| ProGT ID | ProGT9.1 (PglE) |
| Organism Information | |
| Organism Name | Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria Class : Epsilonproteobacteria Orders : Campylobacterales Family : Campylobacteraceae Genus : Campylobacter Species : jejuni Subspecies : jejuni Strain : 81-176 |
| Taxonomic ID (NCBI) | 354242 |
| Genome Information | |
| Gene Bank | CP000538.1 |
| EMBL | CP000538 |
| Gene Information | |
| Gene Name | pglE (Cj1121c) |
| Protein information | |
| Protein Name | PglE |
| UniProtKB/ SwissProt ID | A0A0H3PH73 |
| NCBI Ref Seq | WP_002868949.1. |
| UniProtKB Sequence | >tr|A0A0H3PH73|A0A0H3PH73_CAMJJ General glycosylation pathway protein OS=Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) GN=pglE PE=3 SV=1 MRFFLSPPHMGGNELKYIEEVFKSNYIAPLGEFVNRFEQSVKDYSKSENALALNSATAAL HLALRVAGVKQDDIVLASSFTFIASVAPICYLKAKPVFIDCDETYNIDVDLLKLAIKECE KKPKALILTHLYGNAAKMDEIVEICKENEIVLIEDAAEALGSFYKNKALGTFGEFGAYSY NGNKIITTSGGGMLIGKNKEKIEKARFYSTQARENCLHYEHLDYGYNYRLSNVLGAIGVA QMEVLEQRVLKKREIYEWYKEFLGEYFSFLDELENSRSNRWLSTALIDFDKNELNACQKD VNISQKNIALHPKISKLIEDLKNEQIETRPLWKAMHTQEVFKGAKAYLNGNSELFFQKGI CLPSGTAMSKDDVCEISKLILKSIKA |
| EMBL CDS | EAQ72185.1 |
| Sequence length | 386 AA |
| String | 354242.Cjejjejuni_010100005940. |
| Glycosylation Information | |
| CAZY Family | Non-GT |
| EC Number (BRENDA) | 2.6.1- |
| Sugar Donor Specificity | UDP-GlcNAc |
| Acceptor Substrate Specificity | UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose |
| Experimental Validation | In vivo and In vitro |
| Product | UDP-4-amino-4,6-dideoxy-alpha-D-GlcNAc |
| Donor Specificity | UDP-GlcNAc |
| Function in Glycosylation pathway | 1) Aminotransferase involved in the formation of UDP-4-amino-4,6-dideoxy-alpha-D-GlcNAc. |
| Additional Information | 1) The mutation in pglE gene cause a reduction in adherence and invasion of INT407 cells in vitro, and It also reduced the ability to colonize the intestinal tract of mice. |
| Litrature | |
| Year Of Validation | 2004 |
| Reference | Schoenhofen, I.C., McNally, D.J., Vinogradov, E., Whitfield, D., Young, N.M., Dick, S., Wakarchuk, W.W., Brisson, J.R. and Logan, S.M., 2006. Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways. Journal of Biological Chemistry, 281(2), pp.723-732. |
| Corresponding Author | Institute for Biological Sciences, National Research Council, Ottawa, Ontario K1A OR6, Canada |
| Reference | Larsen, J.C., Szymanski, C. and Guerry, P., 2004. N-linked protein glycosylation is required for full competence in Campylobacter jejuni 81-176. Journal of bacteriology, 186(19), pp.6508-6514. |
| Corresponding Author | Enteric Diseases Department, Naval Medical Research Center, Silver Spring, Maryland |
| Reference | Szymanski, C.M., Burr, D.H. and Guerry, P., 2002. Campylobacter protein glycosylation affects host cell interactions. Infection and immunity, 70(4), pp.2242-2244. |
| Corresponding Author | Enteric Diseases Program, Naval Medical Research Center, Silver Spring, Marland 20910-7500, USA |