Reaction: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
Other name(s): EnvZ; histidine kinase (ambiguous); histidine protein kinase (ambiguous); protein histidine kinase (ambiguous); protein kinase (histidine) (ambiguous); HK1; HP165; Sln1p
Systematic name: ATP:protein-L-histidine N-phosphotransferase
Comments: This entry has been included to accommodate those protein-histidine kinases for which the phosphorylation site has not been established (i.e. either the pros- or tele-nitrogen of histidine). A number of histones can act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 420839-67-4
References:
1. Kowluru, A. Identification and characterization of a novel protein histidine kinase in the islet beta cell: evidence for its regulation by mastoparan, an activator of G-proteins and insulin secretion. Biochem. Pharmacol. 63 (2002) 2091-2100. [PMID: 12110368]
2. Yoshimi, A., Tsuda, M. and Tanaka, C. Cloning and characterization of the histidine kinase gene Dic1 from Cochliobolus heterostrophus that confers dicarboximide resistance and osmotic adaptation. Mol. Genet. Genomics 271 (2004) 228-236. [PMID: 14752661]
3. Beier, D. and Frank, R. Molecular characterization of two-component systems of Helicobacter pylori. J. Bacteriol. 182 (2000) 2068-2076. [PMID: 10735847]
4. Pflock, M., Dietz, P., SchŠr, J. and Beier, D. Genetic evidence for histidine kinase HP165 being an acid sensor of Helicobacter pylori. FEMS Microbiol. Lett. 34 (2004) 51-61. [PMID: 15109719]
5. Roberts, D.L., Bennett, D.W. and Forst, S.A. Identification of the site of phosphorylation on the osmosensor, EnvZ, of Escherichia coli. J. Biol. Chem. 269 (1994) 8728-8733. [PMID: 8132603]