Inhibitors | Comment | Organism | Structure |
---|---|---|---|
SidK | a protein of Legionella pneumophila, an intracellular pathogen, specifically targets host v-ATPase. SidK interacts via an N-terminal portion with VatA, a key component of the proton pump leading to the inhibition of ATP hydrolysis and proton translocation. SidK inhibits vacuole acidification and impairs the ability of the cells to digest non-pathogenic Escherichia coli | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
lysosome | - |
Saccharomyces cerevisiae | 5764 | - |
vacuole | - |
Saccharomyces cerevisiae | 5773 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + H+/in | Saccharomyces cerevisiae | - |
ADP + phosphate + H+/out | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + H+/in | - |
Saccharomyces cerevisiae | ADP + phosphate + H+/out | - |
? |
Synonyms | Comment | Organism |
---|---|---|
V-ATPase | - |
Saccharomyces cerevisiae |
vacuolar H+-ATPase | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
physiological function | v-ATPase is a multi-subunit machinery primarily responsible for organelle acidification in eukaryotic cells | Saccharomyces cerevisiae |