Detail Information for IndEnz0002006462
IED ID IndEnz0002006462
Enzyme Type ID protease006462
Protein Name Mitochondrial-processing peptidase subunit beta
EC 3.4.24.64
Beta-MPP
Gene Name mppb-1 ZC410.2
Organism Caenorhabditis elegans
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans
Enzyme Sequence MYRRLASGLYQTSQRRIAQVQPKSVFVPETIVTTLPNGFRVATENTGGSTATIGVFIDAGSRYENEKNNGTAHFLEHMAFKGTPRRTRMGLELEVENIGAHLNAYTSRESTTYYAKCFTEKLDQSVDILSDILLNSSLATKDIEAERGVIIREMEEVAQNFQEVVFDILHADVFKGNPLSYTILGPIELIQTINKNDLQGYINTHYRSGRMVLAAAGGVNHDAIVKMAEKYFGELKHGDSSTEFVPATYSPCEVRGDIPDLPMLYGAMVVEGVSWTHEDNLALMVANTLMGEYDRMRGFGVNAPTRLAEKLSQDAGIEVFQSFNTCYKETGLVGTYFVAAPESIDNLIDSVLQQWVWLANNIDEAAVDRAKRSLHTNLLLMLDGSTPVCEDIGRQLLCYGRRIPTPELHARIESITVQQLRDVCRRVFLEGQVSAAVVGKTQYWPVNEEIHGRLIRMQ
Enzyme Length 458
Uniprot Accession Number Q23295
Absorption
Active Site ACT_SITE 76; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096
Activity Regulation ACTIVITY REGULATION: Binding to mppa-1 is required for catalytic activity (PubMed:16788047). Inhibited by metal chelator ethylenediaminetetraacetic acid (EDTA) (PubMed:16788047). {ECO:0000269|PubMed:16788047}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of N-terminal transit peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.; EC=3.4.24.64; Evidence={ECO:0000269|PubMed:16788047};
DNA Binding
EC Number 3.4.24.64
Enzyme Function FUNCTION: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (Probable). Preferentially, cleaves after an arginine at position P2 (Probable). {ECO:0000305|PubMed:16788047}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Metal binding (3); Site (2); Transit peptide (1)
Keywords Hydrolase;Metal-binding;Metalloprotease;Mitochondrion;Protease;Reference proteome;Transit peptide;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:O75439}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10778742; 15791247; 21177967; 22267497; 22560298; 23800452; 24884423; 25487147; 6593563;
Motif
Gene Encoded By
Mass 51,156
Kinetics
Metal Binding METAL 73; /note=Zinc; via tele nitrogen; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096; METAL 77; /note=Zinc; via tele nitrogen; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096; METAL 153; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU10096
Rhea ID
Cross Reference Brenda