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, Gene, 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. [DOI] [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. [DOI] [PMID: 14752661] |
3. |
Beier, D. and Frank, R. Molecular characterization of two-component systems of Helicobacter pylori. J. Bacteriol. 182 (2000) 2068–2076. [DOI] [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. [DOI] [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] |
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[EC 2.7.13.3 created 2005] |
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