ID   MPPA_SOLTU              Reviewed;         504 AA.
AC   P29677;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Mitochondrial-processing peptidase subunit alpha;
DE   AltName: Full=Alpha-MPP;
DE   AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000305};
DE   AltName: Full=Ubiquinol-cytochrome-c reductase subunit II;
DE            EC=7.1.1.8;
DE   Flags: Precursor;
GN   Name=MPP;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 270-280 AND 400-419.
RC   STRAIN=cv. Desiree; TISSUE=Green leaf;
RX   PubMed=1324169; DOI=10.1002/j.1460-2075.1992.tb05399.x;
RA   Braun H.P., Emmermann M., Kruft V., Schmitz U.K.;
RT   "The general mitochondrial processing peptidase from potato is an integral
RT   part of cytochrome c reductase of the respiratory chain.";
RL   EMBO J. 11:3219-3227(1992).
CC   -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC       mitochondrial processing protease (MPP), which cleaves the
CC       mitochondrial sequence off newly imported precursors proteins.
CC       {ECO:0000250|UniProtKB:P11914}.
CC   -!- FUNCTION: This is a component of the ubiquinol-cytochrome c reductase
CC       complex (complex III or cytochrome b-c1 complex), which is part of the
CC       mitochondrial respiratory chain. Mediates formation of the complex
CC       between cytochromes c and c1.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC         Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:132124; EC=7.1.1.8;
CC   -!- SUBUNIT: Heterodimer of alpha and beta subunits, forming the
CC       mitochondrial processing protease (MPP) in which subunit alpha is
CC       involved in substrate recognition and binding and subunit beta is the
CC       catalytic subunit. {ECO:0000250|UniProtKB:P11914}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC   -!- CAUTION: Does not seem to have a protease activity as it lack the zinc-
CC       binding site. {ECO:0000305}.
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DR   EMBL; X66284; CAA46990.1; -; mRNA.
DR   PIR; S23558; S23558.
DR   RefSeq; NP_001275168.1; NM_001288239.1.
DR   AlphaFoldDB; P29677; -.
DR   SMR; P29677; -.
DR   IntAct; P29677; 1.
DR   STRING; 4113.PGSC0003DMT400000784; -.
DR   CarbonylDB; P29677; -.
DR   PRIDE; P29677; -.
DR   ProMEX; P29677; -.
DR   EnsemblPlants; RHC12H1G0483.2.1; RHC12H1G0483.2.1; RHC12H1G0483.2.
DR   GeneID; 102580877; -.
DR   Gramene; RHC12H1G0483.2.1; RHC12H1G0483.2.1; RHC12H1G0483.2.
DR   KEGG; sot:102580877; -.
DR   eggNOG; KOG2067; Eukaryota.
DR   InParanoid; P29677; -.
DR   OrthoDB; 631107at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P29677; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW   Transit peptide; Translocase; Transport.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT   CHAIN           ?..504
FT                   /note="Mitochondrial-processing peptidase subunit alpha"
FT                   /id="PRO_0000026776"
SQ   SEQUENCE   504 AA;  54677 MW;  FD3053688571D987 CRC64;
     MYRCASSRLS SLKARQGNRV LTRFSSSAAV ATKPSGGLFS WITGDTSSSV TPLDFPLNDV
     KLSPPLPDYV EPAKTQITTL ANGLKVASEA SVNPAASIGL YVDCGSIYET PASYGATHLL
     ERMAFKSTLN RSHLRIVREI EAIGGNVTAS ASREHMIYTY DALKTYVPQM VEMLADCVRN
     PAFLDWEVKE QLEKVKAEIS EYSKNPQHLL LEAVHSAGYA GPYGNSLMAT EATINRLNST
     VLEEFVAENY TAPRMVLAAS GVEHEEFLKV AEPLLSDLPK VATIEEPKPV YVGGDYRCQA
     DAEMTHFALA FEVPGGWMSE KESMTLTVLQ MLMGGGGSFS AGGPGKGMYS RLYLRVLNQY
     PQIHAFSAFS SIYNNTGLFG IQGTTSSDFG PQAVDVAVKE LIAVANPSEV DQVQLNRAKQ
     ATKSAILMNL ESRMVASEDI GRQLLTYGER NPVEHFLKAI DAVSAKDIAS VVQKLISSPL
     TMASYGDVLS LPSYDAVSSR FRSK