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Literature summary extracted from

  • Licht, S.; Lee, I.
    Resolving individual steps in the operation of ATP-dependent proteolytic molecular machines: from conformational changes to substrate translocation and processivity (2008), Biochemistry, 47, 3595-3605.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.B17 membrane
-
Escherichia coli 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.B17 Zn2+ the proteolytic activity of FtsH is stimulated by Zn2+ Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.B17 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.B17 F0a subunit of the ATP synthetase + H2O
-
Escherichia coli ?
-
?
3.4.24.B17 N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
-
Escherichia coli ?
-
?
3.4.24.B17 protein sigma32 + H2O
-
Escherichia coli ?
-
?

Subunits

EC Number Subunits Comment Organism
3.4.24.B17 homohexamer
-
Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.4.24.B17 FtsH
-
Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
3.4.24.B17 ATP
-
Escherichia coli