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
//