ProGT24 (PglL)

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ProGT ID ProGT24 (PglL)
ProGT Pathway
Organism Information
Organism NameNeisseria meningitidis 8013
Clinical ImplicationPathogenic
Classification Phylum : Proteobacteria
Class : BetaProteobacteria
Orders : Neisseriales
Family : Neisseriaceae
Genus : Neisseria
Species : meningitidis
Strain : 8013
Taxonomic ID (NCBI)604162
Genome Information
Gene BankFM999788.1
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 TypeUDP-diNacBAc
Donor SpecificityLipid linked sugars
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
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. and 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), pp.14783-14788.

Corresponding AuthorEcole 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. and 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), pp.10578-10587.

Corresponding AuthorAlberta Glycomics Centre, Department of Biological Sciences, University of Alberta, Edmonton, Alberta T6G 2E9, Canada.
Reference Musumeci, M.A., Faridmoayer, A., Watanabe, Y. and Feldman, M.F., 2014. Evaluating the role of conserved amino acids in bacterial O-oligosaccharyltransferases by in vivo, in vitro and limited proteolysis assays. Glycobiology, 24(1), pp.39-50.

Corresponding AuthorDepartment of Biological Sciences, Alberta Glycomics Centre, University of Alberta, CW405 Biological Sciences Building, Edmonton, AB, Canada.