The Enzyme Database

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EC 2.7.13.3     
Accepted name: histidine kinase
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 β 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., Schar, J. and Beier, D. Genetic evidence for histidine kinase HP165 being an acid sensor of Helicobacter pylori. FEMS Microbiol. Lett. 234 (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]
[EC 2.7.13.3 created 2005]
 
 


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