ID   ATPD_YEAST              Reviewed;         160 AA.
AC   Q12165; D6VRY4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=ATP synthase subunit delta, mitochondrial;
DE   AltName: Full=F-ATPase delta subunit;
DE   Flags: Precursor;
GN   Name=ATP16; OrderedLocusNames=YDL004W; ORFNames=D2935, YD8119.03;
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], AND PROTEIN SEQUENCE OF 23-72; 112-121
RP   AND 141-160.
RC   STRAIN=D273-10B/A;
RX   PubMed=8026496; DOI=10.1111/j.1432-1033.1994.tb18932.x;
RA   Giraud M.-F., Velours J.;
RT   "ATP synthase of yeast mitochondria. Isolation of the F1 delta subunit,
RT   sequence and disruption of the structural gene.";
RL   Eur. J. Biochem. 222:851-859(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
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   [3]
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   [4]
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   [5]
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).
RN   [6]
RP   3D-STRUCTURE MODELING, FUNCTION, IDENTIFICATION IN THE F-TYPE ATPASE
RP   COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=10576729; DOI=10.1126/science.286.5445.1700;
RA   Stock D., Leslie A.G., Walker J.E.;
RT   "Molecular architecture of the rotary motor in ATP synthase.";
RL   Science 286:1700-1705(1999).
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
CC       F(0) - containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP turnover in
CC       the 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(1) domain and of the central stalk which is part of the complex
CC       rotary element. Rotation of the central stalk against the surrounding
CC       alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate
CC       catalytic sites on the beta subunits. {ECO:0000269|PubMed:10576729}.
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. {ECO:0000269|PubMed:10576729}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:10576729}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z21857; CAA79912.1; -; Genomic_DNA.
DR   EMBL; Z48008; CAA88057.1; -; Genomic_DNA.
DR   EMBL; Z48432; CAA88355.1; -; Genomic_DNA.
DR   EMBL; Z74052; CAA98560.1; -; Genomic_DNA.
DR   EMBL; AY558155; AAS56481.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11844.1; -; Genomic_DNA.
DR   PIR; S45632; S45632.
DR   RefSeq; NP_010280.1; NM_001180063.1.
DR   PDB; 2HLD; X-ray; 2.80 A; H/Q/Z=23-160.
DR   PDB; 2WPD; X-ray; 3.43 A; H=23-160.
DR   PDB; 2XOK; X-ray; 3.01 A; H=1-160.
DR   PDB; 3FKS; X-ray; 3.59 A; H/Q/Z=23-160.
DR   PDB; 3OE7; X-ray; 3.19 A; H/Q/Z=24-160.
DR   PDB; 3OEE; X-ray; 2.74 A; H/Q/Z=23-160.
DR   PDB; 3OEH; X-ray; 3.00 A; H/Q/Z=23-160.
DR   PDB; 3OFN; X-ray; 3.20 A; H/Q=23-160.
DR   PDB; 3ZIA; X-ray; 2.50 A; H/R=23-160.
DR   PDB; 3ZRY; X-ray; 6.50 A; H=23-160.
DR   PDB; 4B2Q; EM; 37.00 A; H/h=29-160.
DR   PDB; 6B8H; EM; 3.60 A; H/l=23-160.
DR   PDB; 6CP3; EM; 3.80 A; H=23-160.
DR   PDB; 6CP6; EM; 3.60 A; H=23-160.
DR   PDB; 7TJY; EM; 3.80 A; H=23-160.
DR   PDB; 7TJZ; EM; 4.40 A; H=23-160.
DR   PDB; 7TK0; EM; 4.40 A; H=23-160.
DR   PDB; 7TK1; EM; 7.10 A; H=23-160.
DR   PDB; 7TK2; EM; 6.50 A; H=23-160.
DR   PDB; 7TK3; EM; 6.30 A; H=23-160.
DR   PDB; 7TK4; EM; 7.00 A; H=23-160.
DR   PDB; 7TK5; EM; 7.80 A; H=23-160.
DR   PDB; 7TK6; EM; 6.50 A; H=23-160.
DR   PDB; 7TK7; EM; 6.70 A; H=23-160.
DR   PDB; 7TK8; EM; 4.70 A; H=23-160.
DR   PDB; 7TK9; EM; 6.00 A; H=23-160.
DR   PDB; 7TKA; EM; 7.10 A; H=23-160.
DR   PDB; 7TKB; EM; 6.30 A; H=23-160.
DR   PDB; 7TKC; EM; 5.80 A; H=23-160.
DR   PDB; 7TKD; EM; 7.70 A; H=23-160.
DR   PDB; 7TKE; EM; 7.10 A; H=23-160.
DR   PDB; 7TKF; EM; 7.10 A; H=23-160.
DR   PDB; 7TKG; EM; 4.50 A; H=23-160.
DR   PDB; 7TKH; EM; 4.40 A; H=23-160.
DR   PDB; 7TKI; EM; 7.10 A; H=23-160.
