ATPB_YEAST
ID ATPB_YEAST Reviewed; 511 AA.
AC P00830; D6VWU0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=ATP synthase subunit beta, mitochondrial;
DE EC=7.1.2.2;
DE Flags: Precursor;
GN Name=ATP2; OrderedLocusNames=YJR121W; ORFNames=J2041;
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].
RX PubMed=2866186; DOI=10.1016/s0021-9258(17)36276-2;
RA Takeda M., Vassarotti A., Douglas M.G.;
RT "Nuclear genes coding the yeast mitochondrial adenosine triphosphatase
RT complex. Primary sequence analysis of ATP2 encoding the F1-ATPase beta-
RT subunit precursor.";
RL J. Biol. Chem. 260:15458-15465(1985).
RN [2]
RP ERRATUM OF PUBMED:2866186.
RA Takeda M., Vassarotti A., Douglas M.G.;
RL J. Biol. Chem. 261:10466-10466(1986).
RN [3]
RP SEQUENCE REVISION.
RA Takeda M.;
RL Submitted (JUL-1986) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24657 / D273-10B;
RX PubMed=8900121; DOI=10.1074/jbc.271.43.26522;
RA Liang Y., Ackerman S.H.;
RT "Characterization of mutations in the beta subunit of the mitochondrial F1-
RT ATPase that produce defects in enzyme catalysis and assembly.";
RL J. Biol. Chem. 271:26522-26528(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
RX PubMed=2138017; DOI=10.1042/bj2660227;
RA Walker M.E., Valentin E., Reid G.A.;
RT "Transport of the yeast ATP synthase beta-subunit into mitochondria.
RT Effects of amino acid substitutions on targeting.";
RL Biochem. J. 266:227-234(1990).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-507.
RX PubMed=6225776; DOI=10.1016/s0021-9258(17)44249-9;
RA Saltzgaber-Muller J., Kunapuli S.P., Douglas M.G.;
RT "Nuclear genes coding the yeast mitochondrial adenosine triphosphatase
RT complex. Isolation of ATP2 coding the F1-ATPase beta subunit.";
RL J. Biol. Chem. 258:11465-11470(1983).
RN [9]
RP PROTEIN SEQUENCE OF 371-379 AND 390-398.
RC STRAIN=ATCC 38531 / Y41;
RX PubMed=8935650; DOI=10.1111/j.1574-6968.1996.tb08073.x;
RA Norbeck J., Blomberg A.;
RT "Protein expression during exponential growth in 0.7 M NaCl medium of
RT Saccharomyces cerevisiae.";
RL FEMS Microbiol. Lett. 137:1-8(1996).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-112; THR-237 AND SER-373, AND
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 [12]
RP 3D-STRUCTURE MODELING.
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 synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Subunits alpha and
CC beta form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC ATP in three separate catalytic sites on the beta subunits.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
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 -!- INTERACTION:
CC P00830; Q02888: INA17; NbExp=2; IntAct=EBI-3242, EBI-7668387;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC Note=Peripheral membrane protein.
CC -!- MISCELLANEOUS: Present with 164000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; M12082; AAA34444.1; -; Genomic_DNA.
DR EMBL; U46215; AAC49475.1; -; Genomic_DNA.
DR EMBL; Z49621; CAA89652.1; -; Genomic_DNA.
DR EMBL; X52004; CAA36255.1; -; Genomic_DNA.
DR EMBL; K00560; AAA34443.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08906.1; -; Genomic_DNA.
DR PIR; S57144; PWBYB.
DR RefSeq; NP_012655.3; NM_001181779.3.
DR PDB; 2HLD; X-ray; 2.80 A; D/E/F/M/N/O/V/W/X=34-511.
DR PDB; 2WPD; X-ray; 3.43 A; D/E/F=34-511.
DR PDB; 2XOK; X-ray; 3.01 A; D/E/F=1-507.
DR PDB; 3FKS; X-ray; 3.59 A; D/E/F/M/N/O/V/W/X=36-511.
DR PDB; 3OE7; X-ray; 3.19 A; D/E/F/M/N/O/V/W/X=36-511.
DR PDB; 3OEE; X-ray; 2.74 A; D/E/F/M/N/O/V/W/X=36-511.
DR PDB; 3OEH; X-ray; 3.00 A; D/E/F/M/N/O/V/W/X=36-511.
DR PDB; 3OFN; X-ray; 3.20 A; D/E/F/M/N/O/V/W/X=36-511.
DR PDB; 3ZIA; X-ray; 2.50 A; D/E/F/N/O/P=34-511.
DR PDB; 3ZRY; X-ray; 6.50 A; D/E/F=34-511.
DR PDB; 4B2Q; EM; 37.00 A; D/d=39-508, E/F/e/f=39-511.
DR PDB; 6B8H; EM; 3.60 A; D/E/F/Y/Z/c=34-511.
DR PDB; 6CP3; EM; 3.80 A; D/E/F=34-511.
DR PDB; 6CP6; EM; 3.60 A; D/E/F=34-511.
