ID   ATP23_SCHPO             Reviewed;         185 AA.
AC   Q1MTR0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Mitochondrial inner membrane protease atp23;
DE            EC=3.4.24.-;
GN   Name=atp23; ORFNames=SPCC320.12, SPCC330.17c;
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).
CC   -!- FUNCTION: Has a dual role in the assembly of mitochondrial ATPase. Acts
CC       as a protease that removes N-terminal residues of mitochondrial ATPase
CC       CF(0) subunit 6 at the intermembrane space side. Also involved in the
CC       correct assembly of the membrane-embedded ATPase CF(0) particle,
CC       probably mediating association of subunit 6 with the subunit 9 ring (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC       protein; Intermembrane side. Note=Associates loosely with the inner
CC       membrane. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M76 family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA20922.1; -; Genomic_DNA.
DR   PIR; T41299; T41299.
DR   RefSeq; NP_587717.1; NM_001022712.2.
DR   AlphaFoldDB; Q1MTR0; -.
DR   BioGRID; 275282; 1.
DR   STRING; 4896.SPCC320.12.1; -.
DR   MEROPS; M76.001; -.
DR   MEROPS; M76.A02; -.
DR   SwissPalm; Q1MTR0; -.
DR   MaxQB; Q1MTR0; -.
DR   PaxDb; Q1MTR0; -.
DR   EnsemblFungi; SPCC320.12.1; SPCC320.12.1:pep; SPCC320.12.
DR   GeneID; 2538697; -.
DR   KEGG; spo:SPCC320.12; -.
DR   PomBase; SPCC320.12; atp23.
DR   VEuPathDB; FungiDB:SPCC320.12; -.
DR   eggNOG; KOG3314; Eukaryota.
DR   HOGENOM; CLU_079125_0_0_1; -.
DR   InParanoid; Q1MTR0; -.
DR   OMA; CFNDREP; -.
DR   PhylomeDB; Q1MTR0; -.
DR   PRO; PR:Q1MTR0; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; ISM:PomBase.
DR   GO; GO:0034982; P:mitochondrial protein processing; ISO:PomBase.
DR   GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; IBA:GO_Central.
DR   InterPro; IPR019165; Peptidase_M76_ATP23.
DR   PANTHER; PTHR21711; PTHR21711; 1.
DR   Pfam; PF09768; Peptidase_M76; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Membrane; Metal-binding; Metalloprotease; Mitochondrion;
KW   Mitochondrion inner membrane; Protease; Reference proteome.
FT   CHAIN           1..185
FT                   /note="Mitochondrial inner membrane protease atp23"
FT                   /id="PRO_0000330073"
FT   ACT_SITE        87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         86
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   185 AA;  21512 MW;  3669EE9EAFAA1893 CRC64;
     MSEDPQSWSK ERKNCERVKR ALMSQSPVII FLKTALDRLN CNIEAKDISC QPCDAQSTGG
     YIPGKGIVLC ENRLYTKKMA ENTIAHEMIH MFDDHRFEVD WNNLRHQACS EIRASSMSGE
     CRWTKELRFG NIKTFRKHHQ ECVKRRATIS VQGNPNCKSK EQAEAIVEEV FNSCFNDFRP
     FEKIY