ATPO_ASHGO
ID ATPO_ASHGO Reviewed; 207 AA.
AC Q75EZ3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=ATP synthase subunit 5, mitochondrial;
DE Short=ATP synthase chain 5;
DE AltName: Full=Oligomycin sensitivity conferral protein;
DE Short=OSCP;
DE Flags: Precursor;
GN Name=ATP5; OrderedLocusNames=AAL065C;
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: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core and F(0)
CC - containing the membrane proton channel, linked together by a central
CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. Part of the complex
CC F(0) domain and the peripheric stalk, which acts as a stator to hold
CC the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC relative to the rotary elements (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the ATPase delta chain family. {ECO:0000305}.
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DR EMBL; AE016814; AAS50301.1; -; Genomic_DNA.
DR RefSeq; NP_982477.1; NM_207830.1.
DR AlphaFoldDB; Q75EZ3; -.
DR SMR; Q75EZ3; -.
DR STRING; 33169.AAS50301; -.
DR EnsemblFungi; AAS50301; AAS50301; AGOS_AAL065C.
DR GeneID; 4618447; -.
DR KEGG; ago:AGOS_AAL065C; -.
DR eggNOG; KOG1662; Eukaryota.
DR HOGENOM; CLU_085114_0_0_1; -.
DR InParanoid; Q75EZ3; -.
DR OMA; MVDNIQD; -.
DR Proteomes; UP000000591; Chromosome I.
DR GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; IBA:GO_Central.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:EnsemblFungi.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR Gene3D; 1.10.520.20; -; 1.
DR HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR InterPro; IPR000711; ATPase_OSCP/dsu.
DR PANTHER; PTHR11910; PTHR11910; 1.
DR Pfam; PF00213; OSCP; 1.
DR PRINTS; PR00125; ATPASEDELTA.
DR SUPFAM; SSF47928; SSF47928; 1.
DR TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..207
FT /note="ATP synthase subunit 5, mitochondrial"
FT /id="PRO_0000002651"
SQ SEQUENCE 207 AA; 21619 MW; BE0D127239086E5E CRC64;
MSSRVFVRSL AAAAKAGVKP PIQLFGLEGT YASALFTAAS KTTSIESAGK ALASLSKTIA
KDAKLGAILA NPALPAGDRT VVVQTLAQKT PGMDAAVQNL MQVLAENNRL NLLQGVAGEF
TKLTDAHNGL VQATVTTAQP LEGKLFRRVE KALAQSSFIG AGKTLKLENV VKPEIQGGLI
VEVADRTVDL SIASRISKLN QVLKESI