|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 reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
Mass balance status: The left side is missing: charge: +1 . The right side is missing: P: 1 O: 3
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]
Depressed by: Mg2+
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
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493