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Literature summary for 2.7.13.3 extracted from
- The histidine kinase inhibitor Sda binds near the site of autophosphorylation and may sterically hinder autophosphorylation and phosphotransfer to Spo0F (2009), Mol. Microbiol., 71, 659-677.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| A413R | the mutation impairs KinA activity, folding or stability | Bacillus subtilis |
| Ala413L | the mutation impairs KinA activity, folding or stability | Bacillus subtilis |
| F432C | the substitution has less effect on Sda binding | Bacillus subtilis |
| F436S | the mutation increases the efficiency of sporulation in cells overexpressing KinA inhibitor Sda by about 10fold while actually reducing the efficiency of sporulation in cells that lack sda | Bacillus subtilis |
| H430C | the substitution has less effect on Sda binding | Bacillus subtilis |
| P410L | the mutation increases the efficiency of sporulation in cells overexpressing KinA inhibitor Sda by about 10fold while actually reducing the efficiency of sporulation in cells that lack sda | Bacillus subtilis |
| P410L/F436S | the mutant has a low affinity for inhibitor Sda | Bacillus subtilis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| KipI | - |
Bacillus subtilis | |
| Sda | - |
Bacillus subtilis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | - |
Bacillus subtilis |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Ni2+-NTA agarose column chromatography | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + Spo0F protein L-histidine | - |
Bacillus subtilis | ADP + Spo0F protein N-phospho-L-histidine | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| KINA | - |
Bacillus subtilis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Bacillus subtilis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | histidine kinase KinA promotes the initiation of sporulation when nutrients are limiting | Bacillus subtilis |
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Release 2023.1 (January 2023)
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