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http://purl.uniprot.org/citations/16820517http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16820517http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16820517http://www.w3.org/2000/01/rdf-schema#comment"The Streptococcus agalactiae bacteriophage B30 endolysin contains three domains: cysteine, histidine-dependent amidohydrolase/peptidase (CHAP), Acm glycosidase, and the SH3b cell wall binding domain. Truncations and point mutations indicated that the Acm domain requires the SH3b domain for activity, while the CHAP domain is responsible for nearly all the cell lysis activity."xsd:string
http://purl.uniprot.org/citations/16820517http://purl.org/dc/terms/identifier"doi:10.1128/aem.03065-05"xsd:string
http://purl.uniprot.org/citations/16820517http://purl.org/dc/terms/identifier"doi:10.1128/aem.03065-05"xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/author"Dong S."xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/author"Dong S."xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/author"Moineau S."xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/author"Moineau S."xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/author"Donovan D.M."xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/author"Donovan D.M."xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/author"Foster-Frey J."xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/author"Foster-Frey J."xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/author"Pritchard D.G."xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/author"Pritchard D.G."xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/author"Rousseau G.M."xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/author"Rousseau G.M."xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/name"Appl. Environ. Microbiol."xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/name"Appl. Environ. Microbiol."xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/pages"5108-5112"xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/pages"5108-5112"xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/title"The cell lysis activity of the Streptococcus agalactiae bacteriophage B30 endolysin relies on the cysteine, histidine-dependent amidohydrolase/peptidase domain."xsd:string
http://purl.uniprot.org/citations/16820517http://purl.uniprot.org/core/title"The cell lysis activity of the Streptococcus agalactiae bacteriophage B30 endolysin relies on the cysteine, histidine-dependent amidohydrolase/peptidase domain."xsd:string