ID   A0A665TMD4_ECHNA        Unreviewed;       430 AA.
AC   A0A665TMD4;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 16.
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:ENSENLP00000007317.1};
OS   Echeneis naucrates (Live sharksucker).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Echeneidae; Echeneis.
OX   NCBI_TaxID=173247 {ECO:0000313|Ensembl:ENSENLP00000007317.1, ECO:0000313|Proteomes:UP000472264};
RN   [1] {ECO:0000313|Ensembl:ENSENLP00000007317.1}
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; A0A665TMD4; -.
DR   Ensembl; ENSENLT00000007631.1; ENSENLP00000007317.1; ENSENLG00000003292.1.
DR   Proteomes; UP000472264; 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; 3.
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:UP000472264}.
FT   DOMAIN          51..197
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          204..359
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   430 AA;  47514 MW;  315149AA21B6EE7F CRC64;
     MLPFPADVGS TKNCTCALSA GPHRLLATQA VQHVALNVPE TKVATLENGL RVASEDAGLT
     TCTVGLWIDA GSRYENERNN GTAHFLEHMA FKGTRKRSQL DLELEIENMG AHLNAYTSRE
     QTVYYAKAFS KDLPRAVEIL ADIIQNSMLG EAEIERERGV ILREMQEVET NLQEVVFDYL
     HATAYQNTAL GRTILGPTEN IKTINRGDLV EYITTHYKGP RIVLAAAGGV SHDELIDLAK
     YHFGKLPGRY QGEAPALPPC LFTGSEIRVR DDKMPLAHIA IAVEAVGWSH PDTIPLMVAN
     TLIGNWDRSF GGGVNLSSKL AQMACQGNLC HSFQSFNTCY TDTGLWGLYM VCEPGSTPIC
     EDIGRQMLCY SRRIPLNELE TRIDAIDATT IKDVCTKYIY NKAPAIAAVG PIEQLPDYNQ
     IRSGMFWMRT
//