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pubmed-article:2512998pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:2512998pubmed:articleTitleBiochemical properties of the Escherichia coli dnaK heat shock protein and its mutant derivatives.lld:pubmed
pubmed-article:2512998pubmed:affiliationDepartment of Cellular, Viral and Molecular Biology, University of Utah Medical Center, Salt Lake City 84132.lld:pubmed
pubmed-article:2512998pubmed:publicationTypeJournal Articlelld:pubmed
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