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Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
3.4.24.B17 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
3.4.24.B18 additional information inactivation of the enzyme impairs respiratory competence Saccharomyces cerevisiae
3.4.24.B18 additional information mutant enzyme variants are sufficient to suppress growth defects of the respective null-mutant cells eukaryota
3.4.24.B19 additional information inactivation of the enzyme causes pleiotropic defects, including impaired respiration and aberrant mitochondrial morphology Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.B18 prohibitin located at the periphery of mitochondria at protein import sites, has a regulatory role, deletion of prohibitin leads to accelerated degradation of non-assembled membrane proteins by the m-AAA protease, overexpression of prohibitin stabilizes non-native polypeptides against degradation Saccharomyces cerevisiae
3.4.24.B19 additional information no inhibition by prohibitin Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.B17 plasma membrane integral membrane protein Escherichia coli 5886
-
3.4.24.B18 mitochondrial inner membrane both subunit types span the membrane twice, integral, active at the matrix side of the inner membrane eukaryota 5743
-
3.4.24.B18 mitochondrial inner membrane both subunit types span the membrane twice, integral, active at the matrix side of the inner membrane Saccharomyces cerevisiae 5743
-
3.4.24.B18 mitochondrial inner membrane integral, active at the matrix side of the inner membrane Saccharomyces cerevisiae 5743
-
3.4.24.B18 mitochondrion
-
 eukaryota 5739
-
3.4.24.B18 mitochondrion
-
 Saccharomyces cerevisiae 5739
-
3.4.24.B19 mitochondrial inner membrane integral, catalytic site facing the intermembrane space Saccharomyces cerevisiae 5743
-
3.4.24.B19 mitochondrial inner membrane integral, catalytic site facing the intermembrane space Neurospora crassa 5743
-
3.4.24.B19 mitochondrial inner membrane only subunit type Yme1p spans the membrane once, integral, catalytic site facing the inter membrane space Saccharomyces cerevisiae 5743
-
3.4.24.B19 mitochondrion
-
 Saccharomyces cerevisiae 5739
-
3.4.24.B19 mitochondrion
-
 Neurospora crassa 5739
-
3.4.24.B20 chloroplast
-
 Arabidopsis thaliana 9507
-
3.4.24.B20 thylakoid membrane integral membrane protein Arabidopsis thaliana 42651
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.B17 Co2+ functional association Escherichia coli
3.4.24.B17 Fe2+ functional association Escherichia coli
3.4.24.B17 Mn2+ functional association Escherichia coli
3.4.24.B17 additional information conserved metal-binding motif HEXGH at the proteolytic centre Escherichia coli
3.4.24.B17 Ni2+ functional association Escherichia coli
3.4.24.B17 Zn2+ dependent on Escherichia coli
3.4.24.B18 additional information conserved metal-binding motif HEXGH at the proteolytic centre Saccharomyces cerevisiae
3.4.24.B18 Zn2+ dependent on eukaryota
3.4.24.B18 Zn2+ dependent on Saccharomyces cerevisiae
3.4.24.B19 additional information a consensus metal-binding site represents the proteolytic centre, metallopeptidase of the M41 family Neurospora crassa
3.4.24.B19 additional information conserved metal-binding motif HEXGH at the proteolytic centre Saccharomyces cerevisiae
3.4.24.B19 Zn2+ dependent on Saccharomyces cerevisiae
3.4.24.B20 Zn2+ dependent on Arabidopsis thaliana

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.B18 additional information
-
 the enzyme is part of a supercomplex in the inner mitochondrial membrane with a native MW of approximately 2000 kDa, assembling with the prohibitin complex Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.B17 additional information Escherichia coli dislocation of membrane proteins mediated by the enzyme, periplasmic segments can also be degraded by the enzyme ?
-
 ?
3.4.24.B17 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
-
 ?
3.4.24.B17 protein F0 subunit a + H2O Escherichia coli degradation of membrane protein, essentially required as a membrane-integrated quality control ?
