Detail Information for IndEnz0002018625
IED ID IndEnz0002018625
Enzyme Type ID protease018625
Protein Name Mitochondrial inner membrane protease ATP23
EC 3.4.24.-
Gene Name ATP23 SCY_4805
Organism Saccharomyces cerevisiae (strain YJM789) (Baker's yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain YJM789) (Baker's yeast)
Enzyme Sequence MNSSGDNAGFEWWRRTMQYKTGIGLTPEEKTRYEDDSKARELKKECLKCYEYRDWMLKYSPTVRFMVQAITKLNKGSDSKFDDSKIICDYCPDWKGGGFHPELGILLCQNRLRDKWHLEDTLSHELIHYFDDLKWQIDWLNLKHHACSEIRASSLSGECRFWEEFKRRGFRTGFHVARGHQDCVRRRAIISVSGNPNCQSKEHAAKIVDEVWDSCFADTRPFDEIYR
Enzyme Length 227
Uniprot Accession Number A6ZS94
Absorption
Active Site ACT_SITE 125; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Has a dual role in the assembly of mitochondrial ATPase. Acts as a protease that removes the N-terminal 10 residues of mitochondrial ATPase CF(0) subunit 6 (ATP6) at the intermembrane space side. Also involved in the correct assembly of the membrane-embedded ATPase CF(0) particle, probably mediating association of ATP6 with the subunit 9 ring (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Metal binding (2)
Keywords Hydrolase;Membrane;Metal-binding;Metalloprotease;Mitochondrion;Mitochondrion inner membrane;Protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. Note=Associates loosely with the inner membrane. {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 26,890
Kinetics
Metal Binding METAL 124; /note=Divalent metal cation; catalytic; /evidence=ECO:0000250; METAL 128; /note=Divalent metal cation; catalytic; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda