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Literature summary for 3.4.24.B17 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
Search for more literature for 3.4.24.B17

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type tagged with His6- and Myc-tag in Escherichia coli Escherichia coli

Protein Variants

Protein Variants Comment Organism
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

Localization Comment Organism GeneOntology No. Textmining
membrane integral, with the active site in the cytoplasm Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protein + H2O Escherichia coli
-
 peptides
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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

Reaction Comment Organism Reaction ID
proteolytic degradation of proteins preference for positively charged and hydrophobic amino acid residues, large cytoplasmic domain contains ATPase and protease activities Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protein + H2O
-
 Escherichia coli peptides
-
 ?
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

Subunits Comment Organism
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

Synonyms Comment Organism
FtsH
-
 Escherichia coli
M41.001 Merops-ID Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP dependent on, large cytoplasmic domain contains ATPase and protease activities Escherichia coli
additional information no activity with adenosine5'-(beta,gamma-imino)triphosphate Escherichia coli