ATPB_BOVIN
ID ATPB_BOVIN Reviewed; 528 AA.
AC P00829; Q1JQA9; Q9T2U4; Q9T2U5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=ATP synthase subunit beta, mitochondrial {ECO:0000305};
DE EC=7.1.2.2;
DE AltName: Full=ATP synthase F1 subunit beta {ECO:0000250|UniProtKB:P06576};
DE Flags: Precursor;
GN Name=ATP5F1B {ECO:0000250|UniProtKB:P06576}; Synonyms=ATP5B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2458129; DOI=10.1021/bi00411a010;
RA Breen G.A.M., Holmans P.L., Garnett K.E.;
RT "Isolation and characterization of a complementary DNA for the nuclear-
RT coded precursor of the beta-subunit of bovine mitochondrial F1-ATPase.";
RL Biochemistry 27:3955-3961(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 51-528.
RX PubMed=6298222; DOI=10.1016/s0021-9258(18)32833-3;
RA Runswick M.J., Walker J.E.;
RT "The amino acid sequence of the beta-subunit of ATP synthase from bovine
RT heart mitochondria.";
RL J. Biol. Chem. 258:3081-3089(1983).
RN [4]
RP PROTEIN SEQUENCE OF 49-528.
RX PubMed=2864455; DOI=10.1016/0022-2836(85)90313-4;
RA Walker J.E., Fearnley I.M., Gay N.J., Gibson B.W., Northrop F.D.,
RA Powell S.J., Runswick M.J., Saraste M., Tybulewicz V.L.J.;
RT "Primary structure and subunit stoichiometry of F1-ATPase from bovine
RT mitochondria.";
RL J. Mol. Biol. 184:677-701(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 172-528.
RC TISSUE=Heart;
RX PubMed=2896550; DOI=10.1007/bf00434661;
RA Wallace D.C., Ye J., Neckelmann S.N., Singh G., Webster K.A.,
RA Greenberg B.D.;
RT "Sequence analysis of cDNAs for the human and bovine ATP synthase beta
RT subunit: mitochondrial DNA genes sustain seventeen times more mutations.";
RL Curr. Genet. 12:81-90(1987).
RN [6]
RP PROTEIN SEQUENCE OF 47-55.
RC TISSUE=Heart;
RX PubMed=1827992; DOI=10.1021/bi00236a007;
RA Walker J.E., Lutter R., Dupuis A., Runswick M.J.;
RT "Identification of the subunits of F1F0-ATPase from bovine heart
RT mitochondria.";
RL Biochemistry 30:5369-5378(1991).
RN [7]
RP PROTEIN SEQUENCE OF 388-422.
RC TISSUE=Heart;
RX PubMed=1833193; DOI=10.1111/j.1432-1033.1991.tb16246.x;
RA Milgrom Y.M.;
RT "When beef-heart mitochondrial F1-ATPase is inhibited by inhibitor protein
RT a nucleotide is trapped in one of the catalytic sites.";
RL Eur. J. Biochem. 200:789-795(1991).
RN [8]
RP ATP-BINDING SITE.
RX PubMed=6223927; DOI=10.1016/s0021-9258(17)44668-0;
RA Hollemans M., Runswick M.J., Fearnley I.M., Walker J.E.;
RT "The sites of labeling of the beta-subunit of bovine mitochondrial F1-
RT ATPase with 8-azido-ATP.";
RL J. Biol. Chem. 258:9307-9313(1983).
RN [9]
RP PROTEIN SEQUENCE OF N-TERMINUS.
RX PubMed=2898218; DOI=10.1016/0003-2697(88)90277-1;
RA Gibson B.W., Daley D.J., Williams D.H.;
RT "Structural elucidation of N-terminal post-translational modifications by
RT mass spectrometry: application to chicken enolase and the alpha- and beta-
RT subunits of bovine mitochondrial F1-ATPase.";
RL Anal. Biochem. 169:217-226(1988).
RN [10]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=95168; DOI=10.1007/bf02785056;
RA Sikerwar S.S., Malhotra S.K.;
RT "Visualization of mitochondrial coupling factor F1(ATPase) by freeze-
RT drying.";
RL Cell Biophys. 1:55-63(1979).
RN [11]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=14633978; DOI=10.1093/emboj/cdg608;
RA Rubinstein J.L., Walker J.E., Henderson R.;
RT "Structure of the mitochondrial ATP synthase by electron cryomicroscopy.";
RL EMBO J. 22:6182-6192(2003).
RN [12]
RP IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
RX PubMed=17570365; DOI=10.1016/j.febslet.2007.05.079;
RA Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.;
RT "Association of two proteolipids of unknown function with ATP synthase from
RT bovine heart mitochondria.";
RL FEBS Lett. 581:3145-3148(2007).
RN [13]
RP INTERACTION WITH PPIF.
