Latest update: September 24, 2018


ProGT9.1 (PglE)

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ProGT ID ProGT9.1 (PglE)
Organism Information
Organism NameCampylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176)
Domain Bacteria
PhylumProteobacteria
ClassificationFamily: Campylobacteraceae
Order: Campylobacterales
Class: Epsilonproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)354242
Genome Information
Gene BankCP000538
EMBLCP000538
Gene Information
Gene NamepglE (Cj1121c) 
Protein information
Protein NamePglE 
UniProtKB/ SwissProt IDA0A0H3PH73
NCBI Ref SeqWP_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 CDSEAQ72185.1
Sequence length386 AA
String354242.Cjejjejuni_010100005940.
Glycosylation Information
CAZY FamilyNon-GT
EC Number (BRENDA)2.6.1-
Sugar Donor SpecificityUDP-GlcNAc 
Acceptor Substrate SpecificityUDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-4-hexulose
Experimental ValidationIn vivo and In vitro
ProductUDP-4-amino-4,6-dideoxy-alpha-D-GlcNAc
Donor SpecificityUDP-GlcNAc
Function in Glycosylation pathway1) Aminotransferase involved in the formation of UDP-4-amino-4,6-dideoxy-alpha-D-GlcNAc.
Additional Information1) 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 Validation2004 
Reference Schoenhofen, I.C., McNally, D.J., Vinogradov, E., Whitfield, D., Young, M., Dick, S., Wakarchuk, W.W., Brisson, J.R. & Logan, S. M. (2005). Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways. Journal of Biological Chemistry.

Authors Schoenhofen, I.C., McNally, D.J., Vinogradov, E., Whitfield, D., Young, M., Dick, S., Wakarchuk, W.W., Brisson, J.R. & Logan, S. M.
Research groupsInstitute for Biological Sciences, National Research Council, Ottawa, Ontario K1A OR6, Canada
Corresponding Author Logan, S. M.
ContactsInstitute for Biological Sciences, National Research Council, Ottawa, Ontario K1A OR6, Canada
Reference Larsen, J. C., Szymanski, C., & Guerry, P. (2004). N-linked protein glycosylation is required for full competence in Campylobacter jejuni 81-176. Journal of bacteriology, 186(19), 6508-6514.

Authors Larsen, J. C., Szymanski, C., & Guerry, P.
Research groupsDepartment of Microbiology and Immunology, F. Edward Hebert School of Medicine, Uniformed Services University of the Health Sciences, Bethesda, Maryland, USA.
Corresponding Author Imperiali, B.
ContactsDepartment of Microbiology and Immunology, F. Edward Hebert School of Medicine, Uniformed Services University of the Health Sciences, Bethesda, Maryland, USA
Reference Szymanski, C. M., Burr, D. H., & Guerry, P. (2002). Campylobacter protein glycosylation affects host cell interactions. Infection and immunity, 70(4), 2242.

Authors Szymanski, C. M., Burr, D. H., & Guerry, P.
Research groupsEnteric Diseases Program, Naval Medical Research Center, Silver Spring, Marland 20910-7500, USA
Corresponding Author Guerry, P.
ContactsEnteric Diseases Program, Naval Medical Research Center, Silver Spring, Marland 20910-7500, USA