrane)
Potential Application1) Bacterial OTases with relaxed substrate specificity function as useful tools for glycoengineering of novel glycoconjugates with promising applications in vaccinology and diagnostics.
Additional Information1) PglBt has an OTases activity and is able to glycosylate proteins which are known substrates of PglL of Neisseria meningitidis, this indicates that it recognizes and glycosylate the same motif as PglL of N. meningitidis.
2) In E. coli it shows relaxed glycan and protein specificity.
Glycosyltransferase Information
Glycosylation TypeO- (Ser/Thr) linked 
EC Number (BRENDA)2.4.99.18
Mechanism of Glycan TransferEn bloc
Donor TypeLipid linked sugars
Glycan Information
Glycan transferredMonosaccharides, oligosaccharides, CjLLO, and E. coli O16 antigen. 
Method of Glycan IndentificationMALDI-MS and MS-MS
Experimental_strategiesIn vivo 
Acceptor Subtrate Information
Acceptor Substrate name Laz (lipid-azurin)
ProGPdb ID ProGP305
Acceptor Substrate name DsbA1
ProGPdb ID ProGP303
Litrature
Year Of Validation2012 
Reference Gebhart, C., Ielmini, M. V., Reiz, B., Price, N. L., Aas, F. E., Koomey, M., & Feldman, M. F. (2012). Characterization of exogenous bacterial oligosaccharyltransferases in Escherichia coli reveals the potential for O-linked protein glycosylation in Vibrio cholerae and Burkholderia thailandensis. Glycobiology, 22(7), 962-974.

Authors Gebhart, C., Ielmini, M. V., Reiz, B., Price, N. L., Aas, F. E., Koomey, M., & Feldman, M. F.
Research groupsDepartment of Biological Sciences, University of Alberta, Edmonton, Canada
Corresponding Author Feldman, M. F.
ContactsDepartment of Biological Sciences, University of Alberta, Edmonton, Canada