Latest update: September 24, 2018


ProGT10.1 (PglH)

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ProGT ID ProGT10.1 (PglH)
Organism Information
Organism NameCampylobacter jejuni 11168H
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 NamepglH 
NCBI Gene ID905420
NCBI Reference SequenceNC_002163.1.
Protein information
Protein NamePglH 
UniProtKB/ SwissProt IDQ0P9C5
NCBI Ref SeqYP_002344522.1
UniProtKB Sequence>sp|Q0P9C5|PGLH_CAMJE GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=pglH PE=1 SV=1 MMKISFIIATLNSGGAERALVTLANALCKEHEVSIIKFHAGESFYKLENEVKVTSLEQFR FDTLYHKIASRFKKFFALRKALKESKSDVFISFLDTTNIACIAAKIGLKTPLIISEHSNE AYLKPKIWRFLRRVSYPFCDALSVLGSSDKVYYERFVKRVKLLLNPCHFSDEISFDSSFE KENLVLFIGRLDHNKNPVMFLKAIAHLDKNLQENYKFVIAGDGQLRQELEYKVKSLGIKV DFLGRVENVKALYEKAKVLCLCSFVEGLPTVLIESLYFEVCRISSSYYNGAKDLIKDNHD GLLVGCDDEIALAKKLELVLNDENFRKELVNNAKQRCKDFEISHIKEEWLKLIAEVKNA
EMBL CDSCAL35246.1.
Sequence length359 AA
String192222.Cj1129c.
Glycosylation Information
CAZY FamilyGT4
EC Number (BRENDA)2.4.1.292
Sugar Donor SpecificityUDP-GalNAc 
Acceptor Substrate SpecificityUndPP-diNAcBac-GalNAc
Experimental ValidationIn vitro
ProductUndPP-diNAcBac-GalNAc-GalNAc-GalNAc-GalNAc
Donor SpecificityUDP-GalNAc
Function in Glycosylation pathway1) It has a GalNAc alpha-1-4 glycosyltransferase activity and it transfers the three terminal GalNAc residues to the Campylobacter jejuni glycan.
Litrature
Year Of Validation2004 
Reference Karlyshev, A. V., Everest, P., Linton, D., Cawthraw, S., Newell, D. G., & Wren, B. W. (2004). The Campylobacter jejuni general glycosylation system is important for attachment to human epithelial cells and in the colonization of chicks. Microbiology, 150(6), 1957-1964.

Authors Karlyshev, A. V., Everest, P., Linton, D., Cawthraw, S., Newell, D. G., & Wren, B. W.
Research groupsLondon School of Hygiene and Tropical Medicine, University of London, Keppel Street, London EC1A 7HT, UK.
Corresponding Author Wren, B. W.
ContactsLondon School of Hygiene and Tropical Medicine, University of London, Keppel Street, London EC1A 7HT, UK.
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 Szymanski, C. M.
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 Szymanski, C. M.
ContactsNational Research Council, Institute for Biological Sciences, 100 Sussex Drive, Ottawa, ON, Canada, K1A 0R6.