ProGT55 (PglLAb)
| ProGT ID | ProGT55 (PglLAb) |
| Organism Information | |
| Organism Name | Acinetobacter baumannii ATCC 17978 |
| Clinical Implication | Pathogenic |
| Domain | Bacteria |
| Classification | Phylum : Proteobacteria Class : GammaProteobacteria Orders : Pseudomonadales Family : Moraxellaceae Genus : Acinetobacter Species : baumannii Strain : ATCC 17978 |
| Taxonomic ID (NCBI) | 400667 |
| Genome Information | |
| Gene Bank | CP000521.1 |
| EMBL | CP000521 |
| Gene Information | |
| Gene Name | A1S_3176 |
| NCBI Reference Sequence | ABO13573.2 |
| Protein information | |
| Protein Name | PglLAb |
| Sequence length | 537 AA |
| Subcellular Location | Membrane (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 Application | 1) 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 Information | 1) 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 amoeba Dictyostelium discoideum and the larvae of the insect Galleria mellonella. |
| Glycosyltransferase Information | |
| Glycosylation Type | O- (Ser/Thr) linked |
| EC Number (BRENDA) | 2.4.1.- |
| Mechanism of Glycan Transfer | En bloc |
| Donor Type | UndPP-Pentasaccharide |
| Donor Specificity | Lipid linked sugars |
| Accessory GT ID | ProGT55.1 |
| Glycan Information | |
| Glycan transferred | Pentasaccharide (HexNAc-Hex-Hex-(HexNAc)-300), where 300 corresponded to an unknown residue of m/z 300 |
| Method of Glycan Indentification | NMR, MALDI-TOF/TOF MS and MS/MS |
| Experimental_strategies | In 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 Validation | 2012 |
| 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. and 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), p.e1002758. |
| Corresponding Author | Alberta 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. and Feldman, M.F., 2013. A common pathway for O?linked protein?glycosylation and synthesis of capsule in A cinetobacter baumannii. Molecular microbiology, 89(5), pp.816-830. |
| Corresponding Author | Alberta Glycomics Centre, Department of Biological Sciences, University of Alberta, CW405 Biological Sciences Building, Edmonton, Alberta, Canada, |