-
 ?
3.4.24.B17 protein lambdaCII + H2O Escherichia coli degradation has regulatory function ?
-
 ?
3.4.24.B17 protein lambdaCIII + H2O Escherichia coli degradation has regulatory function ?
-
 ?
3.4.24.B17 protein lambdaXis + H2O Escherichia coli degradation has regulatory function ?
-
 ?
3.4.24.B17 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 ?
-
 ?
3.4.24.B17 protein SecY + H2O Escherichia coli degradation of membrane protein, essentially required as a membrane-integrated quality control ?
-
 ?
3.4.24.B17 protein sigma32 + H2O Escherichia coli degradation has regulatory function ?
-
 ?
3.4.24.B17 protein YccA + H2O Escherichia coli degradation of membrane protein, essentially required as a membrane-integrated quality control ?
-
 ?
3.4.24.B18 protein + H2O eukaryota enzyme is essential for cell viability, the enzyme affects the splicing of transcripts of mitochondrial genes encoding essential respiratory complexes and the ATP synthase, degradation of membrane proteins, essentially required as a membrane-integrated quality control, inactivation of AAA proteases cause severe defects in various organisms, including neurodegeneration in humans peptides
-
 ?
3.4.24.B18 protein + H2O Saccharomyces cerevisiae enzyme is essential for cell viability, the enzyme affects the splicing of transcripts of mitochondrial genes encoding essential respiratory complexes and the ATP synthase, degradation of membrane proteins, essentially required as a membrane-integrated quality control, inactivation of AAA proteases cause severe defects in various organisms, including neurodegeneration in humans peptides
-
 ?
3.4.24.B18 protein + H2O Saccharomyces cerevisiae important role in the removal of non-assembled polypeptides from the inner membrane, inactivation of the enzyme is lethal, loss of activity causes respiration-deficiency, affects the splicing of transcripts of mitochondrial genes encoding essential respiratory chain subunits and controls the post-translational asembly of respiratory complexes and the ATP synthase, required as a membrane-integrated quality control to facilitate protein folding and to ensure the selective removal of non-native polypeptides peptides
-
 ?
3.4.24.B18 protein Cob + H2O Saccharomyces cerevisiae degradation of membrane proteins, essentially required as a membrane-integrated quality control ?
-
 ?
3.4.24.B18 protein Cox1 + H2O Saccharomyces cerevisiae degradation of membrane proteins, essentially required as a membrane-integrated quality control ?
-
 ?
3.4.24.B18 protein Cox3 + H2O Saccharomyces cerevisiae degradation of membrane proteins, essentially required as a membrane-integrated quality control ?
-
 ?
3.4.24.B18 protein F0 subunit 6 + H2O Saccharomyces cerevisiae degradation of membrane proteins, essentially required as a membrane-integrated quality control ?
-
 ?
3.4.24.B18 protein F0 subunit 8 + H2O Saccharomyces cerevisiae degradation of membrane proteins, essentially required as a membrane-integrated quality control ?
-
 ?
3.4.24.B18 protein F0 subunit 9 + H2O Saccharomyces cerevisiae degradation of membrane proteins, essentially required as a membrane-integrated quality control ?
-
 ?
3.4.24.B19 protein + H2O Saccharomyces cerevisiae important role in the removal of non-assembled polypeptides from the inner membrane, inactivation of the enzyme is lethal, enzyme deficiency causes pleiotropic defects, including impaired respiration at high temperature and an aberrant mitochondrial morphology, required as a membrane-integrated quality control to facilitate protein folding and to ensure the selective removal of non-native polypeptides peptides
-
 ?
3.4.24.B19 protein + H2O Neurospora crassa quality control system to selectively remove non-assembled polypeptides and to prevent their possible deleterious accumulation in the membrane, enzyme is crucial for viability peptides
-
 ?
3.4.24.B19 protein + H2O Saccharomyces cerevisiae the substrate binding region is mapped to the N-terminus of the AAA domain and is probably close to the membrane surface, degradation of membrane proteins, essentially required as a membrane-integrated quality control peptides
-
 ?