RX PubMed=19801635; DOI=10.1074/jbc.m109.020115;
RA Giorgio V., Bisetto E., Soriano M.E., Dabbeni-Sala F., Basso E.,
RA Petronilli V., Forte M.A., Bernardi P., Lippe G.;
RT "Cyclophilin D modulates mitochondrial F0F1-ATP synthase by interacting
RT with the lateral stalk of the complex.";
RL J. Biol. Chem. 284:33982-33988(2009).
RN [14]
RP FUNCTION, IDENTIFICATION IN THE ATP SYNTHASE COMPLEX, SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=23407638; DOI=10.1098/rsob.120160;
RA Runswick M.J., Bason J.V., Montgomery M.G., Robinson G.C., Fearnley I.M.,
RA Walker J.E.;
RT "The affinity purification and characterization of ATP synthase complexes
RT from mitochondria.";
RL Open Biol. 3:120160-120160(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=25851905; DOI=10.1074/jbc.m115.645283;
RA Lee J., Ding S., Walpole T.B., Holding A.N., Montgomery M.G.,
RA Fearnley I.M., Walker J.E.;
RT "Organization of Subunits in the Membrane Domain of the Bovine F-ATPase
RT Revealed by Covalent Cross-linking.";
RL J. Biol. Chem. 290:13308-13320(2015).
RN [16] {ECO:0007744|PDB:1BMF}
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 47-528 IN COMPLEX WITH ATP
RP ANALOG, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=8065448; DOI=10.1038/370621a0;
RA Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E.;
RT "Structure at 2.8-A resolution of F1-ATPase from bovine heart
RT mitochondria.";
RL Nature 370:621-628(1994).
RN [17] {ECO:0007744|PDB:1EFR}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 47-528 IN COMPLEX WITH ATP
RP ANALOG, AND SUBUNIT.
RX PubMed=8790345; DOI=10.1073/pnas.93.18.9420;
RA Abrahams J.P., Buchanan S.K., van Raaij M.J., Fearnley I.M., Leslie A.G.,
RA Walker J.E.;
RT "The structure of bovine F1-ATPase complexed with the peptide antibiotic
RT efrapeptin.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9420-9424(1996).
RN [18] {ECO:0007744|PDB:1NBM}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 47-526 IN COMPLEX WITH ADP AND
RP ATP, FUNCTION, AND SUBUNIT.
RX PubMed=9687365; DOI=10.1016/s0969-2126(98)00085-9;
RA Orriss G.L., Leslie A.G., Braig K., Walker J.E.;
RT "Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan:
RT the structure provides further support for a rotary catalytic mechanism.";
RL Structure 6:831-837(1998).
RN [19] {ECO:0007744|PDB:1OHH}
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 47-528 IN COMPLEX WITH ATP ANALOG;
RP ATPIF1; ATP5F1A AND ATP5F1C, AND SUBUNIT.
RX PubMed=12923572; DOI=10.1038/nsb966;
RA Cabezon E., Montgomery M.G., Leslie A.G., Walker J.E.;
RT "The structure of bovine F1-ATPase in complex with its regulatory protein
RT IF1.";
RL Nat. Struct. Biol. 10:744-750(2003).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 47-528 IN COMPLEX WITH ATPIF1;
RP ATP5F1A; ATP5F1C; ATP5F1D AND ATP5F1E, AND SUBUNIT.
RX PubMed=17895376; DOI=10.1073/pnas.0707326104;
RA Gledhill J.R., Montgomery M.G., Leslie A.G., Walker J.E.;
RT "How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine
RT mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15671-15676(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
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 {ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:9687365}.
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. Component of an ATP synthase complex composed of
CC ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC ATP5MJ (PubMed:17570365, PubMed:12923572, PubMed:17895376,
CC PubMed:25851905). Interacts with PPIF (PubMed:19801635). Interacts with
CC BCL2L1 isoform BCL-X(L); the interaction mediates the association of
CC BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F(1)F(0) ATP
CC synthase and enhances neurons metabolic efficiency. Interacts with CLN5
CC and PPT1 (By similarity). Interacts with S100A1; this interaction
CC increases F1-ATPase activity (By similarity). Interacts with MTLN (By
CC similarity). Interacts with TTC5/STRAP; the interaction results in
CC decreased mitochondrial ATP production (By similarity).
CC {ECO:0000250|UniProtKB:P06576, ECO:0000250|UniProtKB:P10719,
CC ECO:0000250|UniProtKB:P56480, ECO:0000269|PubMed:12923572,
CC ECO:0000269|PubMed:17570365, ECO:0000269|PubMed:17895376,
CC ECO:0000269|PubMed:19801635, ECO:0000269|PubMed:23407638,
CC ECO:0000269|PubMed:25851905, ECO:0000269|PubMed:8065448,
CC ECO:0000269|PubMed:8790345, ECO:0000269|PubMed:9687365}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:23407638,
CC ECO:0000269|PubMed:2864455, ECO:0000269|PubMed:8065448,
CC ECO:0000269|PubMed:95168}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:23407638,
CC ECO:0000269|PubMed:2864455, ECO:0000269|PubMed:8065448,
CC ECO:0000269|PubMed:95168}; Matrix side {ECO:0000269|PubMed:14633978,
CC ECO:0000269|PubMed:95168}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; M20929; AAA30395.1; -; mRNA.
