ID   ATP23_NEUCR             Reviewed;         293 AA.
AC   Q7RYM1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 3.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Mitochondrial inner membrane protease atp23;
DE            EC=3.4.24.-;
GN   Name=atp23; ORFNames=NCU00107;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002238; EAA27995.3; -; Genomic_DNA.
DR   RefSeq; XP_957231.3; XM_952138.3.
DR   AlphaFoldDB; Q7RYM1; -.
DR   STRING; 5141.EFNCRP00000000370; -.
DR   MEROPS; M76.002; -.
DR   EnsemblFungi; EAA27995; EAA27995; NCU00107.
DR   GeneID; 3873394; -.
DR   KEGG; ncr:NCU00107; -.
DR   VEuPathDB; FungiDB:NCU00107; -.
DR   HOGENOM; CLU_079125_0_0_1; -.
DR   InParanoid; Q7RYM1; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
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..293
FT                   /note="Mitochondrial inner membrane protease atp23"
FT                   /id="PRO_0000330068"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         190
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   293 AA;  33405 MW;  79E42D0FEB62025B CRC64;
     MSPAPTTSAG PASSGIPPSS LPTSTVTEDD TKPSSSSSKA NDLLPRYLTN DPSRTGYDPS
     IQWWMNYFKI LTGQITPEGV EHYREDRYKA NEARDCARCE ADRDWLFQNS PVIRFLREKV
     ANLNGVLDET NVVCRRCPSR IVVIPGNKEK GEEDRIEVAR QGGGFSPDHG ILLCANEMRN
     RGHLEDTLAH EMVHAWDHLR WKVDWFGEKS LRHAACTEIR ASMLSGECRW TRESIVRGNW
     TLTQQFQNCV RMRAIQSVMA RPTCKDDVHA TKVVNEVWDS CFSDKRPFEE IYR