ID   MPPB_LENED              Reviewed;         466 AA.
AC   Q9Y8B5;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Mitochondrial-processing peptidase subunit beta;
DE            EC=3.4.24.64 {ECO:0000250|UniProtKB:P10507};
DE   AltName: Full=Beta-MPP;
DE   Flags: Precursor;
GN   Name=mppB;
OS   Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Omphalotaceae; Lentinula.
OX   NCBI_TaxID=5353;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9461410; DOI=10.1016/s0378-1119(97)00576-3;
RA   Zhang M., Xie W., Leung G.S., Deane E.E., Kwan H.S.;
RT   "Cloning and characterization of the gene encoding beta subunit of
RT   mitochondrial processing peptidase from the basidiomycete Lentinula
RT   edodes.";
RL   Gene 206:23-27(1998).
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).
CC       {ECO:0000250|UniProtKB:P10507, 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:P10507};
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 mppA is required for catalytic
CC       activity. {ECO:0000250|UniProtKB:P10507}.
CC   -!- SUBUNIT: Heterodimer of mppA (alpha) and mppB (beta) subunits, forming
CC       the mitochondrial processing protease (MPP) in which mppA is involved
CC       in substrate recognition and binding and mppB is the catalytic subunit.
CC       {ECO:0000250|UniProtKB:P10507}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P10507}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR   EMBL; AF146393; AAD37722.1; -; Genomic_DNA.
DR   PIR; JC6525; JC6525.
DR   AlphaFoldDB; Q9Y8B5; -.
DR   SMR; Q9Y8B5; -.
DR   MEROPS; M16.003; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW   Transit peptide; Zinc.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..466
FT                   /note="Mitochondrial-processing peptidase subunit beta"
FT                   /id="PRO_0000026781"
FT   ACT_SITE        76
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ   SEQUENCE   466 AA;  51163 MW;  CE3E6E797A1C29D6 CRC64;
     MLGRVLKSAA RSQRGLRSFA TTTNLGPFTE ISTLSNGLTV ATESQPHAQT ATVGVWIDAG
     SRAETDKTNG TAHFLEHMAF KGTGRRSQHA LELEVENIGA HLNAYTSREQ TVYYAKSFSK
     DVPVAVDIIS DILQNSKLES GAIERERDVI LREQQEVDKQ LEEVVFDHLH AVAFQGQPLG
     RTILGPKNNI LSIQRDDLAS YIQTNYTADR MVLVGTGGVD HQSLVKLAEK HFSSLPVSAN
     PLALGRLSSE RKPTFVGSEA RIRDDELPTA HVAIAVEGVG WSSPDYFPMM VMQSIFGNWD
     RSLGASSLLS SRLSHIISSN SLANSFMSFS TSYSDTGLWG IYLVSENLMN LDDTLHFTLK
     EWTRMSIAPT EGEVERAKSQ LKAGLLLSLD GTTAVAEDIG RQIVTSGKRM TPAQIENAVD
     AVSVDDIKRV AQKYLWDKDF ALAAFGNIDG LKDYGRIRND MSSMLY