ID   ATP23_YEAS8             Reviewed;         227 AA.
AC   C8ZFP7;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 2.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Mitochondrial inner membrane protease ATP23;
DE            EC=3.4.24.-;
GN   Name=ATP23; ORFNames=EC1118_1N18_0606g;
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse;
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA   Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC   -!- FUNCTION: Has a dual role in the assembly of mitochondrial ATPase. Acts
CC       as a protease that removes the N-terminal 10 residues of mitochondrial
CC       ATPase CF(0) subunit 6 (ATP6) at the intermembrane space side. Also
CC       involved in the correct assembly of the membrane-embedded ATPase CF(0)
CC       particle, probably mediating association of ATP6 with the subunit 9
CC       ring (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ATP6. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAY82213.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; FN393083; CAY82213.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; C8ZFP7; -.
DR   MEROPS; M76.002; -.
DR   EnsemblFungi; CAY82213; CAY82213; EC1118_1N18_0617g.
DR   HOGENOM; CLU_079125_0_0_1; -.
DR   Proteomes; UP000000286; Chromosome XIV, Scaffold EC1118_1N18.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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.
FT   CHAIN           1..227
FT                   /note="Mitochondrial inner membrane protease ATP23"
FT                   /id="PRO_0000392082"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         124
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   227 AA;  26920 MW;  933268495F00710E CRC64;
     MNSSGDNAGF EWWRRTMQYK TGIGLTPEEK TRYEDDSKAR ELKKECLKCY EYRDWMLKYS
     PTVRFMVQAI TKLNKGSDSK FDDSKIICDY CPDWKSGGFH PELGILLCQN RLRDKWHLED
     TLSHELIHYF DDLKWQIDWL NLKHHACSEI RASSLSGECR FWEEFKRRGF RTGFHVARGH
     QDCVRRRAII SVSGNPNCQS KEHAAKIVDE VWDSCFADTR PFDEIYR