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Literature summary extracted from
- ATPase and protease domain movements in the bacterial AAA+ protease FtsH are driven by thermal fluctuations (2018), J. Mol. Biol., 430, 4592-4602 .
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.24.B20 | A359V | homolog of the human pathogenic A510V mutation of paraplegin (SPG7), does not affect the dynamic behavior of the protease but impairs the ATP-coupled domain compaction | Thermotoga maritima |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.24.B20 | Thermotoga maritima | Q9WZ49 | - |
- |
| 3.4.24.B20 | Thermotoga maritima DSM 3109 | Q9WZ49 | - |
- |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.24.B20 | physiological function | FtsH is a highly dynamic protease undergoing sequential transitions between five conformational states on the second timescale. Addition of ATP does not influence the number of states or change the timescale of domain motions but affects the state occupancy distribution leading to an interdomain compaction | Thermotoga maritima |
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Release 2023.1 (January 2023)
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