Literature summary extracted from
Akiyama, Y.
Self-processing of FtsH and its implication for the cleavage specificity of this protease (1999), Biochemistry, 38, 11693-11699.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.4.24.B17 |
expression of wild-type tagged with His6- and Myc-tag in Escherichia coli |
Escherichia coli |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.4.24.B17 |
additional information |
mutational amino acid exchange of the self-processing site M640-S641 reveal the preference for positively charged and hydrophobic amino acid residues at this site for proteolytic cleavage |
Escherichia coli |
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
3.4.24.B17 |
membrane |
integral, with the active site in the cytoplasm |
Escherichia coli |
16020 |
- |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
3.4.24.B17 |
protein + H2O |
Escherichia coli |
- |
peptides |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.24.B17 |
Escherichia coli |
- |
- |
- |
Posttranslational Modification
EC Number |
Posttranslational Modification |
Comment |
Organism |
---|
3.4.24.B17 |
proteolytic modification |
ATP-dependent C-terminally self-processing by cleavage of Met640-Ser641 bond removing a heptapeptide from the C-terminus, preference for positively charged and hydrophobic amino acid residues, both processed and unprocessed enzyme forms are active, levels depending on the growth phase |
Escherichia coli |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
3.4.24.B17 |
proteolytic degradation of proteins |
preference for positively charged and hydrophobic amino acid residues, large cytoplasmic domain contains ATPase and protease activities |
Escherichia coli |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.4.24.B17 |
protein + H2O |
- |
Escherichia coli |
peptides |
- |
? |
|
3.4.24.B17 |
protein + H2O |
preference for positively charged and hydrophobic amino acid residues, degradation of uncomplexed integral membrane proteins and short-life cytoplasmic proteins |
Escherichia coli |
peptides |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.4.24.B17 |
More |
enzyme is composed of an N-terminal membrane-spanning region and a large cytoplasmic domain which contains ATPase and protease activities |
Escherichia coli |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.4.24.B17 |
FtsH |
- |
Escherichia coli |
3.4.24.B17 |
M41.001 |
Merops-ID |
Escherichia coli |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
3.4.24.B17 |
ATP |
dependent on, large cytoplasmic domain contains ATPase and protease activities |
Escherichia coli |
|
3.4.24.B17 |
additional information |
no activity with adenosine5'-(beta,gamma-imino)triphosphate |
Escherichia coli |
|