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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.
    View publication on PubMed

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