DR   PDB; 7TKJ; EM; 7.50 A; H=23-160.
DR   PDB; 7TKK; EM; 7.30 A; H=23-160.
DR   PDB; 7TKL; EM; 6.40 A; H=23-160.
DR   PDB; 7TKM; EM; 4.50 A; H=23-160.
DR   PDB; 7TKN; EM; 7.10 A; H=23-160.
DR   PDB; 7TKO; EM; 4.80 A; H=23-160.
DR   PDB; 7TKP; EM; 4.60 A; H=23-160.
DR   PDB; 7TKQ; EM; 4.50 A; H=23-160.
DR   PDB; 7TKR; EM; 6.50 A; H=23-160.
DR   PDB; 7TKS; EM; 7.50 A; H=23-160.
DR   PDBsum; 2HLD; -.
DR   PDBsum; 2WPD; -.
DR   PDBsum; 2XOK; -.
DR   PDBsum; 3FKS; -.
DR   PDBsum; 3OE7; -.
DR   PDBsum; 3OEE; -.
DR   PDBsum; 3OEH; -.
DR   PDBsum; 3OFN; -.
DR   PDBsum; 3ZIA; -.
DR   PDBsum; 3ZRY; -.
DR   PDBsum; 4B2Q; -.
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   AlphaFoldDB; Q12165; -.
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-7546; -.
DR   EMDB; EMD-7548; -.
DR   SMR; Q12165; -.
DR   BioGRID; 32050; 29.
DR   ComplexPortal; CPX-3281; Mitochondrial proton-transporting ATP synthase complex.
DR   DIP; DIP-3032N; -.
DR   IntAct; Q12165; 6.
DR   MINT; Q12165; -.
DR   STRING; 4932.YDL004W; -.
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; Q12165; -.
DR   MaxQB; Q12165; -.
DR   PaxDb; 4932-YDL004W; -.
DR   PeptideAtlas; Q12165; -.
DR   EnsemblFungi; YDL004W_mRNA; YDL004W; YDL004W.
DR   GeneID; 851560; -.
DR   KEGG; sce:YDL004W; -.
DR   AGR; SGD:S000002162; -.
DR   SGD; S000002162; ATP16.
DR   VEuPathDB; FungiDB:YDL004W; -.
DR   eggNOG; KOG1758; Eukaryota.
DR   GeneTree; ENSGT00390000017576; -.
DR   HOGENOM; CLU_084338_0_0_1; -.
DR   InParanoid; Q12165; -.
DR   OMA; HQTLYSE; -.
DR   OrthoDB; 5394300at2759; -.
DR   BioCyc; YEAST:G3O-29435-MONOMER; -.
DR   BioGRID-ORCS; 851560; 6 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; Q12165; -.
DR   PRO; PR:Q12165; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q12165; Protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; NAS:ComplexPortal.
DR   GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IBA:GO_Central.
DR   GO; GO:0005756; C:mitochondrial proton-transporting ATP synthase, central stalk; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA: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:SGD.
DR   CDD; cd12152; F1-ATPase_delta; 1.
DR   Gene3D; 6.10.140.880; -; 1.
DR   Gene3D; 2.60.15.10; F0F1 ATP synthase delta/epsilon subunit, N-terminal; 1.
DR   HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
DR   InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR   InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR   InterPro; IPR048938; ATPD_C_fung.
DR   InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR   PANTHER; PTHR13822; ATP SYNTHASE DELTA/EPSILON CHAIN; 1.
DR   PANTHER; PTHR13822:SF7; ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL; 1.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   Pfam; PF21334; ATPD_C_fung; 1.
DR   SUPFAM; SSF51344; Epsilon subunit of F1F0-ATP synthase N-terminal domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP synthesis; CF(1); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW   Transport.
FT   TRANSIT         1..22
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:8026496"
FT   CHAIN           23..160
FT                   /note="ATP synthase subunit delta, mitochondrial"
FT                   /id="PRO_0000002671"
FT   STRAND          34..37
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:3OFN"
FT   STRAND          51..54
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   STRAND          56..59
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   STRAND          70..74
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   STRAND          78..83
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   STRAND          86..92
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   STRAND          95..100
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   TURN            101..103
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   STRAND          104..110
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:3OFN"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   HELIX           120..133
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   STRAND          136..139
FT                   /evidence="ECO:0007829|PDB:3ZIA"
FT   HELIX           140..156
FT                   /evidence="ECO:0007829|PDB:3ZIA"
SQ   SEQUENCE   160 AA;  17020 MW;  AE8D0BA364107977 CRC64;
     MLRSIIGKSA SRSLNFVAKR SYAEAAAASS GLKLQFALPH ETLYSGSEVT QVNLPAKSGR
     IGVLANHVPT VEQLLPGVVE VMEGSNSKKF FISGGFATVQ PDSQLCVTAI EAFPLESFSQ
     ENIKNLLAEA KKNVSSSDAR EAAEAAIQVE VLENLQSVLK
//