3.4.24.B19 protein Cox2 + H2O Saccharomyces cerevisiae degradation of membrane protein, essentially required as a membrane-integrated quality control ?
-
 ?
3.4.24.B20 protein + H2O Arabidopsis thaliana degradation of membrane proteins, essentially required as a membrane-integrated quality control peptides
-
 ?
3.4.24.B20 Rieske FeS protein + H2O Arabidopsis thaliana degradation of membrane protein, essentially required as a membrane-integrated quality control ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.B17 Escherichia coli
-
 enzyme belongs to the AAA protease family
-
3.4.24.B18 eukaryota
-
 enzyme belongs to the AAA protease family
-
3.4.24.B18 Saccharomyces cerevisiae
-
-
-
3.4.24.B18 Saccharomyces cerevisiae
-
 enzyme belongs to the AAA protease family
-
3.4.24.B19 Neurospora crassa
-
-
-
3.4.24.B19 Saccharomyces cerevisiae
-
-
-
3.4.24.B19 Saccharomyces cerevisiae
-
 enzyme belongs to the AAA protease family
-
3.4.24.B20 Arabidopsis thaliana
-
 enzyme belongs to the AAA protease family
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.24.B17 proteolytic modification autocatalytically processed at the C-terminus, processing occurs preferentially after positively charged and hydrophobic amino acids Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.24.B17 proteolytic degradation of proteins degenerate cleavage specificity, degradation of hydrophobic membrane-spanning segments of misfolded mitochodrial membrane proteins Escherichia coli
a
3.4.24.B18 proteolytic degradation of proteins degradation of hydrophobic membrane-spanning segments of misfolded mitochondrial membrane proteins Saccharomyces cerevisiae
a
3.4.24.B18 proteolytic degradation of proteins m-AAA protease shows overlapping substrate specificity with the i-AAA protease, enzyme degrades domains of substrate proteins exposed to the opposite membrane surface, active site contains the conserved motif HEXXH, a helical region is located at the extreme C-terminus of the subunit Saccharomyces cerevisiae
a
3.4.24.B18 proteolytic degradation of proteins mechanism, model, degradation of hydrophobic membrane-spanning segments of misfolded mitochodrial membrane proteins eukaryota
a
3.4.24.B19 proteolytic degradation of proteins i-AAA protease shows overlapping substrate specificity with the m-AAA protease, enzyme degrades domains of substrate proteins exposed to the opposite membrane surface, active site contains the conserved motif HEXXH, a helical region is located at the extreme C-terminus of the subunit Saccharomyces cerevisiae
a
3.4.24.B19 proteolytic degradation of proteins mechanism, m-AAA protease shows overlapping substrate specificity with the i-AAA protease, intermolecular catalytic role of SRH domain at the C-terminus of the AAA domain Neurospora crassa
a
3.4.24.B19 proteolytic degradation of proteins mechanism, model, degradation of hydrophobic membrane-spanning segments of misfolded mitochodrial membrane proteins Saccharomyces cerevisiae
a
3.4.24.B20 degradative cleavage of proteins specific for chloroplastic membrane proteins Arabidopsis thaliana
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.B17 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 ?
-
 ?
3.4.24.B17 additional information dislocation of membrane proteins mediated by the enzyme, periplasmic segments can also be degraded by the enzyme Escherichia coli ?
-
 ?
3.4.24.B17 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
-
 ?
3.4.24.B17 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
-
 ?
3.4.24.B17 protein F0 subunit a + H2O
-
 Escherichia coli ?
-
 ?
3.4.24.B17 protein F0 subunit a + H2O degradation of membrane protein, essentially required as a membrane-integrated quality control Escherichia coli ?
-
 ?
3.4.24.B17 protein lambdaCII + H2O
-
 Escherichia coli ?
-
 ?
3.4.24.B17 protein lambdaCII + H2O degradation has regulatory function Escherichia coli ?
