ID   ATP23_CANAL             Reviewed;         238 AA.
AC   Q59Z51; A0A1D8PHW8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Mitochondrial inner membrane protease ATP23;
DE            EC=3.4.24.-;
GN   Name=ATP23; OrderedLocusNames=CAALFM_C206950CA;
GN   ORFNames=CaO19.2249, CaO19.9789;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017624; AOW27695.1; -; Genomic_DNA.
DR   RefSeq; XP_714839.2; XM_709746.2.
DR   AlphaFoldDB; Q59Z51; -.
DR   STRING; 237561.Q59Z51; -.
DR   MEROPS; M76.002; -.
DR   GeneID; 3643527; -.
DR   KEGG; cal:CAALFM_C206950CA; -.
DR   CGD; CAL0000186668; orf19.9789.
DR   VEuPathDB; FungiDB:C2_06950C_A; -.
DR   eggNOG; KOG3314; Eukaryota.
DR   HOGENOM; CLU_079125_0_0_1; -.
DR   InParanoid; Q59Z51; -.
DR   OrthoDB; 1288109at2759; -.
DR   PRO; PR:Q59Z51; -.
DR   Proteomes; UP000000559; Chromosome 2.
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; IEA:InterPro.
DR   GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
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..238
FT                   /note="Mitochondrial inner membrane protease ATP23"
FT                   /id="PRO_0000330057"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         138
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   238 AA;  27807 MW;  21C53A989E9CAD0D CRC64;
     MSTAAPQENS PELKLSPSSK LNGFEWWRRT LSYQTGLGLN AEEKAQYEFD YNNRNLAEKC
     QQCNEYRNWM LEYSPSVLFM MDHIKKLTKD KEPILTKENI TCDVCDFTKG GGFHPDEGIL
     LCANWIRNKW QLEDILTHEL VHVYDYLKFN LDMNNLRHHA CTEIRASMLS GECRIWQEIK
     KTGLGNFGKK FQDCIKRRAV LSVSSNPICK SPEEAEKVVS TVWNSCFNDT RPFERVYR