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Literature summary for 3.4.24.B20 extracted from

  • Narberhaus, F.; Obrist, M.; Fuehrer, F.; Langklotz, S.
    Degradation of cytoplasmic substrates by FtsH, a membrane-anchored protease with many talents (2009), Res. Microbiol., 160, 652-659.
    View publication on PubMed
Search for more literature for 3.4.24.B20

Activating Compound

Activating Compound Comment Organism Structure
ATP dependent on, the C-terminus comprise the cytoplasmic ATPase and protease domain. The ATPase domain contains the Walker A/B motifs and the second region of homology responsible for the binding and hydrolysis of ATP Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the hexameric FtsH protease is anchored to the inner membrane by two transmembrane helices per monomer such that both termini protrude into the cytoplasm Escherichia coli 16020
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Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ dependent on. FtsH is a metalloprotease and the protease domain contains the zinc-coordinating HEXXH motif Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
71000
-
 6 * 71000, FtsH forms a barrel-shaped oligomer Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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 ftsH gene
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H+-ATPase F0alpha + H2O membrane substrate of FtsH Escherichia coli ?
-
 ?
LpxC + H2O cytosolic substrate of FtsH Escherichia coli ?
-
 ?
additional information complex substrate recognition mechanisms, detailed overview. The ATPase domain forms the entrance to the central pore of FtsH with a diameter of about 15 A, a conserved Phe at position 228 of the pore is crucial for substrate binding. Substrates are pulled through the narrow gate and into the following protease domain using the energy of ATP hydrolysis for unfolding and translocation of the proteins. FtsH has only weak unfolding activity and is not able to degrade tightly folded model substrate proteins like GFP or DHFR Escherichia coli ?
-
 ?
subunit SecY of the SecAEG translocase + H2O membrane substrate of FtsH Escherichia coli ?
-
 ?
YccA + H2O membrane substrate of FtsH Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
hexamer 6 * 71000, FtsH forms a barrel-shaped oligomer Escherichia coli
More the C-terminus comprise the cytoplasmic ATPase and protease domain. The ATPase domain contains the Walker A/B motifs and the second region of homology responsible for the binding and hydrolysis of ATP Escherichia coli

Synonyms

Synonyms Comment Organism
FtsH
-
 Escherichia coli
More the enzyme belongs to the AAA protease family Escherichia coli

General Information

General Information Comment Organism
metabolism FtsH cellular functions and regulation involving several factors, overview Escherichia coli
physiological function FtsH is the only known membrane-anchored AAA protease in bacteria that fulfills a variety of regulatory functions. FtsH-mediated regulation of LpxC levels by proteolysis crucial for cell viability. FtsH is involved in the quality control of misfolded or incorrectly inserted membrane proteins and acts either as a chaperone to help them refold or degrades them. Another important function of FtsH in Escherichia coli is control of heat shock gene expression, overview Escherichia coli