| http://purl.uniprot.org/citations/11736654 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11736654 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11736654 | http://www.w3.org/2000/01/rdf-schema#comment | "Two distinct families of protein kinases are involved in signal transduction: Ser, Thr and Tyr kinases, which are predominantly found among eukaryotes, and His kinases, as part of bacterial two-component signalling systems. Genetic studies in Arabidopsis and Saccharomyces have demonstrated that bacterial-type two-component systems may act upstream of Ser/Thr kinases in the same signalling pathway, but how this coupling is accomplished remains unclear. In the present study, we report the characterization of a protein kinase, HstK, from the N(2)-fixing cyanobacterium Anabaena sp. PCC 7120, that possesses both a Ser/Thr kinase domain and a His kinase domain. Proteins with a structural architecture similar to that of HstK can be found in the eukaryote, Schizosaccharomyces pombe, and the bacterium, Rhodococcus sp. M5. HstK was present in cells grown with NH(4)(+) or N(2) as the nitrogen source, but was absent in cells grown with NO(3)(-). The hstK gene was inactivated and the mutant phenotype was characterized. The catalytic domain of the Ser/Thr kinase of HstK functionally replaced that of Hog1p, a well-characterized protein kinase required for the response to high osmolarity in the S. cerevisiae heterologous system. The unusual multidomain structure of HstK suggests that a two-component system could be directly coupled to Ser/Thr kinases in the same signal transduction pathway."xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://purl.org/dc/terms/identifier | "doi:10.1042/0264-6021:3600639"xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://purl.org/dc/terms/identifier | "doi:10.1042/0264-6021:3600639"xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://purl.uniprot.org/core/author | "Li J.H."xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://purl.uniprot.org/core/author | "Li J.H."xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://purl.uniprot.org/core/author | "Zhang C.C."xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://purl.uniprot.org/core/author | "Zhang C.C."xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://purl.uniprot.org/core/author | "Phalip V."xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://purl.uniprot.org/core/author | "Phalip V."xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11736654 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11736654 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://purl.uniprot.org/core/pages | "639-644"xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://purl.uniprot.org/core/pages | "639-644"xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://purl.uniprot.org/core/title | "HstK, a cyanobacterial protein with both a serine/threonine kinase domain and a histidine kinase domain: implication for the mechanism of signal transduction."xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://purl.uniprot.org/core/title | "HstK, a cyanobacterial protein with both a serine/threonine kinase domain and a histidine kinase domain: implication for the mechanism of signal transduction."xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://purl.uniprot.org/core/volume | "360"xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://purl.uniprot.org/core/volume | "360"xsd:string |
| http://purl.uniprot.org/citations/11736654 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11736654 |
| http://purl.uniprot.org/citations/11736654 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11736654 |
| http://purl.uniprot.org/citations/11736654 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11736654 |
| http://purl.uniprot.org/citations/11736654 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11736654 |