ID   ATP23_YEAS7             Reviewed;         227 AA.
AC   A6ZS94;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Mitochondrial inner membrane protease ATP23;
DE            EC=3.4.24.-;
GN   Name=ATP23; ORFNames=SCY_4805;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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}.
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DR   EMBL; AAFW02000067; EDN62826.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZS94; -.
DR   SMR; A6ZS94; -.
DR   PRIDE; A6ZS94; -.
DR   EnsemblFungi; EDN62826; EDN62826; SCY_4805.
DR   HOGENOM; CLU_079125_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
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_0000330072"
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;  26890 MW;  93232C45DB1DB10E CRC64;
     MNSSGDNAGF EWWRRTMQYK TGIGLTPEEK TRYEDDSKAR ELKKECLKCY EYRDWMLKYS
     PTVRFMVQAI TKLNKGSDSK FDDSKIICDY CPDWKGGGFH PELGILLCQN RLRDKWHLED
     TLSHELIHYF DDLKWQIDWL NLKHHACSEI RASSLSGECR FWEEFKRRGF RTGFHVARGH
     QDCVRRRAII SVSGNPNCQS KEHAAKIVDE VWDSCFADTR PFDEIYR