-
 ?
3.4.24.B17 protein lambdaCIII + H2O
-
 Escherichia coli ?
-
 ?
3.4.24.B17 protein lambdaCIII + H2O degradation has regulatory function Escherichia coli ?
-
 ?
3.4.24.B17 protein lambdaXis + H2O
-
 Escherichia coli ?
-
 ?
3.4.24.B17 protein lambdaXis + H2O degradation has regulatory function Escherichia coli ?
-
 ?
3.4.24.B17 protein LpxC + H2O
-
 Escherichia coli ?
-
 ?
3.4.24.B17 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 ?
-
 ?
3.4.24.B17 protein SecY + H2O
-
 Escherichia coli ?
-
 ?
3.4.24.B17 protein SecY + H2O degradation of membrane protein, essentially required as a membrane-integrated quality control Escherichia coli ?
-
 ?
3.4.24.B17 protein sigma32 + H2O
-
 Escherichia coli ?
-
 ?
3.4.24.B17 protein sigma32 + H2O degradation has regulatory function Escherichia coli ?
-
 ?
3.4.24.B17 protein YccA + H2O
-
 Escherichia coli ?
-
 ?
3.4.24.B17 protein YccA + H2O degradation of membrane protein, essentially required as a membrane-integrated quality control Escherichia coli ?
-
 ?
3.4.24.B18 additional information shedding model for availability of water molecules: enzyme shed solvent exposed loops or domains from membrane-embedded polypeptides, pulling model: binding of unfolded substrate protein segments together with ATP-dependent conformational changes in the enzyme can provide a pulling force on membrane proteins, with the enzyme being embedded in the bilayer eukaryota ?
-
 ?
3.4.24.B18 protein + H2O degradation of membrane proteins, essentially required as a membrane-integrated quality control Saccharomyces cerevisiae peptides product peptides in the matrix space are actively transported across the inner membrane by an ABC transporter Mdl1 ?
3.4.24.B18 protein + H2O enzyme probably forms a pore-like structure facilitating the transport of hydrophilic parts of the substrate protein during its extraction, limited substrate recognition Saccharomyces cerevisiae peptides product peptides in the matrix space are actively transported across the inner membrane by an ABC transporter Mdl1 ?
3.4.24.B18 protein + H2O unfoldase activity might be a common property of ATP-dependent proteases eukaryota peptides
-
 ?
3.4.24.B18 protein + H2O enzyme is essential for cell viability, the enzyme affects the splicing of transcripts of mitochondrial genes encoding essential respiratory complexes and the ATP synthase, degradation of membrane proteins, essentially required as a membrane-integrated quality control, inactivation of AAA proteases cause severe defects in various organisms, including neurodegeneration in humans eukaryota peptides
-
 ?
3.4.24.B18 protein + H2O enzyme is essential for cell viability, the enzyme affects the splicing of transcripts of mitochondrial genes encoding essential respiratory complexes and the ATP synthase, degradation of membrane proteins, essentially required as a membrane-integrated quality control, inactivation of AAA proteases cause severe defects in various organisms, including neurodegeneration in humans Saccharomyces cerevisiae peptides
-
 ?
3.4.24.B18 protein + H2O important role in the removal of non-assembled polypeptides from the inner membrane, inactivation of the enzyme is lethal, loss of activity causes respiration-deficiency, affects the splicing of transcripts of mitochondrial genes encoding essential respiratory chain subunits and controls the post-translational asembly of respiratory complexes and the ATP synthase, required as a membrane-integrated quality control to facilitate protein folding and to ensure the selective removal of non-native polypeptides Saccharomyces cerevisiae peptides
-
 ?
3.4.24.B18 protein Cob + H2O degradation of membrane proteins, essentially required as a membrane-integrated quality control Saccharomyces cerevisiae ?
-
 ?
3.4.24.B18 protein Cox1 + H2O degradation of membrane proteins, essentially required as a membrane-integrated quality control Saccharomyces cerevisiae ?
-
 ?
3.4.24.B18 protein Cox3 + H2O degradation of membrane proteins, essentially required as a membrane-integrated quality control Saccharomyces cerevisiae ?
-
 ?
3.4.24.B18 protein F0 subunit 6 + H2O degradation of membrane proteins, essentially required as a membrane-integrated quality control Saccharomyces cerevisiae ?
-
 ?
3.4.24.B18 protein F0 subunit 8 + H2O degradation of membrane proteins, essentially required as a membrane-integrated quality control Saccharomyces cerevisiae ?
-
 ?
3.4.24.B18 protein F0 subunit 9 + H2O degradation of membrane proteins, essentially required as a membrane-integrated quality control Saccharomyces cerevisiae ?
-
 ?
3.4.24.B19 additional information shedding model for availability of water molecules: enzyme shed solvent exposed loops or domains from membrane-embedded polypeptides, pulling model: binding of unfolded substrate protein segments together with ATP-dependent conformational changes in the enzyme can provide a plling force on membrane proteins, with the enzyme being embedded in the bilayer Saccharomyces cerevisiae ?
-
 ?
3.4.24.B19 protein + H2O activity depends on oligomerisation Neurospora crassa peptides
-
 ?
3.4.24.B19 protein + H2O ATP hydrolysis causes conformational changes, regulates the accessibility of the proteolytic sites and trigger unfolding of substrate polypeptides, substrate recognition and binding to the enzymes ATPase domain is crucial for proteolytic function against unfolded membrane protein substrates Saccharomyces cerevisiae peptides product peptides are released directly into the intermembrane space ?
3.4.24.B19 protein + H2O enzyme probably forms a pore-like structure facilitating the transport of hydrophilic parts of the substrate protein during its extraction, limited substrate recognition, 25 amino acids of the substrate exposed to the solvent are sufficient for the enzyme to bind via its AAA domain Saccharomyces cerevisiae peptides product peptides are released directly into the intermembrane space ?
3.4.24.B19 protein + H2O important role in the removal of non-assembled polypeptides from the inner membrane, inactivation of the enzyme is lethal, enzyme deficiency causes pleiotropic defects, including impaired respiration at high temperature and an aberrant mitochondrial morphology, required as a membrane-integrated quality control to facilitate protein folding and to ensure the selective removal of non-native polypeptides Saccharomyces cerevisiae peptides
-
 ?
3.4.24.B19 protein + H2O quality control system to selectively remove non-assembled polypeptides and to prevent their possible deleterious accumulation in the membrane, enzyme is crucial for viability Neurospora crassa peptides
-
 ?
3.4.24.B19 protein + H2O the substrate binding region is mapped to the N-terminus of the AAA domain and is probably close to the membrane surface, degradation of membrane proteins, essentially required as a membrane-integrated quality control Saccharomyces cerevisiae peptides
-
 ?
3.4.24.B19 protein Cox2 + H2O degradation of membrane protein, essentially required as a membrane-integrated quality control Saccharomyces cerevisiae ?
-
 ?
3.4.24.B20 protein + H2O degradation of membrane proteins, essentially required as a membrane-integrated quality control Arabidopsis thaliana peptides
-
 ?
3.4.24.B20 protein + H2O unfoldase activity might be a common property of ATP-dependent proteases Arabidopsis thaliana peptides
-
 ?
3.4.24.B20 Rieske FeS protein + H2O degradation of membrane protein, essentially required as a membrane-integrated quality control Arabidopsis thaliana ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.B17 More enzyme shows a ring-shaped structure, ATP binding is not necessary for enzyme assembly Escherichia coli
3.4.24.B18 ? x * 70000-80000, subunits Yta10 and Yta12 in equimolar amounts Saccharomyces cerevisiae
3.4.24.B18 More ATP binding is required for enzyme assembly eukaryota
3.4.24.B18 More formation of a supercomplex between the enzyme and a large complex containing the prohibitin homologues Phb1p and Phb2p, ATP binding is required for enzyme assembly Saccharomyces cerevisiae
3.4.24.B18 More the enzyme consists of an AAA domain, providing chaperone-like properties and binding to the unfolded, solvent-exposed domains of the substrate protein, a proteolytic doamin, and a Walker-type P-loop ATPase domain, both subunits span the membrane twice Saccharomyces cerevisiae
3.4.24.B18 oligomer homooligomer, Class-I and Class-II subunits eukaryota
3.4.24.B18 oligomer homooligomeric, subunits Yta10p and Yta12p, i.e. Afg3p and Rca1p Saccharomyces cerevisiae
3.4.24.B19 ? x * 70000-80000, subunit Yme1p Saccharomyces cerevisiae
3.4.24.B19 More activity depends on oligomerisation, the enzyme consists of an AAA domain, providing chaperone-like properties and binding to the unfolded, solvent-exposed domains of the substrate protein, a proteolytic doamin, and a Walker-type P-loop ATPase domain, subunits span the membrane once Neurospora crassa
3.4.24.B19 More ATP binding is not necessary for enzyme assembly Saccharomyces cerevisiae
3.4.24.B19 More the enzyme consists of a AAA domain, providing chaperone-like properties and binding at its N-terminus to the unfolded, solvent-exposed domains of the substrate protein, a proteolytic doamin, and a Walker-type P-loop ATPase domain, single subunit type Yme1p contains 1 transmembrane segment Saccharomyces cerevisiae
3.4.24.B19 oligomer homooligomeric, 1 subunit type Yme1p Saccharomyces cerevisiae
3.4.24.B19 oligomer x * 70000-80000, homooligomeric Neurospora crassa
3.4.24.B20 More ATP binding is not necessary for enzyme assembly, enzyme probably forms high molecular weight complexes Arabidopsis thaliana

Synonyms

EC Number Synonyms Comment Organism
3.4.24.B17 FtsH
-
 Escherichia coli
3.4.24.B17 M41.001 Merops-ID Escherichia coli
3.4.24.B18 M41.003 Merops-ID eukaryota
3.4.24.B18 M41.003 Merops-ID Saccharomyces cerevisiae
3.4.24.B19 M41.004 Merops-ID Saccharomyces cerevisiae
3.4.24.B19 M41.004 Merops-ID Neurospora crassa
3.4.24.B19 Yme1p
-
 Saccharomyces cerevisiae
3.4.24.B20 FtsH
-
 Arabidopsis thaliana
3.4.24.B20 M41.005 Merops-ID Arabidopsis thaliana

Cofactor

EC Number Cofactor Comment Organism Structure
3.4.24.B17 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
3.4.24.B18 ATP ATP binding is required for enzyme assembly, enzyme contains conserved Walker-type ATPase domain of approximately 230 amino acids, dependent on eukaryota
3.4.24.B18 ATP ATP binding is required for enzyme assembly, enzyme contains conserved Walker-type ATPase domain of approximately 230 amino acids, dependent on Saccharomyces cerevisiae
3.4.24.B18 ATP dependent on, enzyme contains an ATPase domain with a Walker-type P-loop typical for the AAA protease family, hydrolysis induces conformational changes of the AAA domain driving substrate unfolding and dislocation from the membrane Saccharomyces cerevisiae
3.4.24.B19 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 Saccharomyces cerevisiae
3.4.24.B19 ATP dependent on, enzyme contains an ATPase domain with a Walker-type P-loop typical for the AAA protease family Neurospora crassa
3.4.24.B19 ATP dependent on, enzyme contains an ATPase domain with a Walker-type P-loop typical for the AAA protease family, hydrolysis induces conformational changes of the AAA domain driving substrate unfolding and dislocation from the membrane Saccharomyces cerevisiae
3.4.24.B20 ATP ATP binding is not necessary for enzyme assembly, enzyme contains conserved Walker-type ATPase domain of approximately 230 amino acids, dependent on Arabidopsis thaliana