ID   MPPB_BOVIN              Reviewed;         490 AA.
AC   Q3SZ71;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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; BC103085; AAI03086.1; -; mRNA.
DR   RefSeq; NP_001029785.1; NM_001034613.1.
DR   AlphaFoldDB; Q3SZ71; -.
DR   SMR; Q3SZ71; -.
DR   STRING; 9913.ENSBTAP00000004922; -.
DR   MEROPS; M16.973; -.
DR   PaxDb; Q3SZ71; -.
DR   PRIDE; Q3SZ71; -.
DR   GeneID; 534546; -.
DR   KEGG; bta:534546; -.
DR   CTD; 9512; -.
DR   eggNOG; KOG0960; Eukaryota.
DR   InParanoid; Q3SZ71; -.
DR   OrthoDB; 638125at2759; -.
DR   Proteomes; UP000009136; 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..46
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:O75439"
FT   CHAIN           47..490
FT                   /note="Mitochondrial-processing peptidase subunit beta"
FT                   /id="PRO_0000045850"
FT   ACT_SITE        105
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   SITE            192
FT                   /note="Required for the specific determination of the
FT                   substrate cleavage site"
FT                   /evidence="ECO:0000250|UniProtKB:Q03346"
FT   SITE            196
FT                   /note="Required for the specific determination of the
FT                   substrate cleavage site"
FT                   /evidence="ECO:0000250|UniProtKB:Q03346"
SQ   SEQUENCE   490 AA;  54237 MW;  9C600D19B6712AFE CRC64;
     MAAAAVARAV LFSAARRRLC GFTERLLIGG AAGRSLYFGG NRLRSTQAAA QVVLNVPETR
     VTCLENGLRV ASEDSGLATC TVGLWIDAGS RYENEKNNGT AHFLEHMAFK GTKKRSQLDL
     ELEIENMGAH LNAYTSREQT VYYAKAFSKD LPRAVEILAD IIQNSTLGEA EIERERGVIL
     REMQEVETNL QEVVFDYLHA TAYQNTALGR TILGPTENIK SINRKDLVDY ITTHYKGPRI
     VLAAAGGVSH DELLELAKFH FGESLSTHKG EIPALPPCKF TGSEIRVRDD KMPLAHLAVA
     VEAVGWAHPD TICLMVANTL IGNWDRSFGG GMNLSSKLAQ LTCHGNLCHS FQSFNTSYTD
     TGLWGIYMVC EPATVADMLH VVQKEWMRLC TSVTESEVAR AKNLLKTNML LQLDGSTPIC
     EDIGRQMLCY NRRIPIPELE ARIDAVNAEI IREVCTKYIY DKSPAVAAVG PIEQLPDFNQ
     ICSNMRWLHD