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http://purl.uniprot.org/citations/10500118http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10500118http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10500118http://www.w3.org/2000/01/rdf-schema#comment"The zinc-containing D-alanyl-D-alanine (D-Ala-D-Ala) dipeptidase VanX has been detected in both Gram-positive and Gram-negative bacteria, where it appears to have adapted to at least three distinct physiological roles. In pathogenic vancomycin-resistant enterococci, vanX is part of a five-gene cluster that is switched on to reprogram cell-wall biosynthesis to produce peptidoglycan chain precursors terminating in D-alanyl-D-lactate (D-Ala-D-lactate) rather than D-Ala-D-Ala. The modified peptidoglycan exhibits a 1, 000-fold decrease in affinity for vancomycin, accounting for the observed phenotypic resistance. In the glycopeptide antibiotic producers Streptomyces toyocaensis and Amylocatopsis orientalis, a vanHAX operon may have coevolved with antibiotic biosynthesis genes to provide immunity by reprogramming cell-wall termini to D-Ala-D-lactate as antibiotic biosynthesis is initiated. In the Gram-negative bacterium Escherichia coli, which is never challenged by the glycopeptide antibiotics because they cannot penetrate the outer membrane permeability barrier, the vanX homologue (ddpX) is cotranscribed with a putative dipeptide transport system (ddpABCDF) in stationary phase by the transcription factor RpoS (sigma(s)). The combined action of DdpX and the permease would permit hydrolysis of D-Ala-D-Ala transported back into the cytoplasm from the periplasm as cell-wall crosslinks are refashioned. The D-Ala product could then be oxidized as an energy source for cell survival under starvation conditions."xsd:string
http://purl.uniprot.org/citations/10500118http://purl.org/dc/terms/identifier"doi:10.1073/pnas.96.20.11028"xsd:string
http://purl.uniprot.org/citations/10500118http://purl.org/dc/terms/identifier"doi:10.1073/pnas.96.20.11028"xsd:string
http://purl.uniprot.org/citations/10500118http://purl.uniprot.org/core/author"Walsh C.T."xsd:string
http://purl.uniprot.org/citations/10500118http://purl.uniprot.org/core/author"Walsh C.T."xsd:string
http://purl.uniprot.org/citations/10500118http://purl.uniprot.org/core/author"Lessard I.A.D."xsd:string
http://purl.uniprot.org/citations/10500118http://purl.uniprot.org/core/author"Lessard I.A.D."xsd:string
http://purl.uniprot.org/citations/10500118http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10500118http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10500118http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/10500118http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/10500118http://purl.uniprot.org/core/pages"11028-11032"xsd:string
http://purl.uniprot.org/citations/10500118http://purl.uniprot.org/core/pages"11028-11032"xsd:string
http://purl.uniprot.org/citations/10500118http://purl.uniprot.org/core/title"VanX, a bacterial D-alanyl-D-alanine dipeptidase: resistance, immunity, or survival function?"xsd:string
http://purl.uniprot.org/citations/10500118http://purl.uniprot.org/core/title"VanX, a bacterial D-alanyl-D-alanine dipeptidase: resistance, immunity, or survival function?"xsd:string
http://purl.uniprot.org/citations/10500118http://purl.uniprot.org/core/volume"96"xsd:string
http://purl.uniprot.org/citations/10500118http://purl.uniprot.org/core/volume"96"xsd:string
http://purl.uniprot.org/citations/10500118http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10500118
http://purl.uniprot.org/citations/10500118http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10500118
http://purl.uniprot.org/citations/10500118http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10500118
http://purl.uniprot.org/citations/10500118http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10500118
http://purl.uniprot.org/uniprot/P76128http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10500118
http://purl.uniprot.org/uniprot/P77308http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10500118