ID   IMP1_SCHPO              Reviewed;         157 AA.
AC   O74800;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Mitochondrial inner membrane protease subunit 1;
DE            EC=3.4.21.-;
GN   Name=imp1; ORFNames=SPBC2D10.07c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Catalyzes the removal of transit peptides required for the
CC       targeting of proteins from the mitochondrial matrix, across the inner
CC       membrane, into the inter-membrane space. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of 2 subunits, imp1 and imp2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000305|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. IMP1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAA21165.1; -; Genomic_DNA.
DR   PIR; T40110; T40110.
DR   RefSeq; NP_596226.1; NM_001022146.2.
DR   AlphaFoldDB; O74800; -.
DR   SMR; O74800; -.
DR   STRING; 4896.SPBC2D10.07c.1; -.
DR   MEROPS; S26.002; -.
DR   PaxDb; O74800; -.
DR   EnsemblFungi; SPBC2D10.07c.1; SPBC2D10.07c.1:pep; SPBC2D10.07c.
DR   GeneID; 2540493; -.
DR   KEGG; spo:SPBC2D10.07c; -.
DR   PomBase; SPBC2D10.07c; -.
DR   VEuPathDB; FungiDB:SPBC2D10.07c; -.
DR   eggNOG; KOG0171; Eukaryota.
DR   HOGENOM; CLU_028723_4_3_1; -.
DR   OMA; CKGPSME; -.
DR   PhylomeDB; O74800; -.
DR   PRO; PR:O74800; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0042720; C:mitochondrial inner membrane peptidase complex; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0004222; F:metalloendopeptidase activity; ISS:PomBase.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; ISS:PomBase.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   CDD; cd06530; S26_SPase_I; 1.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; SSF51306; 1.
DR   TIGRFAMs; TIGR02227; sigpep_I_bact; 1.
DR   PROSITE; PS00760; SPASE_I_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Membrane; Mitochondrion; Mitochondrion inner membrane; Protease;
KW   Reference proteome.
FT   CHAIN           1..157
FT                   /note="Mitochondrial inner membrane protease subunit 1"
FT                   /id="PRO_0000314116"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        80
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   157 AA;  17269 MW;  893D2267E108C30D CRC64;
     MAGMFRIPIA VVQIAAFVHQ IHEYLFQVQM TSGPSMMPTL NSGGEFVLLD KLHGRFARSC
     SVGDVVVSAK PSDSKQHVCK RIIGMPGDTI YVDPTSSNKK ITIPLGHVWL AGDNIAHSLD
     SRNYGPVPMG LIKAKVIARV WPHPHWMSNI LNDIDVE