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http://purl.uniprot.org/citations/1556077http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1556077http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1556077http://www.w3.org/2000/01/rdf-schema#comment"Plasmid pIP816 of Enterococcus faecium BM4147 confers inducible resistance to vancomycin and encodes the VanH dehydrogenase and the VanA ligase for synthesis of depsipeptide-containing peptidoglycan precursors which bind the antibiotic with reduced affinity. We have characterized a cluster of five genes of pIP816 sufficient for peptidoglycan synthesis in the presence of vancomycin. The distal part of the van cluster encodes VanH, VanA, and a third enzyme, VanX, all of which are necessary for resistance. Synthesis of these enzymes was regulated at the transcriptional level by the VanS-VanR two-component regulatory system encoded by the proximal part of the cluster. VanR was a transcriptional activator related to response regulators of the OmpR subclass. VanS stimulated VanR-dependent transcription and was related to membrane-associated histidine protein kinases which control the level of phosphorylation of response regulators. Analysis of transcriptional fusions with a reporter gene and RNA mapping indicated that the VanR-VanS two-component regulatory system activates a promoter used for cotranscription of the vanH, vanA, and vanX resistance genes."xsd:string
http://purl.uniprot.org/citations/1556077http://purl.org/dc/terms/identifier"doi:10.1128/jb.174.8.2582-2591.1992"xsd:string
http://purl.uniprot.org/citations/1556077http://purl.org/dc/terms/identifier"doi:10.1128/jb.174.8.2582-2591.1992"xsd:string
http://purl.uniprot.org/citations/1556077http://purl.uniprot.org/core/author"Courvalin P."xsd:string
http://purl.uniprot.org/citations/1556077http://purl.uniprot.org/core/author"Courvalin P."xsd:string
http://purl.uniprot.org/citations/1556077http://purl.uniprot.org/core/author"Arthur M."xsd:string
http://purl.uniprot.org/citations/1556077http://purl.uniprot.org/core/author"Arthur M."xsd:string
http://purl.uniprot.org/citations/1556077http://purl.uniprot.org/core/author"Molinas C."xsd:string
http://purl.uniprot.org/citations/1556077http://purl.uniprot.org/core/author"Molinas C."xsd:string
http://purl.uniprot.org/citations/1556077http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1556077http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1556077http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/1556077http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/1556077http://purl.uniprot.org/core/pages"2582-2591"xsd:string
http://purl.uniprot.org/citations/1556077http://purl.uniprot.org/core/pages"2582-2591"xsd:string
http://purl.uniprot.org/citations/1556077http://purl.uniprot.org/core/title"The VanS-VanR two-component regulatory system controls synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147."xsd:string
http://purl.uniprot.org/citations/1556077http://purl.uniprot.org/core/title"The VanS-VanR two-component regulatory system controls synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147."xsd:string
http://purl.uniprot.org/citations/1556077http://purl.uniprot.org/core/volume"174"xsd:string
http://purl.uniprot.org/citations/1556077http://purl.uniprot.org/core/volume"174"xsd:string
http://purl.uniprot.org/citations/1556077http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1556077
http://purl.uniprot.org/citations/1556077http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1556077
http://purl.uniprot.org/citations/1556077http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1556077
http://purl.uniprot.org/citations/1556077http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1556077