ID   ATP23_YARLI             Reviewed;         250 AA.
AC   Q6C253;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Mitochondrial inner membrane protease ATP23;
DE            EC=3.4.24.-;
GN   Name=ATP23; OrderedLocusNames=YALI0F10769g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382132; CAG78066.1; -; Genomic_DNA.
DR   RefSeq; XP_505259.1; XM_505259.1.
DR   AlphaFoldDB; Q6C253; -.
DR   STRING; 4952.CAG78066; -.
DR   MEROPS; M76.002; -.
DR   EnsemblFungi; CAG78066; CAG78066; YALI0_F10769g.
DR   GeneID; 2908892; -.
DR   KEGG; yli:YALI0F10769g; -.
DR   VEuPathDB; FungiDB:YALI0_F10769g; -.
DR   HOGENOM; CLU_079125_0_0_1; -.
DR   InParanoid; Q6C253; -.
DR   OMA; VDHLACT; -.
DR   Proteomes; UP000001300; Chromosome F.
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..250
FT                   /note="Mitochondrial inner membrane protease ATP23"
FT                   /id="PRO_0000330077"
FT   ACT_SITE        151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         150
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   250 AA;  28421 MW;  771117253E92B5CC CRC64;
     MSDKPTETVS VSESVATPAV AATEPAPSLP VVNPSSLPSG FEWWRQTMAY KTGFMSAEES
     VQYEQDRLIK ERYAECLSCE KNKQWVMAYS PTVRFMKDQI EKIGGDISSN NVFCDHCDDF
     KAGGFHPKYG ILVCQNHVKS RSHLEDTLAH EMVHYYDNTK FKVDWMNLKH HACSEIRAST
     LSGECRMMNE LMKGKLARLT RGHQECAKRR AILSVMANPG CKDEAQATQV VNEVWDSCFN
     DTRPFDTIYR