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Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP. Catalysis of the reaction: ATP + protein L-histidine = ADP + protein phospho-L-histidine. Catalysis of the reaction: ATP + protein L-histidine = ADP + protein N(tau)-phospho-L-histidine. Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule. A transmembrane receptor that perceives a stimulus and that produces a molecular signal via phosphotransfer at histidine residues. Catalysis of the reaction: ATP + protein L-histidine = ADP + protein N(pi)-phospho-L-histidine. Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to an alcohol group (acceptor). Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to a nitrogenous group (acceptor). Catalysis of the phosphorylation of a specific transcription regulator in response to the presence of a particular signal substance outside the cell. Catalysis of the transfer of a phosphorus-containing group from one compound (donor) to another (acceptor).

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: protein histidine kinase activity
Acc: GO:0004673
Aspect: Molecular Function
Desc: Catalysis of the reaction: ATP + protein L-histidine = ADP + protein phospho-L-histidine.
Synonyms:
  • histidine kinase (ambiguous)
  • histidine protein kinase (ambiguous)
  • protein kinase (histidine)
  • histidine protein kinase activity
  • GO:0008896
  • protein histidine kinase (ambiguous)
  • EnvZ
  • histidine kinase activity
  • HK1
  • Sln1p
  • protein-histidine kinase activity
  • ATP:protein-L-histidine N-phosphotransferase activity
  • HP165
  • protein kinase (histidine) (ambiguous)
Proteins in PDR annotated with:
   This term: 73 [Search]
   Term or descendants: 424 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0004673 - protein histidine kinase activity (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle