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 |
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 |
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 | - |
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 |
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 |
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 | ? | - |
? |
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 | - |
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 |
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 | |
3.4.24.B18 | proteolytic degradation of proteins | degradation of hydrophobic membrane-spanning segments of misfolded mitochondrial membrane proteins | Saccharomyces cerevisiae | |
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 | |
3.4.24.B18 | proteolytic degradation of proteins | mechanism, model, degradation of hydrophobic membrane-spanning segments of misfolded mitochodrial membrane proteins | eukaryota | |
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 | |
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 | |
3.4.24.B19 | proteolytic degradation of proteins | mechanism, model, degradation of hydrophobic membrane-spanning segments of misfolded mitochodrial membrane proteins | Saccharomyces cerevisiae | |
3.4.24.B20 | degradative cleavage of proteins | specific for chloroplastic membrane proteins | Arabidopsis thaliana |
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 | ? | - |
? |
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 |
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 |
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 |