ID   ATPO_YEAST              Reviewed;         212 AA.
AC   P09457; D6VSS7;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-SEP-2026, entry version 211.
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; Synonyms=OSCP; OrderedLocusNames=YDR298C;
GN   ORFNames=D9740.11;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 24657 / D273-10B;
RX   PubMed=2971156; DOI=10.1093/nar/16.16.8181;
RA   Lee M., Jones D., Mueller D.M.;
RT   "The sequence of the yeast ATP5 gene.";
RL   Nucleic Acids Res. 16:8181-8181(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2146269; DOI=10.1016/s0021-9258(17)30622-1;
RA   Uh M., Jones D., Mueller D.M.;
RT   "The gene coding for the yeast oligomycin sensitivity-conferring protein.";
RL   J. Biol. Chem. 265:19047-19052(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867; DOI=10.1038/387s075;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA   Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA   van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT   "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT   phosphorylation in assembly of the ATP synthase.";
RL   Mol. Cell. Proteomics 6:1896-1906(2007).
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.
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- MISCELLANEOUS: Present with 32400 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family. {ECO:0000305}.
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DR   EMBL; X12356; CAA30917.1; -; Genomic_DNA.
DR   EMBL; M32487; AAA34836.1; -; Genomic_DNA.
DR   EMBL; U28374; AAB64734.1; -; Genomic_DNA.
DR   EMBL; AY557732; AAS56058.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12137.1; -; Genomic_DNA.
DR   PIR; S05726; PWBYD.
DR   RefSeq; NP_010584.1; NM_001180606.1.
DR   PDB; 6B8H; EM; 3.60 A; O/o=18-212.
DR   PDB; 6CP3; EM; 3.80 A; Y=18-212.
DR   PDB; 6CP6; EM; 3.60 A; Y=18-212.
DR   PDB; 7TJY; EM; 3.80 A; O=18-212.
DR   PDB; 7TJZ; EM; 4.40 A; O=18-212.
DR   PDB; 7TK0; EM; 4.40 A; O=18-212.
DR   PDB; 7TK1; EM; 7.10 A; O=18-212.
DR   PDB; 7TK2; EM; 6.50 A; O=18-212.
DR   PDB; 7TK3; EM; 6.30 A; O=18-212.
DR   PDB; 7TK4; EM; 7.00 A; O=18-212.
DR   PDB; 7TK5; EM; 7.80 A; O=18-212.
DR   PDB; 7TK6; EM; 6.50 A; O=18-212.
DR   PDB; 7TK7; EM; 6.70 A; O=18-212.
DR   PDB; 7TK8; EM; 4.70 A; O=18-212.
DR   PDB; 7TK9; EM; 6.00 A; O=18-212.
DR   PDB; 7TKA; EM; 7.10 A; O=18-212.
DR   PDB; 7TKB; EM; 6.30 A; O=18-212.
DR   PDB; 7TKC; EM; 5.80 A; O=18-212.
DR   PDB; 7TKD; EM; 7.70 A; O=18-212.
DR   PDB; 7TKE; EM; 7.10 A; O=18-212.
DR   PDB; 7TKF; EM; 7.10 A; O=18-212.
DR   PDB; 7TKG; EM; 4.50 A; O=18-212.
DR   PDB; 7TKH; EM; 4.40 A; O=18-212.
DR   PDB; 7TKI; EM; 7.10 A; O=18-212.
DR   PDB; 7TKJ; EM; 7.50 A; O=18-212.
DR   PDB; 7TKK; EM; 7.30 A; O=18-212.
DR   PDB; 7TKL; EM; 6.40 A; O=18-212.
DR   PDB; 7TKM; EM; 4.50 A; O=18-212.
DR   PDB; 7TKN; EM; 7.10 A; O=18-212.
DR   PDB; 7TKO; EM; 4.80 A; O=18-212.
DR   PDB; 7TKP; EM; 4.60 A; O=18-212.
DR   PDB; 7TKQ; EM; 4.50 A; O=18-212.
DR   PDB; 7TKR; EM; 6.50 A; O=18-212.
