ID   ATP23_CHAGB             Reviewed;         276 AA.
AC   Q2H8S7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Mitochondrial inner membrane protease ATP23;
DE            EC=3.4.24.-;
GN   Name=ATP23; ORFNames=CHGG_03377;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAQ91442.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAQ91442.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CH408030; EAQ91442.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001229893.1; XM_001229892.1.
DR   AlphaFoldDB; Q2H8S7; -.
DR   STRING; 306901.Q2H8S7; -.
DR   MEROPS; M76.002; -.
DR   EnsemblFungi; EAQ91442; EAQ91442; CHGG_03377.
DR   GeneID; 4389292; -.
DR   HOGENOM; CLU_079125_0_0_1; -.
DR   InParanoid; Q2H8S7; -.
DR   OrthoDB; 1288109at2759; -.
DR   Proteomes; UP000001056; 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; Reference proteome.
FT   CHAIN           1..276
FT                   /note="Mitochondrial inner membrane protease ATP23"
FT                   /id="PRO_0000330059"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..39
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         173
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   276 AA;  31556 MW;  E086BB097A351C86 CRC64;
     MATPPPPQLS STSTQPPSPS SASSNPQQPS PPKTQPPLPR FLDNDPARTG YDPTVKWWLN
     YFRIMTGQVT REGVEHYRED RYKANEARDC ARCEADRAYL FAYSPTIRFL RDKVAALNGT
     LDETNVVCRR CPARVAEDGR VVRQGGGFSP EHGILICANE MRDRSHLEDT LAHEMVHAWD
     HLRWKVDWSG GGNLRHAACT EIRASMLSGE CRWTRETMTR GNWTLTQQFQ NCVRMRAIQS
     VMARPTCRDD VHATKVVNEV WDSCFSDKRP FEEVYR