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Literature summary extracted from
- Interaction of the Thermoplasma acidophilum A1A0-ATP synthase peripheral stalk with the catalytic domain (2009), FEBS Lett., 583, 3121-3126 .
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.1.2.2 | Thermoplasma acidophilum | NP_393483 | B subunit | - |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.1.2.2 | A-ATPase | - |
Thermoplasma acidophilum |
| 7.1.2.2 | A1A0-ATP synthase | - |
Thermoplasma acidophilum |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 7.1.2.2 | additional information | the peripheral stalk of the A1A0-ATP synthase is formed by the heterodimeric EH complex and is part of the stator domain, which counteracts the torque of rotational catalysis. The BNT peptide specifically interacts with 26 residues of the ECT1HCT domain | Thermoplasma acidophilum |
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Release 2023.1 (January 2023)
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