ATP23_MAGO7
ID ATP23_MAGO7 Reviewed; 273 AA.
AC A4RF31; G4NBU0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Mitochondrial inner membrane protease ATP23;
DE EC=3.4.24.-;
GN Name=ATP23; ORFNames=MGG_00480;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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; CM001235; EHA48998.1; -; Genomic_DNA.
DR RefSeq; XP_003718582.1; XM_003718534.1.
DR AlphaFoldDB; A4RF31; -.
DR STRING; 318829.MGG_00480T0; -.
DR MEROPS; M76.002; -.
DR PRIDE; A4RF31; -.
DR EnsemblFungi; MGG_00480T0; MGG_00480T0; MGG_00480.
DR GeneID; 2674715; -.
DR KEGG; mgr:MGG_00480; -.
DR VEuPathDB; FungiDB:MGG_00480; -.
DR eggNOG; KOG3314; Eukaryota.
DR HOGENOM; CLU_079125_0_0_1; -.
DR InParanoid; A4RF31; -.
DR OMA; VDHLACT; -.
DR OrthoDB; 1288109at2759; -.
DR Proteomes; UP000009058; Chromosome 5.
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..273
FT /note="Mitochondrial inner membrane protease ATP23"
FT /id="PRO_0000330066"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 170
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 273 AA; 31660 MW; DEB457D990FBE0C3 CRC64;
MASPQDNTPS GATPKPQTHE ETPDQVKLRI NGGERLNIRK NNPAETGFDP ATSKWVNYFK
VLTGSMTKEG QFHYREHLYR TNEERDLRRC EEQRDWLFRY SPVVRYMRDQ IRLLGGELDA
DNVVCRRCPS RLTADGRILG QAGGFSPQHG ILVCANSIRD RKHLEDTLAH EMVHAYDHLR
WQVDFVGEKD LRHAACTEIR ASMLSGECRW TREAFGRGNW TVTQQFQNCV RSRAIMSVRA
RARCRDTEHA TKVVNQVWDS CFSDTRPFDE IYK