ID   MPPA2_DICDI             Reviewed;         445 AA.
AC   Q54F93;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Mitochondrial-processing peptidase subunit alpha-2;
DE   AltName: Full=Alpha-MPP 2;
DE            Short=Ddalpha-MPP 2;
DE   AltName: Full=Inactive zinc metalloprotease alpha-2 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=mppA2; Synonyms=pmpca; ORFNames=DDB_G0290997;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA   Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA   Soldati T.;
RT   "Proteomics fingerprinting of phagosome maturation and evidence for the
RT   role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
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:Q86A84}.
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:P10507}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q86A84}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR   EMBL; AAFI02000174; EAL61929.1; -; Genomic_DNA.
DR   RefSeq; XP_635444.1; XM_630352.1.
DR   AlphaFoldDB; Q54F93; -.
DR   SMR; Q54F93; -.
DR   STRING; 44689.DDB0237967; -.
DR   PaxDb; Q54F93; -.
DR   EnsemblProtists; EAL61929; EAL61929; DDB_G0290997.
DR   GeneID; 8627944; -.
DR   KEGG; ddi:DDB_G0290997; -.
DR   dictyBase; DDB_G0290997; mppA2.
DR   eggNOG; KOG2067; Eukaryota.
DR   HOGENOM; CLU_009902_0_0_1; -.
DR   InParanoid; Q54F93; -.
DR   OMA; WVGEFFT; -.
DR   PhylomeDB; Q54F93; -.
DR   Reactome; R-DDI-611105; Respiratory electron transport.
DR   PRO; PR:Q54F93; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IBA:GO_Central.
DR   GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
PE   1: Evidence at protein level;
KW   Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..13
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           14..445
FT                   /note="Mitochondrial-processing peptidase subunit alpha-2"
FT                   /id="PRO_0000337763"
SQ   SEQUENCE   445 AA;  47746 MW;  C8D40AF48528740B CRC64;
     MIGRFIARNY TTSIFQESKR IVESTTLSNG LKVVSLVGGY TGPAVSLGLY IKTGSRNETQ
     ETAGLNQVLK GLAFESNTNK LGIEVQRDIE VSGSTAFAQA SRDNLLIALQ TLPNRSLQML
     NNLANITKPT LPYHEVRDVT EIIVKESEAY NHDSYSSIFE SVHQTAFRGK TLGRPLVAPI
     CNLGNITKDA VTNWVNSTYK PSNMILVGVG LSHNELIEEA EKVTFGNDES STSISNETAQ
     YIGGESLKYS SGNSKVVLAF EGTAQSNIKD VAAFSVLQSI LGNGCPKTAP GHGRTSRLFS
     LTKNNSNIVN SEAFNLTYGD SGLFGVVAEV EGATVGKTVS LITSEIVAAS KTAGQELERA
     KAVTKSSVLE QAESRTSALE FIGKQAIYTD KVLTPAEFAE EISKVTSEDI KRVAKKMTSK
     KPTLVVVGDV SDAPTIESVQ SQLKL