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http://purl.uniprot.org/citations/11013210http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11013210http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11013210http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/11013210http://www.w3.org/2000/01/rdf-schema#comment"Regulated covalent modifications of lipid A are implicated in virulence of pathogenic Gram-negative bacteria. The Salmonella typhimurium PhoP/PhoQ-activated gene pagP is required both for biosynthesis of hepta-acylated lipid A species containing palmitate and for resistance to cationic anti-microbial peptides. Palmitoylated lipid A can also function as an endotoxin antagonist. We now show that pagP and its Escherichia coli homolog (crcA) encode an unusual enzyme of lipid A biosynthesis localized in the outer membrane. PagP transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A (or its precursors). PagP bearing a C-terminal His(6)-tag accumulated in outer membranes during overproduction, was purified with full activity and was shown by cross-linking to behave as a homodimer. PagP is the first example of an outer membrane enzyme involved in lipid A biosynthesis. Additional pagP homologs are encoded in the genomes of Yersinia and Bordetella species. PagP may provide an adaptive response toward both Mg(2+) limitation and host innate immune defenses."xsd:string
http://purl.uniprot.org/citations/11013210http://purl.org/dc/terms/identifier"doi:10.1093/emboj/19.19.5071"xsd:string
http://purl.uniprot.org/citations/11013210http://purl.org/dc/terms/identifier"doi:10.1093/emboj/19.19.5071"xsd:string
http://purl.uniprot.org/citations/11013210http://purl.org/dc/terms/identifier"doi:10.1093/emboj/19.19.5071"xsd:string
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/author"Guina T."xsd:string
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/author"Guina T."xsd:string
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/author"Miller S.I."xsd:string
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/author"Miller S.I."xsd:string
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/author"Gibbons H.S."xsd:string
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/author"Gibbons H.S."xsd:string
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/author"Raetz C.R."xsd:string
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/author"Raetz C.R."xsd:string
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/author"Trent M.S."xsd:string
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/author"Trent M.S."xsd:string
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/author"Bishop R.E."xsd:string
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/author"Bishop R.E."xsd:string
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/pages"5071-5080"xsd:string
http://purl.uniprot.org/citations/11013210http://purl.uniprot.org/core/pages"5071-5080"xsd:string