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