ID   ATP23_AJECN             Reviewed;         240 AA.
AC   A6RCS8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Mitochondrial inner membrane protease ATP23;
DE            EC=3.4.24.-;
GN   Name=ATP23; ORFNames=HCAG_07436;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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=EDN10975.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EDN10975.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CH476662; EDN10975.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001538014.1; XM_001537964.1.
DR   AlphaFoldDB; A6RCS8; -.
DR   STRING; 339724.A6RCS8; -.
DR   MEROPS; M76.002; -.
DR   EnsemblFungi; EDN10975; EDN10975; HCAG_07436.
DR   GeneID; 5444331; -.
DR   KEGG; aje:HCAG_07436; -.
DR   HOGENOM; CLU_079125_4_1_1; -.
DR   OrthoDB; 1288109at2759; -.
DR   Proteomes; UP000009297; 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..240
FT                   /note="Mitochondrial inner membrane protease ATP23"
FT                   /id="PRO_0000330050"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        140
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         139
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   240 AA;  27823 MW;  9AE02BAA4063715B CRC64;
     MAGTNSLGAG PDTPVPSKDT GFTPGDDTWT QMKNMFSILT GNMTEEGKEQ FLLARDIRNE
     ENDCKRCEDQ RDYLIKYSPI IIRFLQDNIR QLGGDISSHN IHCRRCTQRQ AGGFDPQYGI
     RICANAMKDQ GHLEDTMAHE MMHAYDHLRF KLDWTDNLRH AACTEIRASS LSGECRWARE
     FFRRGQWKLT QQHQECVRRR AALSVMARPA CKDAEHAKQV VDEVWDSCFR DTRPFDEIYR