ProGT104 (PglLRs)
| ProGT ID | ProGT104 (PglLRs) |
| Organism Information | |
| Organism Name | Ralstonia solanacearum GMI1000 |
| Clinical Implication | Plant pathogen |
| Domain | Bacteria |
| Phylum | Proteobacteria |
| Classification | Family: Ralstoniaceae Order: Burkholderiales Class: Betaproteobacteria Phylum: Proteobacteria |
| Taxonomic ID (NCBI) | 267608 |
| Genome Information | |
| Gene Bank | AL646052 |
| EMBL | AL646052 |
| Gene Information | |
| Gene Name | Rsc0559 |
| NCBI Reference Sequence | CAD14089 |
| Protein information | |
| Protein Name | PglLRs |
| UniProtKB/ SwissProt ID | Q8Y1X8 |
| UniProtKB Sequence | >tr|Q8Y1X8|Q8Y1X8_RALSO Putative lipida core-o-antigen ligase transmembrane protein OS=Ralstonia solanacearum (strain GMI1000) GN=RSc0559 PE=4 SV=1 MLWPVWLATVACWSVPFLVAVHSYPIPTFYSEFVAAIGWVALAAGVLGSTWHSKAGLPKV VLAPLALIGVLIVQLVVATPLNPFFTFAAIVFLLGTVAVCGLGARCRDVPGVLESIAVAV IIGGLLTVAIECLHLFRVSGLPINWISIMPTGAGRRMWGNLNQPNHVATYLAFGLAACLF LGSTRRRYWAPLAAIALALLLGMALTVSRMSWLHLVLVGGVAGLAWSAEERGARRWIRAG VPVLGLAVVYQLCNWLVAYANVLWHLDLPISLDERLQQGVGLRVFLWKHAWHMFLAHPWL GGGWGDYAWNQYVQTDVLGHVEMSMNAHNLVLDLLAKVGVFGLLAVMLPFLGLVHAAWKR RMTPALAFLYAVILVTVAHSMLEYPLHYLYFLLPFAFALGYVDDRKSRVLSPDTAWVLTG IVAICGAVLTGRMWIDYQSVERLYYSLDGPVELQRYQRSGQLLLVPYGNLSIANNAGMTA ETAPIMAAVEHQAVQFYPGSGTVQRWAIALAFQGKTDEALTQVRRLHNQYWIDYAGDSKL LTLVCTKKLEGLATFCARLKAENLVVGVD |
| EMBL CDS | CAD14089.1 |
| Sequence length | 569 AA |
| Subcellular Location | Membrane (Integral component of membrane) |
| Function in Native Organism | 1) PglLRs is essential for O-glycosylation. |
| String | 267608.RSc0559 |
| Additional Information | 1) Deletion of gene encoding PglLRs shows complete loss of protein glycosylation, together with a defect in biofilm formation and reduced pathogenicity towards tomato plants. 2) PglLRs can transfer a diNAcBac to a Neisseria protein (DsbA) when co-expressed in E. coli. |
| Glycosyltransferase Information | |
| Glycosylation Type | O- (Ser/Thr) linked |
| EC Number (BRENDA) | 2.4.99.18 |
| Mechanism of Glycan Transfer | En bloc |
| Donor Type | Lipid linked sugars |
| Glycan Information | |
| Glycan transferred | Pentasaccharide (HexNAc-(Pen)-dHex3) and bacillosamine |
| Method of Glycan Indentification | LC-MS and MS/MS (HCD and CID) |
| Experimental_strategies | In vivo |
| Acceptor Subtrate Information | |
| Acceptor Substrate name | Putative membrane fusion protein |
| ProGPdb ID | ProGP522 |
| Acceptor Substrate name | FtsN |
| ProGPdb ID | ProGP528 |
| Acceptor Substrate name | AcrA |
| ProGPdb ID | ProGP529 |
| Acceptor Substrate name | Probable tpr domain signal peptide protein |
| ProGPdb ID | ProGP527 |
| Acceptor Substrate name | RagB |
| ProGPdb ID | ProGP528 |
| Acceptor Substrate name | Hypothetical signal peptide protein |
| ProGPdb ID | ProGP525 |
| Acceptor Substrate name | Probable transmembrane protein |
| ProGPdb ID | ProGP522 |
| Acceptor Substrate name | Probable lipoprotein transmembrane |
| ProGPdb ID | ProGP523 |
| Acceptor Substrate name | Probable peptidase transmembrane protein |
| ProGPdb ID | ProGP522 |
| Acceptor Substrate name | FtsL |
| ProGPdb ID | ProGP541 |
| Acceptor Substrate name | PilA |
| ProGPdb ID | ProGP539 |
| Acceptor Substrate name | Probable transmembrane protein |
| ProGPdb ID | ProGP540 |
| Acceptor Substrate name | Peptidyl-prolyl cis-trans isomerase |
| ProGPdb ID | ProGP539 |
| Acceptor Substrate name | Probable transmembrane protein |
| ProGPdb ID | ProGP538 |
| Acceptor Substrate name | Probable lipoprotein |
| ProGPdb ID | ProGP535 |
| Acceptor Substrate name | PilN |
| ProGPdb ID | ProGP534 |
| Acceptor Substrate name | Probable m20-related peptidase |
| ProGPdb ID | ProGP533 |
| Acceptor Substrate name | Probable serine protease protein |
| ProGPdb ID | ProGP532 |
| Acceptor Substrate name | Probable transmembrane protein |
| ProGPdb ID | ProGP531 |
| Acceptor Substrate name | D-(−)-3-hydroxybutyrate oligomer hydrolase |
| ProGPdb ID | ProGP530 |
| Acceptor Substrate name | PilA |
| ProGPdb ID | ProGP539 |
| Litrature | |
| Year Of Validation | 2015 |
| Reference | Elhenawy, W., Scott, N. E., Tondo, M. L., Orellano, E. G., Foster, L. J., & Feldman, M. F. (2015). Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum. Glycobiology, 26(3), 301-311. |
| Authors | Elhenawy, W., Scott, N. E., Tondo, M. L., Orellano, E. G., Foster, L. J., & Feldman, M. F. |
| Research groups | 1 Department of Biological Sciences, University of Alberta, Edmonton, AB, Canada. 2 Centre for High-Throughput Biology, University of British Columbia, Vancouver, BC, Canada. 3 Faculty of Biochemical and Pharmaceutical Sciences (FBIOYF-UNR), Institute of Molecular and Cellular Biology of Rosario (IBR-CONICET), Rosario, Santa Fe, Argentina. 4 Department of Biological Sciences, University of Alberta, Edmonton, AB, Canada Department of Molecular Microbiology, Washington University School of Medicine St. Louis, St. Louis, MO, USA. |
| Corresponding Author | Feldman, M. F. |
| Contacts | Department of Biological Sciences, University of Alberta, Edmonton, AB, Canada Department of Molecular Microbiology, Washington University School of Medicine St. Louis, St. Louis, MO, USA |