IED ID | IndEnz0002004689 |
Enzyme Type ID | protease004689 |
Protein Name |
Mitochondrial inner membrane protease atp23 EC 3.4.24.- |
Gene Name | atp23 BC1G_15820 |
Organism | Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Leotiomycetes Helotiales Sclerotiniaceae Botrytis Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea) Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
Enzyme Sequence | MSSSEGNKPPLVPDSTKESEPQFDPTARTRNWFSILLGTMPPSHQILYREDQYARHEKRDCDRCEEWRDYNLKYSPIVIFMQKNIRDLNGKLDADNIRCRRCPTRITEDGKTVRQGGGFSPEHGIQLCANEMRDSKHVEDTLAHEMVHAWDHLRWKVDWGDLRHAACSEIRAASLSGECRWAREFWTRNNYRVTQQHQDCVRRRAVKSVLARPWCKDDVQAVRVVNEVWDSCYSDTRPFDEIYK |
Enzyme Length | 244 |
Uniprot Accession Number | A6SSS5 |
Absorption | |
Active Site | ACT_SITE 145; /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 N-terminal residues of mitochondrial ATPase CF(0) subunit 6 at the intermembrane space side. Also involved in the correct assembly of the membrane-embedded ATPase CF(0) particle, probably mediating association of subunit 6 with the subunit 9 ring (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Erroneous gene model prediction (1); Metal binding (2); Region (1) |
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 | 28,756 |
Kinetics | |
Metal Binding | METAL 144; /note=Divalent metal cation; catalytic; /evidence=ECO:0000250; METAL 148; /note=Divalent metal cation; catalytic; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |