ProGT57 (PglLVc)
| ProGT ID | ProGT57 (PglLVc) |
| Organism Information | |
| Organism Name | Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) |
| Clinical Implication | Pathogenic |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria Class : GammaProteobacteria Orders : Vibrionales Family : Vibrionaceae Genus : Vibrio Species : cholerae Strain : ATCC 39315 / El Tor Inaba N16961 |
| Taxonomic ID (NCBI) | 243277 |
| Genome Information | |
| Gene Bank | AE003852.1 |
| EMBL | AE003852 |
| Gene Information | |
| Gene Name | VC0393 |
| NCBI Gene ID | 2614990 |
| NCBI Reference Sequence | AE003852 |
| Protein information | |
| Protein Name | PglLVc |
| UniProtKB/ SwissProt ID | Q9KUW6 |
| NCBI Ref Seq | NP_230047 |
| UniProtKB Sequence | >tr|Q9KUW6|Q9KUW6_VIBCH Uncharacterized protein OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) GN=VC_0393 PE=4 SV=1 MNCMATLLLSGTRLEPHAPNLPLNKPFLFALAVVYLLAMHFFMPNPGGAGLALSFNTTVW IATSITLAIGLYQLANNQALRYSKLTIGLWLSCALLTLPITYSNADWFHTLGRLVGLWAG FTLFLVLQQFRFSNKHKQRLLWFILLGSVIEAVIGLIQYFWLEPGNPFGYDTEANRPYGI FQQPNVMASFLATGLVLSGYLLARQPEKYDSRWSKIGILYATPLLTAPLLVVLASRTGWL ASLLSIALVAPYLYRFASRRRFTLWLLAITLGICAGFTAMYGQGTSGFVANKADLESPRR FTFPQTIDMIIEKPFTGYGYGKFEAQYLLYTARQHQLNSSYPAGLASMDHPHNELLYWGV EGGLLPVMGILLAACFCALRIYAAKRGTRMAMLALFVPITLHAQLEYPFYHSAIHWITFI ILIYWVDQRVARYRLASFTTLTKSLLRITSLVLPIVTSLYMVTALHTNYVLTQFEKSQPL NPELLKNVTNPLVWQDRFDWDIYSTYLNIGLHEQKAELIQPYIDWSLQIIQHKPRPAFYS NLILAYQGLGDTSRAQQIRREAEFLFPNQDFSTVQYHPSIKVNSATSDAEVPSAATP |
| EMBL CDS | AAF93566.1 |
| Sequence length | 597 AA |
| Subcellular Location | Membrane (Integral component of membrane) |
| String | 243277.VC0393 |
| 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) PglLVc 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 Escherichia coli it shows relaxed glycan and protein specificity. |
| Glycosyltransferase Information | |
| Glycosylation Type | O- (Ser/Thr) linked |
| EC Number (BRENDA) | 2.4.1.- |
| Mechanism of Glycan Transfer | En bloc |
| Donor Specificity | Lipid linked sugars |
| Glycan Information | |
| Glycan transferred | Monosaccharide, diNAcBac, and CjLLO. |
| Method of Glycan Indentification | MALDI-MS and MS/MS and C-ESI-QTOF-MS/MS. |
| Experimental_strategies | In vivo |
| Acceptor Subtrate Information | |
| Acceptor Substrate name | Type IV pilin subunit protein, |
| ProGPdb ID | ProGP99 |
| 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. and 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), pp.962-974. |
| Corresponding Author | Department of Biological Sciences, University of Alberta, Edmonton, Canada |