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Literature summary for 2.7.13.3 extracted from

  • Bortolotti, A.; Vazquez, D.; Almada, J.; Inda, M.; Drusin, S.; Villalba, J.; Moreno, D.; Ruysschaert, J.; Cybulski, L.
    A transmembrane histidine kinase functions as a pH sensor (2020), Biomolecules, 10, 1183 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.13.3

Protein Variants

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

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Bacillus subtilis 16020
-

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O34757
-
-
Bacillus subtilis 168 O34757
-
-

Synonyms

Synonyms Comment Organism
DesK
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 Bacillus subtilis
sensor histidine kinase DesK
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 Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
7
-
 catalytic activity is inhibited below pH 7 Bacillus subtilis

General Information

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