Protein Variants | Comment | Organism |
---|---|---|
H5K | mutation in extracellular tail, mutant is sensitive to pH | Bacillus subtilis |
K32E/E36K | mutations in linker region, mutant shows higher activity at higher pH and maintains pH regulation | Bacillus subtilis |
additional information | a truncated version of DesK, which lacks the transmembrane domain, is not pH-dependent | Bacillus subtilis |
R34E/ E36K/ R37E | mutations in linker region, mutant is inactive and insensitive to pH | Bacillus subtilis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Bacillus subtilis | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | O34757 | - |
- |
Bacillus subtilis 168 | O34757 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
DesK | - |
Bacillus subtilis |
sensor histidine kinase DesK | - |
Bacillus subtilis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
7 | - |
catalytic activity is inhibited below pH 7 | Bacillus subtilis |
General Information | Comment | Organism |
---|---|---|
physiological function | a helix linking the transmembrane region with the cytoplasmic catalytic domain is involved in DesK pH sensing. This helix contains several glutamate, lysine, and arginine residues At neutral pH, the linker forms an alpha helix that is stabilized by hydrogen bonds in the i, i + 4 register and favors the kinase state. At low pH, protonation of glutamate residues breaks salt bridges, which results in helix destabilization and interruption of signaling. This mechanism inhibits unsaturated fatty acid synthesis and rigidifies the membrane when Bacillus subtilis grows in acidic conditions | Bacillus subtilis |