DR   PDB; 7TKS; EM; 7.50 A; O=18-212.
DR   PDB; 8F29; EM; 4.00 A; Y=24-210.
DR   PDB; 8F39; EM; 3.50 A; Y=24-189.
DR   PDB; 8FKJ; EM; 4.20 A; Y=24-189.
DR   PDB; 8FL8; EM; 4.20 A; Y=24-189.
DR   AlphaFoldDB; P09457; -.
DR   EMDB; EMD-25946; -.
DR   EMDB; EMD-25947; -.
DR   EMDB; EMD-25948; -.
DR   EMDB; EMD-25949; -.
DR   EMDB; EMD-25954; -.
DR   EMDB; EMD-25955; -.
DR   EMDB; EMD-25956; -.
DR   EMDB; EMD-25957; -.
DR   EMDB; EMD-25958; -.
DR   EMDB; EMD-25959; -.
DR   EMDB; EMD-25960; -.
DR   EMDB; EMD-25961; -.
DR   EMDB; EMD-25962; -.
DR   EMDB; EMD-25963; -.
DR   EMDB; EMD-25964; -.
DR   EMDB; EMD-25965; -.
DR   EMDB; EMD-25966; -.
DR   EMDB; EMD-25967; -.
DR   EMDB; EMD-25968; -.
DR   EMDB; EMD-25969; -.
DR   EMDB; EMD-25970; -.
DR   EMDB; EMD-25971; -.
DR   EMDB; EMD-25972; -.
DR   EMDB; EMD-25973; -.
DR   EMDB; EMD-25974; -.
DR   EMDB; EMD-25975; -.
DR   EMDB; EMD-25976; -.
DR   EMDB; EMD-25977; -.
DR   EMDB; EMD-25978; -.
DR   EMDB; EMD-25979; -.
DR   EMDB; EMD-25980; -.
DR   EMDB; EMD-28809; -.
DR   EMDB; EMD-28835; -.
DR   EMDB; EMD-7546; -.
DR   EMDB; EMD-7548; -.
DR   SMR; P09457; -.
DR   BioGRID; 32350; 190.
DR   ComplexPortal; CPX-3281; Mitochondrial proton-transporting ATP synthase complex.
DR   DIP; DIP-3037N; -.
DR   FunCoup; P09457; 920.
DR   IntAct; P09457; 44.
DR   MINT; P09457; -.
DR   STRING; 4932.YDR298C; -.
DR   TCDB; 3.A.2.1.3; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   iPTMnet; P09457; -.
DR   PaxDb; 4932-YDR298C; -.
DR   PeptideAtlas; P09457; -.
DR   EnsemblFungi; YDR298C_mRNA; YDR298C; YDR298C.
DR   GeneID; 851892; -.
DR   KEGG; sce:YDR298C; -.
DR   AGR; SGD:S000002706; -.
DR   SGD; S000002706; ATP5.
DR   VEuPathDB; FungiDB:YDR298C; -.
DR   eggNOG; KOG1662; Eukaryota.
DR   HOGENOM; CLU_085114_0_0_1; -.
DR   InParanoid; P09457; -.
DR   OMA; MVDNIQD; -.
DR   OrthoDB; 1262810at2759; -.
DR   BioCyc; YEAST:G3O-29859-MONOMER; -.
DR   Reactome; R-SCE-9837999; Mitochondrial protein degradation.
DR   BioGRID-ORCS; 851892; 6 hits in 10 CRISPR screens.
DR   PRO; PR:P09457; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P09457; protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; IDA:SGD.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:ComplexPortal.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR   FunFam; 1.10.520.20:FF:000002; ATP synthase subunit O, mitochondrial; 1.
DR   Gene3D; 1.10.520.20; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1.
DR   HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR   InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR   InterPro; IPR020781; ATPase_OSCP/d_CS.
DR   InterPro; IPR000711; ATPase_OSCP/dsu.
DR   NCBIfam; TIGR01145; ATP_synt_delta; 1.
DR   PANTHER; PTHR11910; ATP SYNTHASE DELTA CHAIN; 1.
