ProGT52 (PglLBt)
| ProGT ID | ProGT52 (PglLBt) |
| Organism Information | |
| Organism Name | Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264) |
| Clinical Implication | Non-pathogenic |
| Domain | Bacteria |
| Phylum | Proteobacteria |
| Classification | Family: Burkholderiaceae Order: Burkholderiales Class: Betaproteobacteria Phylum: Proteobacteria |
| Taxonomic ID (NCBI) | 271848 |
| Genome Information | |
| Gene Bank | CP000086 |
| EMBL | CP000086 |
| Gene Information | |
| Gene Name | BTH_I0650 |
| Protein information | |
| Protein Name | PglLBt |
| UniProtKB/ SwissProt ID | Q2T0U3 |
| NCBI Ref Seq | WP_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 CDS | ABC39069.1 |
| Sequence length | 595 AA |
| Subcellular Location | Membrane (Integral component of membrane) |
| Potential Application | 1) Bacterial OTases with relaxed substrate specificity function as useful tools for glycoengineering of novel glycoconjugates with promising applications in vaccinology and diagnostics. |
| Additional Information | 1) 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 Type | O- (Ser/Thr) linked |
| EC Number (BRENDA) | 2.4.99.18 |
| Mechanism of Glycan Transfer | En bloc |
| Donor Type | Lipid linked sugars |
| Glycan Information | |
| Glycan transferred | Monosaccharides, oligosaccharides, CjLLO, and E. coli O16 antigen. |
| Method of Glycan Indentification | MALDI-MS and MS-MS |
| Experimental_strategies | In vivo |
| Acceptor Subtrate Information | |
| Acceptor Substrate name | Laz (lipid-azurin) |
| ProGPdb ID | ProGP305 |
| Acceptor Substrate name | DsbA1 |
| ProGPdb ID | ProGP303 |
| Litrature | |
| Year Of Validation | 2012 |
| 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 groups | Department of Biological Sciences, University of Alberta, Edmonton, Canada |
| Corresponding Author | Feldman, M. F. |
| Contacts | Department of Biological Sciences, University of Alberta, Edmonton, Canada |