Latest update: September 24, 2018


ProGT55 (PglLAb)

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ProGT ID ProGT55 (PglLAb)
Organism Information
Organism NameAcinetobacter baumannii ATCC 17978
Clinical ImplicationPathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Moraxellaceae
Order: Pseudomonadales
Class: Gammaproteobacteria
Phylum: Proteobacteria
Taxonomic ID (NCBI)400667
Genome Information
Gene BankCP000521
EMBLCP000521
Gene Information
Gene NameA1S_3176
NCBI Reference SequenceABO13573.2
Protein information
Protein NamePglLAb 
Sequence length537 AA
Subcellular LocationMembrane (Integral component of membrane)
Function in Native Organism 1) PglLAb is required for glycosylation of membrane proteins and also required for efficient biofilm formation.
Potential Application1) Protein O-glycosylation represents a novel target for the development of antibiotics and glycoproteins identified in this study may be the base of future vaccine formulations and diagnostic methods.
Additional Information1) PglLAb transfer of O-linked pentasaccharide to several proteins in A. baumanii.
2) The defect in O-glycosylation resulted in reduced virulence in infection models like amoebae Dictyostelium discoideum and the larvae of the insect Galleria mellonella.
Glycosyltransferase Information
Glycosylation TypeO- (Ser/Thr) linked 
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferEn bloc
Donor TypeLipid linked sugars
Donor SpecificityUndPP-Pentasaccharide
Accessory GT IDProGT55.1
Glycan Information
Glycan transferredPentasaccharide (HexNAc-Hex-Hex-(HexNAc)-300), where 300 corresponded to an unknown residue of m/z 300 
Method of Glycan IndentificationNMR, MALDI-TOF/TOF MS and MS/MS
Experimental_strategiesIn vivo 
Acceptor Subtrate Information
Acceptor Substrate name Putative Uncharacterized Protein
ProGPdb ID ProGP413
Acceptor Substrate name Putative Uncharacterized Protein
ProGPdb ID ProGP414
Acceptor Substrate name OmpA/MotB
ProGPdb ID ProGP412
Acceptor Substrate name Putative uncharacterized protein
ProGPdb ID ProGP415
Acceptor Substrate name Putative uncharacterized protein
ProGPdb ID ProGP420
Acceptor Substrate name Putative uncharacterized protein
ProGPdb ID ProGP417
Acceptor Substrate name Putative uncharacterized protein
ProGPdb ID ProGP414
Litrature
Year Of Validation2012 
Reference Iwashkiw, J.A., Seper, A., Weber, B.S., Scott, N.E., Vinogradov, E., Stratilo, C., Reiz, B., Cordwell, S.J., Whittal, R., Schild, S & Feldman, M. F. (2012). Identification of a general O-linked protein glycosylation system in Acinetobacter baumannii and its role in virulence and biofilm formation. PLoS pathogens, 8(6), e1002758.

Authors Iwashkiw, J.A., Seper, A., Weber, B.S., Scott, N.E., Vinogradov, E., Stratilo, C., Reiz, B., Cordwell, S.J., Whittal, R., Schild, S & Feldman, M. F.
Research groupsAlberta Glycomics Centre, Department of Biological Sciences, University of Alberta, Edmonton, Alberta, Canada.
Corresponding Author Feldman, M. F.
ContactsAlberta Glycomics Centre, Department of Biological Sciences, University of Alberta, Edmonton, Alberta, Canada.
Reference Lees-Miller, R. G., Iwashkiw, J. A., Scott, N. E., Seper, A., Vinogradov, E., Schild, S., & Feldman, M. F. (2013). A common pathway for O-linked protein-glycosylation and synthesis of capsule in A cinetobacter baumannii. Molecular microbiology, 89(5), 816-830.

Authors Lees-Miller, R. G., Iwashkiw, J. A., Scott, N. E., Seper, A., Vinogradov, E., Schild, S., & Feldman, M. F.
Research groupsAlberta Glycomics Centre, Department of Biological Sciences, University of Alberta, CW405 Biological Sciences Building, Edmonton, Alberta, Canada,
Corresponding Author Feldman, M. F.
ContactsAlberta Glycomics Centre, Department of Biological Sciences, University of Alberta, CW405 Biological Sciences Building, Edmonton, Alberta, Canada,