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Literature summary extracted from

  • Ito, K.; Akiyama, Y.
    Cellular functions, mechanism of action, and regulation of FtsH protease (2005), Annu. Rev. Microbiol., 59, 211-231.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.B17 cytoplasmic membrane FtsH has N-terminally located transmembrane segments and a main cytosolic region consisting of AAA-ATPase and Zn2+-metalloprotease domains Escherichia coli
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-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.B17 Zn2+ degradation of sigma32 is dependent on Zn2+ Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.B17 LpxC + H2O Escherichia coli ATP-dependent. Essentiality of FtsH lies in its function to keep the proper LPS/phospholipid ratio by degrading LpxC ?
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 ?
3.4.24.B17 protein + H2O Escherichia coli FtsH degrades a set of short-lived proteins, enabling cellular regulation at the level of protein stability. FtsH also degrades some misassembles membrane proteins, contributing to their quality maintenance. One biological role of FtsH might be to affect the development and life cycle of infecting or episomal genetic systems, by degrading their key regulatory molecules. The enzyme has a special ability to dislocate membrane protein substrates out of the membrane for which its own membrane-embedded nature is essential peptides
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 ?

Organism

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

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.24.B17 proteolytic modification FtsH undergoes self-cleavage between M640 and S641, removing seven C-terminal residues. Functional significance of this self-cleavage reaction is obscure, as both the full-length and the processed forms of FtsH are active as protease Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.B17 LpxC + H2O ATP-dependent. Essentiality of FtsH lies in its function to keep the proper LPS/phospholipid ratio by degrading LpxC Escherichia coli ?
-
 ?
3.4.24.B17 LpxC + H2O ATP-dependent Escherichia coli ?
-
 ?
3.4.24.B17 protein + H2O FtsH degrades a set of short-lived proteins, enabling cellular regulation at the level of protein stability. FtsH also degrades some misassembles membrane proteins, contributing to their quality maintenance. One biological role of FtsH might be to affect the development and life cycle of infecting or episomal genetic systems, by degrading their key regulatory molecules. The enzyme has a special ability to dislocate membrane protein substrates out of the membrane for which its own membrane-embedded nature is essential Escherichia coli peptides
-
 ?
3.4.24.B17 sigma32 + H2O ATP- and Zn2+-dependent degradation Escherichia coli ?
-
 ?
3.4.24.B17 SoxS + H2O
-
 Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.B17 hexamer
-
 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 degradation of sigma32 and LpxC is dependent on Escherichia coli