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http://purl.uniprot.org/citations/17693724http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17693724http://www.w3.org/2000/01/rdf-schema#comment"In the Gram-positive bacterium Bacillus subtilis as well as in other firmicutes, the HPr protein of the phosphotransferase system (PTS) has two distinct phosphorylation sites, His-15 and Ser-46. These sites are phosphorylated by the Enzyme I of the PTS and by the ATP-dependent HPr kinase/phosphorylase, respectively. As a result, the phosphorylation state of HPr reflects the nutrient supply of the cell and is in turn involved in several responses at the levels of transport activity and expression of catabolic genes. Most important, HPr(Ser-P) serves as a cofactor for the pleiotropic transcription regulator CcpA. In addition to the proteins that phosphorylate HPr, those that are involved in the dephosphorylation are important in controlling the overall HPr phosphorylation state and the resulting regulatory and physiological outputs. In this study, we found that in addition to the phosphorylase activity of the HPr kinase/phosphorylase, the serine/threonine protein phosphatase PrpC uses HPr(Ser-P) as a target."xsd:string
http://purl.uniprot.org/citations/17693724http://purl.org/dc/terms/identifier"doi:10.1159/000103608"xsd:string
http://purl.uniprot.org/citations/17693724http://purl.uniprot.org/core/author"Stulke J."xsd:string
http://purl.uniprot.org/citations/17693724http://purl.uniprot.org/core/author"Halbedel S."xsd:string
http://purl.uniprot.org/citations/17693724http://purl.uniprot.org/core/author"Gorke B."xsd:string
http://purl.uniprot.org/citations/17693724http://purl.uniprot.org/core/author"Singh K.D."xsd:string
http://purl.uniprot.org/citations/17693724http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17693724http://purl.uniprot.org/core/name"J Mol Microbiol Biotechnol"xsd:string
http://purl.uniprot.org/citations/17693724http://purl.uniprot.org/core/pages"165-171"xsd:string
http://purl.uniprot.org/citations/17693724http://purl.uniprot.org/core/title"Control of the phosphorylation state of the HPr protein of the phosphotransferase system in Bacillus subtilis: implication of the protein phosphatase PrpC."xsd:string
http://purl.uniprot.org/citations/17693724http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/17693724http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17693724
http://purl.uniprot.org/citations/17693724http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17693724
http://purl.uniprot.org/uniprot/#_P08877-mappedCitation-17693724http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17693724
http://purl.uniprot.org/uniprot/P08877http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17693724