ID   A0A668AG27_9TELE        Unreviewed;       456 AA.
AC   A0A668AG27;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Mitochondrial-processing peptidase subunit beta {ECO:0000256|ARBA:ARBA00020510};
DE            EC=3.4.24.64 {ECO:0000256|ARBA:ARBA00012299};
DE   AltName: Full=Beta-MPP {ECO:0000256|ARBA:ARBA00031018};
GN   Name=pmpcb {ECO:0000313|Ensembl:ENSMMDP00005052312.1};
OS   Myripristis murdjan (pinecone soldierfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Holocentriformes; Holocentridae; Myripristis.
OX   NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005052312.1, ECO:0000313|Proteomes:UP000472263};
RN   [1] {ECO:0000313|Ensembl:ENSMMDP00005052312.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001098};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:0000256|ARBA:ARBA00011587}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|RuleBase:RU004447}.
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DR   AlphaFoldDB; A0A668AG27; -.
DR   Ensembl; ENSMMDT00005053336.1; ENSMMDP00005052312.1; ENSMMDG00005023055.1.
DR   GeneTree; ENSGT00940000156608; -.
DR   Proteomes; UP000472263; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
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   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF103; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT BETA; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000472263}.
FT   DOMAIN          35..181
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          188..371
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   456 AA;  50814 MW;  DA3759058C6A4E01 CRC64;
     IINTALHRHL ATRAAGQVIL NVPETKVTAL ENGLRVASED SGLSTCTVGL WIDAGSRYEN
     ERNNGTAHFL EHMAFKGTRK RSQLDLELEI ENMGAHLNAY TSREQTVYYA KAFSKDLPRA
     VEILADIIQN STLGEAEIER ERGVILREMQ EVETNLQEVV FDYLHATAYQ ATALGRTILG
     PTENIKTINR ADLVEYITTH YKGPRIVLAA AGGVSHDELI DLAKYHFGKL PTRYKGEAPA
     LPLCSFTGSE IRVRDDKMPL AHIAIAVEAV GWSHPDTIPL MVANTLIGNW DRSFGGGVNL
     SSKLAQMACQ GNLCHSFQSF NTCYTDTGLW GLYMVCEPGT VRDMMHFTQM EWMSLCTSVT
     ESEVARAKNL LKTNMLLHLD GSTPICEDIG RQMLCYSRRI PLHELEARID AIDATTIKDV
     CTKYIYDKAP AIAAVGPIEQ LPDYNRIRSG MFWMRT
//