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
Classification Phylum : Proteobacteria
Class : Epsilonproteobacteria
Orders : Campylobacterales
Family : Campylobacteraceae
Genus : Campylobacter
Species : jejuni
Subspecies : jejuni
Strain : ATCC 700819 / NCTC 11168
Taxonomic ID (NCBI)192222
Genome Information
Gene BankAL111168.1
EMBLAL111168.1
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. and 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), pp.14255-14259.

Corresponding AuthorDepartments 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. and 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), pp.5468-5475.

Corresponding AuthorNational Research Council, Institute for Biological Sciences, 100 Sussex Drive, Ottawa, ON, Canada, K1A 0R6.
Reference Reid, C.W., Stupak, J., Chen, M.M., Imperiali, B., Li, J. and 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), pp.5468-5475.

Corresponding AuthorNational 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. and 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), pp.2427-2434.

Corresponding AuthorInstitute for Biological Sciences, National Research Council, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada