ProGT10.4 (PglI)

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ProGT ID ProGT10.4 (PglI)
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 NamepglI 
NCBI Gene ID905419
NCBI Reference SequenceNC_002163.1.
Protein information
Protein NamePglI 
UniProtKB/ SwissProt IDQ0P9C6
NCBI Ref SeqWP_002852770.1.
UniProtKB Sequence>sp|Q0P9C6|PGLI_CAMJE GalNAc(5)-diNAcBac-PP-undecaprenol beta-1,3-glucosyltransferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=pglI PE=1 SV=1 MPKLSVIVPTFNRQVLLEKAIKSIQNQDFKDLEIIVSDDNSSDDTKSVVQNLQKDDDRIK YFLNQNYKQGPNGNKNNGLDQASGEFVTFLDDDDELLSGALSTLMQKANEGYAHVFGNCL IEKEGNLSKEFSGKGLEKDSEISKKDFLMAKFSGEFFSVFKKSLLENKRFNEEFYGNEAT LWVNLYKEKSFYIHKAFRIYRIFRQDSVTLGASKNAYRVYLGYLELAKILENELRMSKDK DYKKTCASYYKMAAYYAKLAKNYKALYKCLFKSLSIKINAPALILLILSIIPNNMIEKLS KIRVALCKN
EMBL CDSCAL35245.1.
Sequence length309 AA
Subcellular LocationMembrane (Integral component of membrane)
String192222.Cj1128c.
Glycosylation Information
CAZY FamilyGT2
EC Number (BRENDA)2.4.1.293
Sugar Donor SpecificityUDP-Glc 
Experimental ValidationIn vitro
Donor SpecificityUDP-Glc
Function in Glycosylation pathway1) PglI function as a beta-1,-3 glucosyltransferase and responsible for the addition of the final branching glucose to complete the heptasaccharide biosynthesis.
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 02140
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