Latest update: September 24, 2018


ProGT10.3 (PglJ)

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ProGT ID ProGT10.3 (PglJ)
Organism Information
Organism NameCampylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Domain Bacteria
PhylumProteobacteria
ClassificationFamily: Campylobacteraceae
Order: Campylobacterales
Class: Epsilonproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)192222
Genome Information
Gene BankAL111168
EMBLAL111168
Gene Information
Gene NamepglJ 
NCBI Reference SequenceNC_002163.1.
Protein information
Protein NamePglJ 
UniProtKB/ SwissProt IDQ0P9C7
NCBI Ref SeqWP_002852870.1.
UniProtKB Sequence>sp|Q0P9C7|PGLJ_CAMJE N-acetylgalactosamine-N,N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-alpha-N-acetylgalactosaminyltransferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=pglJ PE=1 SV=1 MQKLGIFIYSLGSGGAERVVATLLPILSLKFEVHLILMNDKISYEIPECQIHFLECSKPS ENPILKFLKLPFLALKYKKLCRNLGIDTEFVFLNRPNYIALMARMFGNKTRLVINECTTP SVMYMKNNFNSLVNKFLISLLYPKADLILPNSKGNLEDLVQNFSISPKKCEILYNAIDLE NIGQKALEDIALKDKFILSVGRLDKGKNHALLIRAYARLKTDLKLVILGEGVLKDELLAL IKELNLEEKVLLLGFDNNPYKYMAKCEFFAFASVFEGFSNVLIESLACSCAVVCTDHKSG ARELFGDDEFGLLVEVDNENSMFQGLKTMLEDDKLRKAYKNKAKTRAKAFDKVKIARDAL KYLLG
EMBL CDSCAL35244.1.
Sequence length365 AA
Subcellular LocationMembrane (Inner membrane)
String192222.Cj1127c.
Glycosylation Information
CAZY FamilyGT4
EC Number (BRENDA)2.4.1.291
Sugar Donor SpecificityUDP-GalNAc 
Acceptor Substrate SpecificityUndPP-diNAcBac-GalNAc
Experimental ValidationIn vitro and In vivo
ProductUndPP-diNAcBac-GalNAc-GalNAc
Donor SpecificityUDP-GalNAc
Function in Glycosylation pathway1) PglJ is a GalNAc transferase and adds the second GalNAc to create trisaccharide.
Litrature
Year Of Validation2005 
Reference Glover, K. J., Weerapana, E., & Imperiali, B. (2005). In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proceedings of the National Academy of Sciences, 102(40), 14255-14259.

Authors Glover, K. J., Weerapana, E., & Imperiali, B.
Research groupsDepartments of Chemistry and Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139
Corresponding Author Imperiali, B.
ContactsDepartments of Chemistry and Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139
Reference Reid, C. W., Stupak, J., Chen, M. M., Imperiali, B., Li, J., & Szymanski, C. M. (2008). Affinity-capture tandem mass spectrometric characterization of polyprenyl-linked oligosaccharides: tool to study protein N-glycosylation pathways. Analytical chemistry, 80(14), 5468-5475.

Authors Reid, C. W., Stupak, J., Chen, M. M., Imperiali, B., Li, J., & Szymanski, C. M.
Research groupsNational Research Council, Institute for Biological Sciences, 100 Sussex Drive, Ottawa, ON, Canada, K1A 0R6.
Corresponding Author Imperiali, B.
ContactsNational Research Council, Institute for Biological Sciences, 100 Sussex Drive, Ottawa, ON, Canada, K1A 0R6.
Reference Kelly, J., Jarrell, H., Millar, L., Tessier, L., Fiori, L.M., Lau, P.C., Allan, B. & Szymanski, C. M.(2006). Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer. Journal of bacteriology, 188(7), 2427-2434.

Authors Kelly, J., Jarrell, H., Millar, L., Tessier, L., Fiori, L.M., Lau, P.C., Allan, B. & Szymanski, C. M.
Research groupsInstitute for Biological Sciences, National Research Council, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada
Corresponding AuthorSzymanski, C. M.
ContactsInstitute for Biological Sciences, National Research Council, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada