ID   MPPB_PONAB              Reviewed;         489 AA.
AC   Q5REK3;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Mitochondrial-processing peptidase subunit beta;
DE            EC=3.4.24.64 {ECO:0000250|UniProtKB:Q03346};
DE   AltName: Full=Beta-MPP;
DE   Flags: Precursor;
GN   Name=PMPCB;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalytic subunit of the essential mitochondrial processing
CC       protease (MPP), which cleaves the mitochondrial sequence off newly
CC       imported precursors proteins (By similarity). Preferentially, cleaves
CC       after an arginine at position P2 (By similarity). Required for PINK1
CC       turnover by coupling PINK1 mitochondrial import and cleavage, which
CC       results in subsequent PINK1 proteolysis (By similarity).
CC       {ECO:0000250|UniProtKB:O75439, ECO:0000250|UniProtKB:Q03346}.
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:0000250|UniProtKB:Q03346};
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 PMPCA is required for catalytic
CC       activity. {ECO:0000250|UniProtKB:P10507}.
CC   -!- SUBUNIT: Heterodimer of PMPCA (alpha) and PMPCB (beta) subunits,
CC       forming the mitochondrial processing protease (MPP) in which PMPCA is
CC       involved in substrate recognition and binding and PMPCB is the
CC       catalytic subunit. {ECO:0000250|UniProtKB:P10507}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:O75439}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR   EMBL; CR857522; CAH89804.1; -; mRNA.
DR   RefSeq; NP_001127198.1; NM_001133726.1.
DR   AlphaFoldDB; Q5REK3; -.
DR   SMR; Q5REK3; -.
DR   STRING; 9601.ENSPPYP00000020042; -.
DR   MEROPS; M16.973; -.
DR   GeneID; 100174253; -.
DR   KEGG; pon:100174253; -.
DR   CTD; 9512; -.
DR   eggNOG; KOG0960; Eukaryota.
DR   InParanoid; Q5REK3; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0017087; C:mitochondrial processing peptidase complex; IEA:InterPro.
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; IEA:InterPro.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR037718; MPP_beat.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF103; PTHR11851:SF103; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW   Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..45
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:O75439"
FT   CHAIN           46..489
FT                   /note="Mitochondrial-processing peptidase subunit beta"
FT                   /id="PRO_0000045851"
FT   ACT_SITE        104
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   SITE            191
FT                   /note="Required for the specific determination of the
FT                   substrate cleavage site"
FT                   /evidence="ECO:0000250|UniProtKB:Q03346"
FT   SITE            195
FT                   /note="Required for the specific determination of the
FT                   substrate cleavage site"
FT                   /evidence="ECO:0000250|UniProtKB:Q03346"
SQ   SEQUENCE   489 AA;  54334 MW;  062FB483C362D063 CRC64;
     MAAAAARVVL LPAARRRLWG FSESLLIRGA AGRSSYFGEN RLRSTQAATQ VVLNVPETRV
     TCLESGLRVA SEDSGLSTCT VGLWIDAGSR YENEKNNGTA HFLEHMAFKG TKKRSQLDLE
     LEIENMGAHL NAYTSREQTV YYAKAFSKDL PRAVEILADI IQNSTLGEAE IERERGVILR
     EMQEVETNLQ EVVFDYLHAT AYQNTALGRT ILGPTENIKS ISRKDLVDYI TTHYKGPRIV
     LAAAGGVSHD ELLDLAKFHF GDSLCTHKGE IPALPPCKFT GSEIRVRDDK MPLAHLAIAV
     EAVGWAHPDT ICLMVANTLI GNWDRSFGGG MNLSSKLAQL TCHGNLCHSF QSFNTSYTDT
     GLWGLYMVCE PSTVADMLHV VQKEWMRLCT SVTESEVARA RNLLKTNMLL QLDGSTPICE
     DIGRQMLCYN RRIPIPELEA RIDAVNAETI REVCTKYIYN RSPAIAAVGP IEQLPDFKQI
     CSNMCWLRD