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   16-JUN-2009, entry version 47.
DE   RecName: Full=Mitochondrial-processing peptidase subunit beta;
DE            EC=3.4.24.64;
DE   AltName: Full=Beta-MPP;
DE   Flags: Precursor;
GN   Name=mppB;
OS   Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Homobasidiomycetes; Agaricomycetidae; Agaricales; Tricholomataceae;
OC   Lentinula.
OX   NCBI_TaxID=5353;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98121308; 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: Cleaves presequences (transit peptides) from
CC       mitochondrial protein precursors.
CC   -!- CATALYTIC ACTIVITY: Release of N-terminal transit peptides from
CC       precursor proteins imported into the mitochondrion, typically with
CC       Arg in position P2.
CC   -!- COFACTOR: Divalent cations (By similarity).
CC   -!- SUBUNIT: Heterodimer of alpha and beta subunits (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
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DR   EMBL; AF146393; AAD37722.1; -; Genomic_DNA.
DR   PIR; JC6525; JC6525.
DR   HSSP; P10507; 1HR6.
DR   MEROPS; M16.003; -.
DR   MEROPS; M16.980; -.
DR   BRENDA; 3.4.24.64; 260981.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR011237; Pept_M16_core.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   Gene3D; G3DSA:3.30.830.10; Pept_M16_core; 2.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW   Transit peptide; Zinc.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    466       Mitochondrial-processing peptidase
FT                                subunit beta.
FT                                /FTId=PRO_0000026781.
FT   ACT_SITE     76     76       Proton acceptor (By similarity).
FT   METAL        73     73       Zinc (By similarity).
FT   METAL        77     77       Zinc (By similarity).
FT   METAL       153    153       Zinc (By similarity).
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
//