EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.4.24.B17 | X-ray structure determination and analysis at about 1.5 A, molecular modeling | Escherichia coli |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.4.24.B17 | membrane | integral | Escherichia coli | 16020 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.24.B17 | protein + H2O | Escherichia coli | degrades misassembled membrane protein complexes and plays a vital role in membrane quality control, degrades cytoplasmic regulatory proteins | peptides | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.24.B17 | Escherichia coli | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.4.24.B17 | proteolytic degradation of proteins | essential for activity are residues Asn301, Asp307, Arg312, and Arg315, mechanism, ligand binding site at residues 144-398 | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.24.B17 | lambda protein CII + H2O | cytoplasmic regulatory protein | Escherichia coli | ? | - |
? | |
3.4.24.B17 | protein + H2O | - |
Escherichia coli | peptides | - |
? | |
3.4.24.B17 | protein + H2O | degrades misassembled membrane protein complexes and plays a vital role in membrane quality control, degrades cytoplasmic regulatory proteins | Escherichia coli | peptides | - |
? | |
3.4.24.B17 | protein LpxC + H2O | cytoplasmic regulatory protein | Escherichia coli | ? | - |
? | |
3.4.24.B17 | protein sigma32 + H2O | cytoplasmic regulatory protein | Escherichia coli | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.24.B17 | hexamer | modeling from crystal structure | Escherichia coli |
3.4.24.B17 | More | molecular structure model of the AAA domain, intersubunit interactions, overview | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.24.B17 | FtsH | - |
Escherichia coli |
3.4.24.B17 | M41.001 | Merops-ID | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
3.4.24.B17 | ATP | dependent on, the Walker-type ATPase modul is an alpha/beta-nucleotide binding domain connected to a four-helix bundle | Escherichia coli |