DR   Pfam; PF00213; OSCP; 1.
DR   PRINTS; PR00125; ATPASEDELTA.
DR   SUPFAM; SSF47928; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1.
DR   PROSITE; PS00389; ATPASE_DELTA; 1.
DR   PDBsum; 6B8H; -.
DR   PDBsum; 6CP3; -.
DR   PDBsum; 6CP6; -.
DR   PDBsum; 7TJY; -.
DR   PDBsum; 7TJZ; -.
DR   PDBsum; 7TK0; -.
DR   PDBsum; 7TK1; -.
DR   PDBsum; 7TK2; -.
DR   PDBsum; 7TK3; -.
DR   PDBsum; 7TK4; -.
DR   PDBsum; 7TK5; -.
DR   PDBsum; 7TK6; -.
DR   PDBsum; 7TK7; -.
DR   PDBsum; 7TK8; -.
DR   PDBsum; 7TK9; -.
DR   PDBsum; 7TKA; -.
DR   PDBsum; 7TKB; -.
DR   PDBsum; 7TKC; -.
DR   PDBsum; 7TKD; -.
DR   PDBsum; 7TKE; -.
DR   PDBsum; 7TKF; -.
DR   PDBsum; 7TKG; -.
DR   PDBsum; 7TKH; -.
DR   PDBsum; 7TKI; -.
DR   PDBsum; 7TKJ; -.
DR   PDBsum; 7TKK; -.
DR   PDBsum; 7TKL; -.
DR   PDBsum; 7TKM; -.
DR   PDBsum; 7TKN; -.
DR   PDBsum; 7TKO; -.
DR   PDBsum; 7TKP; -.
DR   PDBsum; 7TKQ; -.
DR   PDBsum; 7TKR; -.
DR   PDBsum; 7TKS; -.
DR   PDBsum; 8F29; -.
DR   PDBsum; 8F39; -.
DR   PDBsum; 8FKJ; -.
DR   PDBsum; 8FL8; -.
PE   1: Evidence at protein level;
KW   3D-structure; ATP synthesis; Hydrogen ion transport; Ion transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transit peptide; Transport.
FT   TRANSIT         1..17
FT                   /note="Mitochondrion"
FT   CHAIN           18..212
FT                   /note="ATP synthase subunit 5, mitochondrial"
FT                   /id="PRO_0000002656"
FT   STRAND          31..33
FT                   /evidence="ECO:0007829|PDB:8F39"
FT   HELIX           35..47
FT                   /evidence="ECO:0007829|PDB:8F39"
FT   HELIX           52..66
FT                   /evidence="ECO:0007829|PDB:8F39"
FT   HELIX           68..71
FT                   /evidence="ECO:0007829|PDB:8F39"
FT   HELIX           81..91
FT                   /evidence="ECO:0007829|PDB:8F39"
FT   TURN            94..96
FT                   /evidence="ECO:0007829|PDB:8F39"
FT   HELIX           102..110
FT                   /evidence="ECO:0007829|PDB:8F39"
FT   HELIX           118..131
FT                   /evidence="ECO:0007829|PDB:8F39"
FT   TURN            152..154
FT                   /evidence="ECO:0007829|PDB:8F39"
FT   HELIX           155..165
FT                   /evidence="ECO:0007829|PDB:8F39"
FT   HELIX           177..188
FT                   /evidence="ECO:0007829|PDB:8F39"
SQ   SEQUENCE   212 AA;  22814 MW;  BD5F8EF4503E4D66 CRC64;
     MFNRVFTRSF ASSLRAAASK AAAPPPVRLF GVEGTYATAL YQAAAKNSSI DAAFQSLQKV
     ESTVKKNPKL GHLLLNPALS LKDRNSVIDA IVETHKNLDG YVVNLLKVLS ENNRLGCFEK
     IASDFGVLND AHNGLLKGTV TSAEPLDPKS FKRIEKALSA SKLVGQGKSL KLENVVKPEI
     KGGLIVELGD KTVDLSISTK IQKLNKVLED SI
//