Latest update: September 24, 2018


ProGT24 (PglL)

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ProGT ID ProGT24 (PglL)
ProGT Pathway
Organism Information
Organism NameNeisseria meningitidis 8013
Clinical ImplicationPathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Neisseriaceae
Order: Neisseriales
Class: Betaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)604162
Genome Information
Gene BankFM999788
EMBLFM999788
Gene Information
Protein information
Protein NamePglL 
Subcellular LocationMembrane (Integral component of membrane)
Additional Information1) PglL can use UDP-diNacBAc as substrate instead of UDP-GlcNAc or UDP-GalNAc in vitro.
Glycosyltransferase Information
Glycosylation TypeO- (Ser/Thr) linked 
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferEn bloc
Donor TypeLipid linked sugars
Donor SpecificityUDP-diNacBAc
Accessory GT IDProGT24.1 ProGT24.2 ProGT24.3 ProGT24.4
Glycan Information
Glycan transferred2,4-diacetamido-2,4,6-trideoxyhexose (GATDH) 
Method of Glycan IndentificationMALDI-TOF, Q-TOF MS and FT-ICR .
Experimental_strategiesIn vitro and In vivo  
Acceptor Subtrate Information
Acceptor Substrate name PilE
ProGPdb ID ProGP99
Litrature
Year Of Validation2007 
Reference Chamot-Rooke, J., Rousseau, B., Lanternier, F., Mikaty, G., Mairey, E., Malosse, C., Bouchoux, G., Pelicic, V., Camoin, L., Nassif, X. & Duménil, G. (2007). Alternative Neisseria spp. type IV pilin glycosylation with a glyceramido acetamido trideoxyhexose residue. Proceedings of the National Academy of Sciences, 104(37), 14783-14788.

Authors Chamot-Rooke, J., Rousseau, B., Lanternier, F., Mikaty, G., Mairey, E., Malosse, C., Bouchoux, G., Pelicic, V., Camoin, L., Nassif, X. & Duménil, G.
Research groupsEcole Polytechnique, Laboratory of Reaction Mechanisms, Department of Chemistry, F-91128 Palaiseau, France
Corresponding Author Duménil, G.
ContactsEcole Polytechnique, Laboratory of Reaction Mechanisms, Department of Chemistry, F-91128 Palaiseau, France
Reference Musumeci, M. A., Hug, I., Scott, N. E., Ielmini, M. V., Foster, L. J., Wang, P. G., & Feldman, M. F. (2013). In vitro activity of Neisseria meningitidis PglL O-oligosaccharyltransferase with diverse synthetic lipid donors and a UDP-activated sugar. Journal of Biological Chemistry, 288(15), 10578-10587.

Authors Musumeci, M. A., Hug, I., Scott, N. E., Ielmini, M. V., Foster, L. J., Wang, P. G., & Feldman, M. F.
Research groupsAlberta Glycomics Centre, Department of Biological Sciences, University of Alberta, Edmonton, Alberta T6G 2E9, Canada.
Corresponding Author Feldman, M. F.
ContactsAlberta Glycomics Centre, Department of Biological Sciences, University of Alberta, Edmonton, Alberta T6G 2E9, Canada.
Reference Musumeci, M. A., Faridmoayer, A., Watanabe, Y., & Feldman, M. F. (2013). Evaluating the role of conserved amino acids in bacterial O-oligosaccharyltransferases by in vivo, in vitro and limited proteolysis assays. Glycobiology, 24(1), 39-50.

Authors Musumeci, M. A., Faridmoayer, A., Watanabe, Y., & Feldman, M. F.
Research groupsDepartment of Biological Sciences, Alberta Glycomics Centre, University of Alberta, CW405 Biological Sciences Building, Edmonton, AB, Canada T6G 2E9.
Corresponding Author Feldman, M. F.
ContactsDepartment of Biological Sciences, Alberta Glycomics Centre, University of Alberta, CW405 Biological Sciences Building, Edmonton, AB, Canada.