Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.24.B17 extracted from

  • Langer, T.; Kaser, M.; Klanner, C.; Leonhard, K.
    AAA proteases of mitochondria: quality control of membrane proteins and regulatory functions during mitochondrial biogenesis (2001), Biochem. Soc. Trans., 29, 431-436.
    View publication on PubMed
Search for more literature for 3.4.24.B17

Protein Variants

Protein Variants Comment Organism
additional information mutations cause an abnormal orientation of some model proteins in the plasma membrane, the effect can be supressed by overexpression of molecular-chaperone proteins, deletion of FtsH is lethal Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
plasma membrane integral membrane protein Escherichia coli 5886
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ functional association Escherichia coli
Fe2+ functional association Escherichia coli
Mn2+ functional association Escherichia coli
additional information conserved metal-binding motif HEXGH at the proteolytic centre Escherichia coli
Ni2+ functional association Escherichia coli
Zn2+ dependent on Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli dislocation of membrane proteins mediated by the enzyme, periplasmic segments can also be degraded by the enzyme ?
-
 ?
protein + H2O Escherichia coli enzyme affects several processes including cell division, the synthesis of phospholipids and lipopolysaccharides, the anchoring of integral membrane proteins, mRNA stability, and colchicin tolerance, degradation of membrane proteins, essentially required as a membrane-integrated quality control peptides
-
 ?
protein F0 subunit a + H2O Escherichia coli degradation of membrane protein, essentially required as a membrane-integrated quality control ?
-
 ?
protein lambdaCII + H2O Escherichia coli degradation has regulatory function ?
-
 ?
protein lambdaCIII + H2O Escherichia coli degradation has regulatory function ?
-
 ?
protein lambdaXis + H2O Escherichia coli degradation has regulatory function ?
-
 ?
protein LpxC + H2O Escherichia coli essential for cell viability, enzyme controls the steady-state level of the LpxC protein, which has a key regulatory role in the biosynthesis of lipopolysaccharides ?
-
 ?
protein SecY + H2O Escherichia coli degradation of membrane protein, essentially required as a membrane-integrated quality control ?
-
 ?
protein sigma32 + H2O Escherichia coli degradation has regulatory function ?
-
 ?
protein YccA + H2O Escherichia coli degradation of membrane protein, essentially required as a membrane-integrated quality control ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 enzyme belongs to the AAA protease family
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification autocatalytically processed at the C-terminus, processing occurs preferentially after positively charged and hydrophobic amino acids Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
proteolytic degradation of proteins degenerate cleavage specificity, degradation of hydrophobic membrane-spanning segments of misfolded mitochodrial membrane proteins Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme acts in cooperation with the homologous proteins HflK and HflC, the 3 proteins assemble at the periplasmic site of the plasma membrane, resulting in prohibitin-like modulation of the enzymes substrate specificity and activity Escherichia coli ?
-
 ?
additional information dislocation of membrane proteins mediated by the enzyme, periplasmic segments can also be degraded by the enzyme Escherichia coli ?
-
 ?
protein + H2O ATP hydrolysis cause conformational changes, regulate the accessibility of the proteolytic sites and trigger unfolding of substrate polypeptides, C-terminally located second region of homology, i.e. SRH region, is conserved throughout the AAA proteases and plays an intermolecular catalytic role Escherichia coli peptides
-
 ?
protein + H2O enzyme affects several processes including cell division, the synthesis of phospholipids and lipopolysaccharides, the anchoring of integral membrane proteins, mRNA stability, and colchicin tolerance, degradation of membrane proteins, essentially required as a membrane-integrated quality control Escherichia coli peptides
-
 ?
protein F0 subunit a + H2O
-
 Escherichia coli ?
-
 ?
protein F0 subunit a + H2O degradation of membrane protein, essentially required as a membrane-integrated quality control Escherichia coli ?
-
 ?
protein lambdaCII + H2O
-
 Escherichia coli ?
-
 ?
protein lambdaCII + H2O degradation has regulatory function Escherichia coli ?
-
 ?
protein lambdaCIII + H2O
-
 Escherichia coli ?
-
 ?
protein lambdaCIII + H2O degradation has regulatory function Escherichia coli ?
-
 ?
protein lambdaXis + H2O
-
 Escherichia coli ?
-
 ?
protein lambdaXis + H2O degradation has regulatory function Escherichia coli ?
-
 ?
protein LpxC + H2O
-
 Escherichia coli ?
-
 ?
protein LpxC + H2O essential for cell viability, enzyme controls the steady-state level of the LpxC protein, which has a key regulatory role in the biosynthesis of lipopolysaccharides Escherichia coli ?
-
 ?
protein SecY + H2O
-
 Escherichia coli ?
-
 ?
protein SecY + H2O degradation of membrane protein, essentially required as a membrane-integrated quality control Escherichia coli ?
-
 ?
protein sigma32 + H2O
-
 Escherichia coli ?
-
 ?
protein sigma32 + H2O degradation has regulatory function Escherichia coli ?
-
 ?
protein YccA + H2O
-
 Escherichia coli ?
-
 ?
protein YccA + H2O degradation of membrane protein, essentially required as a membrane-integrated quality control Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
More enzyme shows a ring-shaped structure, ATP binding is not necessary for enzyme assembly Escherichia coli

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
ATP ATP binding is not necessary for enzyme assembly, enzyme contains conserved Walker-type ATPase domain of approximately 230 amino acids, dependent on, hydrolysis induces conformational changes Escherichia coli