ID   MPPA_NEUCR              Reviewed;         577 AA.
AC   P23955; Q7RVH4;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   25-MAY-2022, entry version 150.
DE   RecName: Full=Mitochondrial-processing peptidase subunit alpha {ECO:0000303|PubMed:8106471};
DE   AltName: Full=Alpha-MPP;
DE   AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000305};
DE   AltName: Full=Matrix processing peptidase {ECO:0000303|PubMed:2967109};
DE   Flags: Precursor;
GN   Name=mpp {ECO:0000303|PubMed:2967109}; ORFNames=NCU06270;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF N-TERMINUS.
RX   PubMed=2141023; DOI=10.1016/s0021-9258(19)38754-x;
RA   Schneider H., Arretz M., Wachter E., Neupert W.;
RT   "Matrix processing peptidase of mitochondria. Structure-function
RT   relationships.";
RL   J. Biol. Chem. 265:9881-9887(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
RN   [3]
RP   FUNCTION, INTERACTION WITH PEP, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=2967109; DOI=10.1016/0092-8674(88)90096-7;
RA   Hawlitschek G., Schneider H., Schmidt B., Tropschug M., Hartl F.-U.,
RA   Neupert W.;
RT   "Mitochondrial protein import: identification of processing peptidase and
RT   of PEP, a processing enhancing protein.";
RL   Cell 53:795-806(1988).
RN   [4]
RP   FUNCTION.
RX   PubMed=8106471; DOI=10.1016/s0021-9258(17)37639-1;
RA   Arretz M., Schneider H., Guiard B., Brunner M., Neupert W.;
RT   "Characterization of the mitochondrial processing peptidase of Neurospora
RT   crassa.";
RL   J. Biol. Chem. 269:4959-4967(1994).
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:0000269|PubMed:8106471, ECO:0000305|PubMed:2967109}.
CC   -!- SUBUNIT: Heterodimer of mpp (alpha) and pep (beta) subunits, forming
CC       the mitochondrial processing protease (MPP) in which mpp is involved in
CC       substrate recognition and binding and pep is the catalytic subunit.
CC       {ECO:0000269|PubMed:2967109}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:2967109}.
CC   -!- DOMAIN: Appears to contain two domains of approximately equal size
CC       which are separated by a loop-like sequence.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be the catalytic subunit
CC       (PubMed:2967109). The low processing activity which was previously
CC       observed with alpha-MPP which has been immunoprecipitated from a
CC       mitochondrial extract is most likely due to contamination by the beta-
CC       subunit (PubMed:8106471). Does not seem to have a protease activity as
CC       it lack the zinc-binding site. {ECO:0000305,
CC       ECO:0000305|PubMed:2967109, ECO:0000305|PubMed:8106471}.
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DR   EMBL; J05484; AAA33597.1; -; mRNA.
DR   EMBL; CM002238; EAA33638.1; -; Genomic_DNA.
DR   PIR; A36442; A36442.
DR   RefSeq; XP_962874.1; XM_957781.2.
DR   AlphaFoldDB; P23955; -.
DR   SMR; P23955; -.
DR   STRING; 5141.EFNCRP00000005979; -.
DR   EnsemblFungi; EAA33638; EAA33638; NCU06270.
DR   GeneID; 3879027; -.
DR   KEGG; ncr:NCU06270; -.
DR   VEuPathDB; FungiDB:NCU06270; -.
DR   HOGENOM; CLU_009902_5_2_1; -.
DR   InParanoid; P23955; -.
DR   OMA; LKYHHSP; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0017087; C:mitochondrial processing peptidase complex; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0061133; F:endopeptidase activator activity; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IBA:GO_Central.
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; Mitochondrion; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..35
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2141023"
FT   CHAIN           36..577
FT                   /note="Mitochondrial-processing peptidase subunit alpha"
FT                   /id="PRO_0000026771"
FT   REGION          259..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        107
FT                   /note="T -> A (in Ref. 1; AAA33597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        107
FT                   /note="T -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   577 AA;  63041 MW;  029491B2FBA01ADB CRC64;
     MLNRFRPARL VAQSSRCLPL TRARAGPLPV NNARTLATRA AAVNTKEPTE RDNITTLSNG
     VRVASEDLPD AFSGVGVYID AGSRYENDYV RGASHIMDRL AFKSTSTRTA DEMLETVEKL
     GGNIQCASSR ESMMYQAATF NKAIPTAVEL MAETIRDPKL TDEELEGQIM TAQYEVNEIW
     SKAELILPEL VHMAAFKDNT LGNPLLCPKE RLDYINRDVI QTYRDAFYRP ERLVVAFAGV
     PHERAVKLAE KYFGDMKASD APGLSRTGSE TSVDSLVSES SEASSESSSS SSDSSESSGG
     LLSKLFSPKA KKATPNPFLT RVPISTEDLT RPAHYTGGFL TLPSQPPPLN PNLPTFTHIQ
     LAFEGLAISD DDIYALATLQ TLLGGGGSFS AGGPGKGMYS RLYTNVLNQH GWVESCVAFN
     HSYTDSGLFG IAASCYPGRT LPMLQVMCRE LHALTTDHGY SALGELEVSR AKNQLRSSLL
     MNLESRMVEL EDLGRQVQVH GRKIPVREMT RRINELTVKD LRRVAKRVVG GMANNAGQGS
     GAPTVVLQEA TVQGLKTTEL GWDQIQDTIA QWKLGRR