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http://purl.uniprot.org/citations/27028884http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27028884http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27028884http://www.w3.org/2000/01/rdf-schema#comment"The discovery of new ribosomally synthesized and post-translationally modified peptide natural products (RiPPs) has greatly benefitted from the influx of genomic information. The lanthipeptides are a subset of this class of compounds. Adopting the genome-mining approach revealed a novel lanthipeptide gene cluster encoded in the genome of Ruminococcus flavefaciens FD-1, an anaerobic bacterium that is an important member of the rumen microbiota of livestock. The post-translationally modified peptides were produced via heterologous expression in Escherichia coli. Subsequent structural characterization and assessment of their bioactivity revealed features reminiscent of and distinct from previously reported lanthipeptides. The lanthipeptides of R. flavefaciens FD-1 represent a unique example within two-component lanthipeptides, consisting of a highly conserved α-peptide and a diverse set of eight β-peptides."xsd:string
http://purl.uniprot.org/citations/27028884http://purl.org/dc/terms/identifier"doi:10.1016/j.chembiol.2015.11.014"xsd:string
http://purl.uniprot.org/citations/27028884http://purl.org/dc/terms/identifier"doi:10.1016/j.chembiol.2015.11.014"xsd:string
http://purl.uniprot.org/citations/27028884http://purl.uniprot.org/core/author"Zhao X."xsd:string
http://purl.uniprot.org/citations/27028884http://purl.uniprot.org/core/author"Zhao X."xsd:string
http://purl.uniprot.org/citations/27028884http://purl.uniprot.org/core/author"van der Donk W.A."xsd:string
http://purl.uniprot.org/citations/27028884http://purl.uniprot.org/core/author"van der Donk W.A."xsd:string
http://purl.uniprot.org/citations/27028884http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27028884http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27028884http://purl.uniprot.org/core/name"Cell Chem. Biol."xsd:string
http://purl.uniprot.org/citations/27028884http://purl.uniprot.org/core/name"Cell Chem. Biol."xsd:string
http://purl.uniprot.org/citations/27028884http://purl.uniprot.org/core/pages"246-256"xsd:string
http://purl.uniprot.org/citations/27028884http://purl.uniprot.org/core/pages"246-256"xsd:string
http://purl.uniprot.org/citations/27028884http://purl.uniprot.org/core/title"Structural characterization and bioactivity analysis of the two-component lantibiotic Flv system from a ruminant bacterium."xsd:string
http://purl.uniprot.org/citations/27028884http://purl.uniprot.org/core/title"Structural characterization and bioactivity analysis of the two-component lantibiotic Flv system from a ruminant bacterium."xsd:string
http://purl.uniprot.org/citations/27028884http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/27028884http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/27028884http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27028884
http://purl.uniprot.org/citations/27028884http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27028884
http://purl.uniprot.org/citations/27028884http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27028884
http://purl.uniprot.org/citations/27028884http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27028884
http://purl.uniprot.org/uniprot/P0DQL5http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/27028884
http://purl.uniprot.org/uniprot/P0DQL4http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/27028884