RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/17209016http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17209016http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17209016http://www.w3.org/2000/01/rdf-schema#comment"Thermobifida fusca is a moderately thermophilic soil bacterium that belongs to Actinobacteria. It is a major degrader of plant cell walls and has been used as a model organism for the study of secreted, thermostable cellulases. The complete genome sequence showed that T. fusca has a single circular chromosome of 3,642,249 bp predicted to encode 3,117 proteins and 65 RNA species with a coding density of 85%. Genome analysis revealed the existence of 29 putative glycoside hydrolases in addition to the previously identified cellulases and xylanases. The glycosyl hydrolases include enzymes predicted to exhibit mainly dextran/starch- and xylan-degrading functions. T. fusca possesses two protein secretion systems: the sec general secretion system and the twin-arginine translocation system. Several of the secreted cellulases have sequence signatures indicating their secretion may be mediated by the twin-arginine translocation system. T. fusca has extensive transport systems for import of carbohydrates coupled to transcriptional regulators controlling the expression of the transporters and glycosylhydrolases. In addition to providing an overview of the physiology of a soil actinomycete, this study presents insights on the transcriptional regulation and secretion of cellulases which may facilitate the industrial exploitation of these systems."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.org/dc/terms/identifier"doi:10.1128/jb.01899-06"xsd:string
http://purl.uniprot.org/citations/17209016http://purl.org/dc/terms/identifier"doi:10.1128/jb.01899-06"xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Copeland A."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Copeland A."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Ivanova N."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Ivanova N."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Kyrpides N."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Kyrpides N."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Land M."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Land M."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Lapidus A."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Lapidus A."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Lucas S."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Lucas S."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Mavromatis K."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Mavromatis K."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Anderson I."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Anderson I."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Lykidis A."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Lykidis A."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Martinez M."xsd:string
http://purl.uniprot.org/citations/17209016http://purl.uniprot.org/core/author"Martinez M."xsd:string