ProGT47 (ClPglB)
| ProGT ID | ProGT47 (ClPglB) |
| Organism Information | |
| Organism Name | Campylobacter lari ATCC BAA-1060D |
| Clinical Implication | Pathogenic |
| Domain | Bacteria |
| Phylum | Proteobacteria |
| Classification | Family: Campylobacteraceae Order: Campylobacterales Class: Epsilonproteobacteria Division or phylum: "Proteobacteria" |
| Taxonomic ID (NCBI) | 306263 |
| Genome Information | |
| Gene Bank | CP000932 |
| EMBL | CP000932 |
| Gene Information | |
| Gene Name | pglB |
| NCBI Gene ID | 7410986 |
| Protein information | |
| Protein Name | ClPglBÂ |
| UniProtKB/ SwissProt ID | B9KDD4 |
| NCBI Ref Seq | ACM64573.1 |
| UniProtKB Sequence | >sp|B9KDD4|PGLB_CAMLR Undecaprenyl-diphosphooligosaccharide--protein glycotransferase OS=Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060) GN=pglB PE=1 SV=1 MKLQQNFTDNNSIKYTCILILIAFAFSVLCRLYWVAWASEFYEFFFNDQLMITTNDGYAF AEGARDMIAGFHQPNDLSYFGSSLSTLTYWLYSILPFSFESIILYMSAFFASLIVVPIIL IAREYKLTTYGFIAALLGSIANSYYNRTMSGYYDTDMLVLVLPMLILLTFIRLTINKDIF TLLLSPVFIMIYLWWYPSSYSLNFAMIGLFGLYTLVFHRKEKIFYLTIALMIIALSMLAW QYKLALIVLLFAIFAFKEEKINFYMIWALIFISILILHLSGGLDPVLYQLKFYVFKASDV QNLKDAAFMYFNVNETIMEVNTIDPEVFMQRISSSVLVFILSFIGFILLCKDHKSMLLAL PMLALGFMALRAGLRFTIYAVPVMALGFGYFLYAFFNFLEKKQIKLSLRNKNILLILIAF FSISPALMHIYYYKSSTVFTSYEASILNDLKNKAQREDYVVAWWDYGYPIRYYSDVKTLI DGGKHLGKDNFFSSFVLSKEQIPAANMARLSVEYTEKSFKENYPDVLKAMVKDYNKTSAK DFLESLNDKDFKFDTNKTRDVYIYMPYRMLRIMPVVAQFANTNPDNGEQEKSLFFSQANA IAQDKTTGSVMLDNGVEIINDFRALKVEGASIPLKAFVDIESITNGKFYYNEIDSKAQIY LLFLREYKSFVILDESLYNSSYIQMFLLNQYDQDLFEQITNDTRAKIYRLKR |
| EMBL CDS | ACM64573.1 |
| Sequence length | 712 AA |
| Subcellular Location | Membrane (Integral component of membrane) |
| Function in Native Organism | 1) Transfer the C.jejuni heptasaccharide to the peptide having the consensus sequence. |
| String | 306263.Cla_1253 |
| PDB ID | 3RCE |
| Glycosyltransferase Information | |
| Glycosylation Type | N- (Asn) linked |
| CAZY Family | GT66 |
| EC Number (BRENDA) | 2.4.1.119 |
| Mechanism of Glycan Transfer | En bloc |
| Acceptor specificity Sequon_1 | Asp/Glu- Asn-Xaa-Ser/Thr |
| Donor Type | Lipid linked sugars |
| Donor Specificity | UndPP-Heptasaccharide |
| Glycan Information | |
| Glycan transferred | Heptasaccharide |
| Method of Glycan Indentification | LC-MS, and MALDI-TOF/TOF |
| Experimental_strategies | In vivo and In vitro |
| Acceptor Subtrate Information | |
| Acceptor Substrate name | scFv13-R4 DQNAT |
| Acceptor Substrate name | scFv13-R4 EQNAT |
| Acceptor Substrate name | TAMRA-GDQNATAF |
| Litrature | |
| Year Of Validation | 2011Â |
| Reference | Lizak, C., Gerber, S., Numao, S., Aebi, M., & Locher, K. P. (2011). X-ray structure of a bacterial oligosaccharyltransferase. Nature, 474(7351), 350. |
| Authors | Lizak, C., Gerber, S., Numao, S., Aebi, M., & Locher, K. P. |
| Research groups | Institute of Microbiology, Department of Biology, ETH Zurich, CH-8093 Zurich, Switzerland |
| Corresponding Author | Locher, K. P. |
| Contacts | Institute of Microbiology, Department of Biology, ETH Zurich, CH-8093 Zurich, Switzerland. |
| 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. |