MPPB_CAEEL
ID MPPB_CAEEL Reviewed; 458 AA.
AC Q23295;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Mitochondrial-processing peptidase subunit beta {ECO:0000303|PubMed:16788047};
DE EC=3.4.24.64 {ECO:0000269|PubMed:16788047};
DE AltName: Full=Beta-MPP {ECO:0000303|PubMed:16788047};
DE Flags: Precursor;
GN Name=mppb-1 {ECO:0000303|PubMed:16788047, ECO:0000312|WormBase:ZC410.2};
GN ORFNames=ZC410.2 {ECO:0000312|WormBase:ZC410.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, IDENTIFICATION IN
RP COMPLEX WITH MPPA-1, AND DISRUPTION PHENOTYPE.
RX PubMed=16788047; DOI=10.1093/jb/mvj114;
RA Nomura H., Athauda S.B., Wada H., Maruyama Y., Takahashi K., Inoue H.;
RT "Identification and reverse genetic analysis of mitochondrial processing
RT peptidase and the core protein of the cytochrome bc1 complex of
RT Caenorhabditis elegans, a model parasitic nematode.";
RL J. Biochem. 139:967-979(2006).
CC -!- FUNCTION: Catalytic subunit of the essential mitochondrial processing
CC protease (MPP), which cleaves the mitochondrial sequence off newly
CC imported precursors proteins (Probable). Preferentially, cleaves after
CC an arginine at position P2 (Probable). {ECO:0000305|PubMed:16788047}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal transit peptides from precursor proteins
CC imported into the mitochondrion, typically with Arg in position P2.;
CC EC=3.4.24.64; Evidence={ECO:0000269|PubMed:16788047};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P10507};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P10507};
CC -!- ACTIVITY REGULATION: Binding to mppa-1 is required for catalytic
CC activity (PubMed:16788047). Inhibited by metal chelator
CC ethylenediaminetetraacetic acid (EDTA) (PubMed:16788047).
CC {ECO:0000269|PubMed:16788047}.
CC -!- SUBUNIT: Heterodimer of mppa-1 (alpha) and mppb-1 (beta) subunits,
CC forming the mitochondrial processing protease (MPP) in which mppa-1 is
CC involved in substrate recognition and binding and mppb-1 is the
CC catalytic subunit. {ECO:0000305|PubMed:16788047}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:O75439}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes 54 percent
CC embryonic lethality (PubMed:16788047). Embryonic lethality is further
CC increased in simultaneous RNAi-mediated knockdown of mmpa-1 and mmpb-1
CC or ucr-1 and mppb-1 (PubMed:16788047). {ECO:0000269|PubMed:16788047}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000255|RuleBase:RU004447}.
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DR EMBL; BX284604; CAA92566.2; -; Genomic_DNA.
DR PIR; T27548; T27548.
DR RefSeq; NP_501576.2; NM_069175.6.
DR AlphaFoldDB; Q23295; -.
DR SMR; Q23295; -.
DR STRING; 6239.ZC410.2; -.
DR MEROPS; M16.980; -.
DR EPD; Q23295; -.
DR PaxDb; Q23295; -.
DR PeptideAtlas; Q23295; -.
DR EnsemblMetazoa; ZC410.2.1; ZC410.2.1; WBGene00013880.
DR GeneID; 177725; -.
DR KEGG; cel:CELE_ZC410.2; -.
DR UCSC; ZC410.2.1; c. elegans.
DR CTD; 177725; -.
DR WormBase; ZC410.2; CE35701; WBGene00013880; mppb-1.
DR eggNOG; KOG0960; Eukaryota.
DR GeneTree; ENSGT00940000156608; -.
DR HOGENOM; CLU_009902_4_2_1; -.
DR InParanoid; Q23295; -.
DR OMA; IDVVCDM; -.
DR OrthoDB; 638125at2759; -.
DR PhylomeDB; Q23295; -.
DR Reactome; R-CEL-8949664; Processing of SMDT1.
DR PRO; PR:Q23295; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00013880; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0017087; C:mitochondrial processing peptidase complex; IDA:WormBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IDA:WormBase.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..458
FT /note="Mitochondrial-processing peptidase subunit beta"
FT /id="PRO_0000448709"
FT ACT_SITE 76
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT SITE 163
FT /note="Required for the specific determination of the
FT substrate cleavage site"
FT /evidence="ECO:0000250|UniProtKB:Q03346"
FT SITE 167
FT /note="Required for the specific determination of the
FT substrate cleavage site"
FT /evidence="ECO:0000250|UniProtKB:Q03346"
SQ SEQUENCE 458 AA; 51156 MW; F13F26F47CEDE01C CRC64;
MYRRLASGLY QTSQRRIAQV QPKSVFVPET IVTTLPNGFR VATENTGGST ATIGVFIDAG
SRYENEKNNG TAHFLEHMAF KGTPRRTRMG LELEVENIGA HLNAYTSRES TTYYAKCFTE
KLDQSVDILS DILLNSSLAT KDIEAERGVI IREMEEVAQN FQEVVFDILH ADVFKGNPLS
YTILGPIELI QTINKNDLQG YINTHYRSGR MVLAAAGGVN HDAIVKMAEK YFGELKHGDS
STEFVPATYS PCEVRGDIPD LPMLYGAMVV EGVSWTHEDN LALMVANTLM GEYDRMRGFG
VNAPTRLAEK LSQDAGIEVF QSFNTCYKET GLVGTYFVAA PESIDNLIDS VLQQWVWLAN
NIDEAAVDRA KRSLHTNLLL MLDGSTPVCE DIGRQLLCYG RRIPTPELHA RIESITVQQL
RDVCRRVFLE GQVSAAVVGK TQYWPVNEEI HGRLIRMQ
