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Literature summary for 3.4.24.B17 extracted from
- Cellular functions, mechanism of action, and regulation of FtsH protease (2005), Annu. Rev. Microbiol., 59, 211-231.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytoplasmic membrane | FtsH has N-terminally located transmembrane segments and a main cytosolic region consisting of AAA-ATPase and Zn2+-metalloprotease domains | Escherichia coli | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | degradation of sigma32 is dependent on Zn2+ | Escherichia coli |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| LpxC + H2O | Escherichia coli | ATP-dependent. Essentiality of FtsH lies in its function to keep the proper LPS/phospholipid ratio by degrading LpxC | ? | - |
? | |
| protein + H2O | Escherichia coli | FtsH degrades a set of short-lived proteins, enabling cellular regulation at the level of protein stability. FtsH also degrades some misassembles membrane proteins, contributing to their quality maintenance. One biological role of FtsH might be to affect the development and life cycle of infecting or episomal genetic systems, by degrading their key regulatory molecules. The enzyme has a special ability to dislocate membrane protein substrates out of the membrane for which its own membrane-embedded nature is essential | peptides | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | FtsH undergoes self-cleavage between M640 and S641, removing seven C-terminal residues. Functional significance of this self-cleavage reaction is obscure, as both the full-length and the processed forms of FtsH are active as protease | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| LpxC + H2O | ATP-dependent. Essentiality of FtsH lies in its function to keep the proper LPS/phospholipid ratio by degrading LpxC | Escherichia coli | ? | - |
? | |
| LpxC + H2O | ATP-dependent | Escherichia coli | ? | - |
? | |
| protein + H2O | FtsH degrades a set of short-lived proteins, enabling cellular regulation at the level of protein stability. FtsH also degrades some misassembles membrane proteins, contributing to their quality maintenance. One biological role of FtsH might be to affect the development and life cycle of infecting or episomal genetic systems, by degrading their key regulatory molecules. The enzyme has a special ability to dislocate membrane protein substrates out of the membrane for which its own membrane-embedded nature is essential | Escherichia coli | peptides | - |
? | |
| sigma32 + H2O | ATP- and Zn2+-dependent degradation | Escherichia coli | ? | - |
? | |
| SoxS + H2O | - |
Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | - |
Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FtsH | - |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | degradation of sigma32 and LpxC is dependent on | Escherichia coli | |
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