ProGT95 (CuPglB)
| ProGT ID | ProGT95 (CuPglB) |
| Organism Information | |
| Organism Name | Campylobacter upsaliensis |
| Clinical Implication | Pathogenic |
| Domain | Bacteria |
| Phylum | Proteobacteria |
| Classification | Family: Campylobacteraceae Order: Campylobacterales Class: Epsilonproteobacteria Division or phylum: "Proteobacteria" |
| Taxonomic ID (NCBI) | 306264 |
| Genome Information | |
| Gene Bank | AAFJ01000002 |
| EMBL | AAFJ01000002 |
| Gene Information | |
| Gene Name | pglB |
| Protein information | |
| Protein Name | CuPglB |
| Subcellular Location | Membrane (Integral component of membrane) |
| Additional Information | 1) 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 Type | N- (Asn) linked |
| CAZY Family | GT66 |
| EC Number (BRENDA) | 2.4.99.18 |
| Mechanism of Glycan Transfer | En bloc |
| Acceptor specificity Sequon_1 | Asn-Xaa-Ser |
| Donor Type | Lipid linked sugars |
| Donor Specificity | UndPP-Heptasaccharide |
| Glycan Information | |
| Glycan transferred | Heptasaccharide |
| Method of Glycan Indentification | LC-MS |
| Experimental_strategies | In 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 Validation | 2015 |
| 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 groups | 1 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. |
| Contacts | Proteomics and Mass Spectrometry Core Facility, Cornell University, Ithaca, New York 14853. |