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http://purl.uniprot.org/citations/17237178http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17237178http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17237178http://www.w3.org/2000/01/rdf-schema#comment"The glycan chain of the S-layer glycoprotein of Geobacillus stearothermophilus NRS 2004/3a is composed of repeating units [-->2)-alpha-l-Rhap-(1-->3)-beta-l-Rhap-(1-->2)-alpha-l-Rhap-(1-->], with a 2-O-methyl modification of the terminal trisaccharide at the nonreducing end of the glycan chain, a core saccharide composed of two or three alpha-l-rhamnose residues, and a beta-d-galactose residue as a linker to the S-layer protein. In this study, we report the biochemical characterization of WsaP of the S-layer glycosylation gene cluster as a UDP-Gal:phosphoryl-polyprenol Gal-1-phosphate transferase that primes the S-layer glycoprotein glycan biosynthesis of Geobacillus stearothermophilus NRS 2004/3a. Our results demonstrate that the enzyme transfers in vitro a galactose-1-phosphate from UDP-galactose to endogenous phosphoryl-polyprenol and that the C-terminal half of WsaP carries the galactosyltransferase function, as already observed for the UDP-Gal:phosphoryl-polyprenol Gal-1-phosphate transferase WbaP from Salmonella enterica. To confirm the function of the enzyme, we show that WsaP is capable of reconstituting polysaccharide biosynthesis in WbaP-deficient strains of Escherichia coli and Salmonella enterica serovar Typhimurium."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.org/dc/terms/identifier"doi:10.1128/JB.01592-06"xsd:string
http://purl.uniprot.org/citations/17237178http://purl.org/dc/terms/identifier"doi:10.1128/jb.01592-06"xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/author"Messner P."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/author"Messner P."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/author"Patel K."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/author"Patel K."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/author"Steiner K."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/author"Steiner K."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/author"Vinogradov E."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/author"Vinogradov E."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/author"Valvano M.A."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/author"Valvano M.A."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/author"Whitfield C."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/author"Whitfield C."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/author"Novotny R."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/author"Novotny R."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/author"Schaffer C."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/author"Schaffer C."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/17237178http://purl.uniprot.org/core/name"J Bacteriol"xsd:string