|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
Mass balance status: Balance undetermined; a substrate lacks a chemical formula
In this reaction the sensor kinase-phosphotransferase PhoQ autophosphorylates. Based on analogy to other sensor proteins the phosphorylation site is shown as a histidine residue.
Sensor kinase-phosphotransferase PhoQ is a member of the two-component regulatory system PhoQ/PhoP. In E. coli this system is believed to play a role in Mg++, or other divalent cation, starvation response. The PhoQ protein responds to low concentrations of extracellular divalent cations by autophosphorylating and activating the transcription regulator PhoP by transfer of the phosphate group. [Waldburger96, Kasahara92]
Waldburger96: Waldburger CD, Sauer RT (1996). "Signal detection by the PhoQ sensor-transmitter. Characterization of the sensor domain and a response-impaired mutant that identifies ligand-binding determinants." J Biol Chem 1996;271(43);26630-6. PMID: 8900137
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