ATP23_ASHGO
ID ATP23_ASHGO Reviewed; 247 AA.
AC Q75EL5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Mitochondrial inner membrane protease ATP23;
DE EC=3.4.24.-;
GN Name=ATP23; OrderedLocusNames=AAR064W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016814; AAS50429.1; -; Genomic_DNA.
DR RefSeq; NP_982605.1; NM_207958.1.
DR AlphaFoldDB; Q75EL5; -.
DR STRING; 33169.AAS50429; -.
DR MEROPS; M76.001; -.
DR MEROPS; M76.002; -.
DR EnsemblFungi; AAS50429; AAS50429; AGOS_AAR064W.
DR GeneID; 4618790; -.
DR KEGG; ago:AGOS_AAR064W; -.
DR eggNOG; KOG3314; Eukaryota.
DR HOGENOM; CLU_079125_0_0_1; -.
DR InParanoid; Q75EL5; -.
DR OMA; VDHLACT; -.
DR Proteomes; UP000000591; Chromosome I.
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..247
FT /note="Mitochondrial inner membrane protease ATP23"
FT /id="PRO_0000330051"
FT ACT_SITE 147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 146
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 247 AA; 29138 MW; 21C932514285DF1C CRC64;
MSKEPNFPPS EKLEKVEAPA DLRSIAGFEW WRRTFEYKTG LGLTPEAKVQ YEKDYQYVLQ
REQCKQCYDN RDWLLKYSPT VVFMTQQIAK LNRRRTGDDS LHFDTSKIIC DVCPEWKSGG
FNPSLGILLC QNRIRDKWQM EDTLSHELVH QFDELKFEVD WMNLKHHACS EVRASNLSGE
CRLSQEFFRR GFNGSFGRGH QECVRRRAVL SVMGNPKCKD KAEAEQIVDE VWQSCFNDTR
PFEEIYR