PMID:2512998

Citation	Cegielska, A and Georgopoulos, C Biochemical properties of the Escherichia coli dnaK heat shock protein and its mutant derivatives. Biochimie 71:1071-7
Abstract	The dnaK protein of Escherichia coli has been shown to possess both autophosphorylating and 5'-nucleotidase activities. The dnaK protein has been shown to bind avidly to ATP, but hydrolyzing it slowly. In vitro autophosphorylation occurs at a threonine residue when either ATP or GTP are used as phosphate donors. The extent of autophosphorylation is low; only a few percent of the molecules are phosphorylated. This activity is stimulated at least tenfold in the presence of Ca2+ ions with either ATP or GTP as the donor. The autophosphorylating activity of the mutant dnaK756 protein in the presence or absence of Ca2+ is reduced compared to that of the wild type.
Links	PubMed
Keywords	Amino Acids/analysis; Calcium/pharmacology; Electrophoresis, Gel, Two-Dimensional; Escherichia coli/drug effects; Escherichia coli/genetics; Escherichia coli/metabolism; Guanosine Triphosphate/metabolism; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Mutation; Phosphorylation
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