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 AlphaFoldDB; P00830; -.
DR SMR; P00830; -.
DR BioGRID; 33877; 232.
DR ComplexPortal; CPX-3281; Mitochondrial proton-transporting ATP synthase complex.
DR DIP; DIP-3028N; -.
DR IntAct; P00830; 177.
DR MINT; P00830; -.
DR STRING; 4932.YJR121W; -.
DR BindingDB; P00830; -.
DR ChEMBL; CHEMBL1075103; -.
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; P00830; -.
DR SWISS-2DPAGE; P00830; -.
DR MaxQB; P00830; -.
DR PaxDb; P00830; -.
DR PRIDE; P00830; -.
DR EnsemblFungi; YJR121W_mRNA; YJR121W; YJR121W.
DR GeneID; 853585; -.
DR KEGG; sce:YJR121W; -.
DR SGD; S000003882; ATP2.
DR VEuPathDB; FungiDB:YJR121W; -.
DR eggNOG; KOG1350; Eukaryota.
DR GeneTree; ENSGT00550000074800; -.
DR HOGENOM; CLU_022398_0_2_1; -.
DR InParanoid; P00830; -.
DR OMA; GFNMIMD; -.
DR BioCyc; YEAST:G3O-31742-MON; -.
DR BRENDA; 7.1.2.2; 984.
DR Reactome; R-SCE-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-SCE-8949613; Cristae formation.
DR ChiTaRS; ATP2; yeast.
DR EvolutionaryTrace; P00830; -.
DR PRO; PR:P00830; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P00830; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
DR GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IMP:SGD.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:SGD.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01039; atpD; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; ATP-binding; CF(1); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transit peptide; Translocase; Transport.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT CHAIN 34..511
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000002454"
FT BINDING 190..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT CONFLICT 201
FT /note="Q -> M (in Ref. 8; AAA34443)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="T -> A (in Ref. 1; AAA34444 and 8; AAA34443)"
FT /evidence="ECO:0000305"
FT CONFLICT 232..237
FT /note="REMKET -> HEMEDS (in Ref. 8; AAA34443)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="G -> E (in Ref. 8; AAA34443)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..288
FT /note="FI -> Y (in Ref. 8; AAA34443)"
FT /evidence="ECO:0000305"
FT CONFLICT 354..358
FT /note="APATT -> SPSTS (in Ref. 1; AAA34444)"
FT /evidence="ECO:0000305"
FT CONFLICT 365..366
FT /note="TT -> SS (in Ref. 1; AAA34444 and 8; AAA34443)"
FT /evidence="ECO:0000305"
FT CONFLICT 469..473
FT /note="DTVAS -> RTRCL (in Ref. 8; AAA34443)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="A -> R (in Ref. 8; AAA34443)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="A -> R (in Ref. 1; AAA34444)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="A -> R (in Ref. 1; AAA34444)"
FT /evidence="ECO:0000305"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2XOK"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2HLD"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:2WPD"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3OEE"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:3OEH"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:2WPD"
FT HELIX 196..207
FT /evidence="ECO:0007829|PDB:3ZIA"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:3OEE"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 224..235
FT /evidence="ECO:0007829|PDB:3ZIA"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:3OFN"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 259..278
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 292..302
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 318..326
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:3OEE"
FT STRAND 335..344
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:3ZIA"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 370..374
FT /evidence="ECO:0007829|PDB:3ZIA"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 393..396
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 398..423
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:2HLD"
FT HELIX 431..446
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 455..458
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 467..479
FT /evidence="ECO:0007829|PDB:3ZIA"
FT TURN 480..484
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:3ZIA"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:3ZIA"
FT HELIX 496..507
FT /evidence="ECO:0007829|PDB:3ZIA"
SQ SEQUENCE 511 AA; 54794 MW; EDFF256826F68F0C CRC64;
MVLPRLYTAT SRAAFKAAKQ SAPLLSTSWK RCMASAAQST PITGKVTAVI GAIVDVHFEQ
SELPAILNAL EIKTPQGKLV LEVAQHLGEN TVRTIAMDGT EGLVRGEKVL DTGGPISVPV
GRETLGRIIN VIGEPIDERG PIKSKLRKPI HADPPSFAEQ STSAEILETG IKVVDLLAPY
ARGGKIGLFG GAGVGKTVFI QELINNIAKA HGGFSVFTGV GERTREGNDL YREMKETGVI
NLEGESKVAL VFGQMNEPPG ARARVALTGL TIAEYFRDEE GQDVLLFIDN IFRFTQAGSE
VSALLGRIPS AVGYQPTLAT DMGLLQERIT TTKKGSVTSV QAVYVPADDL TDPAPATTFA
HLDATTVLSR GISELGIYPA VDPLDSKSRL LDAAVVGQEH YDVASKVQET LQTYKSLQDI
IAILGMDELS EQDKLTVERA RKIQRFLSQP FAVAEVFTGI PGKLVRLKDT VASFKAVLEG
KYDNIPEHAF YMVGGIEDVV AKAEKLAAEA N
