title: Genetic and biochemical studies of phosphatase activity of PhoR.
abstract: In Escherichia coli, PhoR is the histidine kinase of the phosphate regulon. It has been postulated that PhoR may function as a phospho-PhoB phosphatase. Experiments with four precise phoR deletion mutants supported this hypothesis and suggested that this activity resides within the histidine phosphorylation domain. This biochemical activity was confirmed by using a separately expressed histidine phosphorylation domain.
authors.affiliation: Microbiology and Molecular Biology Department, Brigham Young University, Provo, UT 84602-5253, USA.
authors.forename: Daniel O
authors.initials: DO
authors.lastname: Carmany
authors.forename: Kristine
authors.initials: K
authors.lastname: Hollingsworth
authors.forename: William R
authors.initials: WR
authors.lastname: McCleary
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D006639:Histidine / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D010766:Phosphorylation
chemical_list: D001426:Bacterial Proteins; C061279:PhoR protein, Bacteria; D006639:Histidine; D000255:Adenosine Triphosphate; D010744:Phosphoric Monoester Hydrolases