Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrial inner membrane | integral, active at the matrix side of the inner membrane | Saccharomyces cerevisiae | 5743 | - |
mitochondrion | - |
Saccharomyces cerevisiae | 5739 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | a consensus metal-binding site represents the proteolytic centre, metallopeptidase of the M41 family | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
protein + H2O | Saccharomyces cerevisiae | quality control system to selectively remove non-assembled polypeptides and to prevent their possible deleterious accumulation in the membrane, enzyme is crucial for viability | peptides | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
proteolytic degradation of proteins | mechanism, m-AAA protease shows overlapping substrate specificity with the i-AAA protease, intermolecular catalytic role of SRH domain at the C-terminus of the AAA domain, m-AAA protease shows overlapping substrate specificity with the i-AAA protease, enzyme degrades domains of substrate proteins exposed to the opposite membrane surface, active site contains the conserved motif HEXXH, a helical region is located at the extreme C-terminus of the subunit | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
protein + H2O | activity depends on oligomerisation | Saccharomyces cerevisiae | peptides | - |
? | |
protein + H2O | quality control system to selectively remove non-assembled polypeptides and to prevent their possible deleterious accumulation in the membrane, enzyme is crucial for viability | Saccharomyces cerevisiae | peptides | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | subunits span the membrane twice, activity depends on oligomerisation, the enzyme consists of a AAA domain, providing chaperone-like properties and binding to the unfolded, solvent-exposed domains of the substrate protein, a proteolytic domain, and a Walker-type P-loop ATPase domain | Saccharomyces cerevisiae |
oligomer | x * 70000-80000, homooligomeric | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
M41.003 | Merops-ID | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | dependent on, enzyme contains an ATPase domain with a Walker-type P-loop typical for the AAA protease family | Saccharomyces cerevisiae |