ProGT104 (PglLRs)
ProGT ID | ProGT104 (PglLRs) |
Organism Information | |
Organism Name | Ralstonia solanacearum GMI1000 |
Clinical Implication | Plant pathogen |
Domain | Bacteria |
Classification | Phylum : Proteobacteria Class : BetaProteobacteria Orders : Burkholderiales Family : Burkholderiaceae Genus : Ralstonia Species : solanacearum Strain : GMI1000 |
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 Escherichia coli. |
Glycosyltransferase Information | |
Glycosylation Type | O- (Ser/Thr) linked |
EC Number (BRENDA) | 2.4.99.18 |
Mechanism of Glycan Transfer | En bloc |
Donor Specificity | 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. and Feldman, M.F., 2016. Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum. Glycobiology, 26(3), pp.301-311. |
Corresponding Author | 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 |