DR EMBL; BC116099; AAI16100.1; -; mRNA.
DR EMBL; X05605; CAA29094.1; -; mRNA.
DR PIR; A28717; PWBOB.
DR RefSeq; NP_786990.1; NM_175796.3.
DR PDB; 1BMF; X-ray; 2.85 A; D/E/F=47-528.
DR PDB; 1COW; X-ray; 3.10 A; D/E/F=47-528.
DR PDB; 1E1Q; X-ray; 2.61 A; D/E/F=47-528.
DR PDB; 1E1R; X-ray; 2.50 A; D/E/F=47-528.
DR PDB; 1E79; X-ray; 2.40 A; D/E/F=47-528.
DR PDB; 1EFR; X-ray; 3.10 A; D/E/F=47-528.
DR PDB; 1H8E; X-ray; 2.00 A; D/E/F=47-528.
DR PDB; 1H8H; X-ray; 2.90 A; D/E/F=47-528.
DR PDB; 1NBM; X-ray; 3.00 A; D/E/F=47-526.
DR PDB; 1OHH; X-ray; 2.80 A; D/E/F=47-528.
DR PDB; 1QO1; X-ray; 3.90 A; D/E/F=47-525.
DR PDB; 1W0J; X-ray; 2.20 A; D/E/F=47-528.
DR PDB; 1W0K; X-ray; 2.85 A; D/E/F=47-528.
DR PDB; 2CK3; X-ray; 1.90 A; D/E/F=47-528.
DR PDB; 2JDI; X-ray; 1.90 A; D/E/F=47-528.
DR PDB; 2JIZ; X-ray; 2.30 A; D/E/F/K/L/M=47-528.
DR PDB; 2JJ1; X-ray; 2.70 A; D/E/F/K/L/M=47-528.
DR PDB; 2JJ2; X-ray; 2.40 A; D/E/F/K/L/M=47-528.
DR PDB; 2V7Q; X-ray; 2.10 A; D/E/F=47-528.
DR PDB; 2W6E; X-ray; 6.50 A; D/E/F=1-528.
DR PDB; 2W6F; X-ray; 6.00 A; D/E/F=1-528.
DR PDB; 2W6G; X-ray; 6.00 A; D/E/F=1-528.
DR PDB; 2W6H; X-ray; 5.00 A; D/E/F=1-528.
DR PDB; 2W6I; X-ray; 4.00 A; D/E/F=1-528.
DR PDB; 2W6J; X-ray; 3.84 A; D/E/F=1-528.
DR PDB; 2WSS; X-ray; 3.20 A; D/E/F/M/N/O=47-528.
DR PDB; 2XND; X-ray; 3.50 A; D/E/F=59-525.
DR PDB; 4ASU; X-ray; 2.60 A; D/E/F=49-528.
DR PDB; 4TSF; X-ray; 3.20 A; D/E/F=49-528.
DR PDB; 4TT3; X-ray; 3.21 A; D/E/F=49-528.
DR PDB; 4YXW; X-ray; 3.10 A; D/E/F=47-528.
DR PDB; 4Z1M; X-ray; 3.30 A; D/E/F=47-528.
DR PDB; 5ARA; EM; 6.70 A; D/E/F=47-528.
DR PDB; 5ARE; EM; 7.40 A; D/E/F=47-528.
DR PDB; 5ARH; EM; 7.20 A; D/E/F=47-528.
DR PDB; 5ARI; EM; 7.40 A; D/E/F=47-528.
DR PDB; 5FIJ; EM; 7.40 A; D/E/F=47-528.
DR PDB; 5FIK; EM; 6.40 A; D/E/F=47-528.
DR PDB; 5FIL; EM; 7.10 A; D/E/F=47-528.
DR PDB; 6YY0; EM; 3.23 A; D/E/F=47-528.
DR PDB; 6Z1R; EM; 3.29 A; D/E/F=47-528.
DR PDB; 6Z1U; EM; 3.47 A; D/E/F=47-528.
DR PDB; 6ZPO; EM; 4.00 A; D/E/F=47-528.
DR PDB; 6ZQM; EM; 3.29 A; D/E/F=47-528.
DR PDB; 6ZQN; EM; 4.00 A; D/E/F=47-528.
DR PDB; 7AJB; EM; 9.20 A; AD/AE/AF/D/E/F=47-528.
DR PDB; 7AJC; EM; 11.90 A; AD/AE/AF/D/E/F=47-528.
DR PDB; 7AJD; EM; 9.00 A; AD/AE/AF/D/E/F=47-528.
DR PDB; 7AJE; EM; 9.40 A; AD/AE/AF/D/E/F=47-528.
DR PDB; 7AJF; EM; 8.45 A; AD/AE/AF/D/E/F=47-528.
DR PDB; 7AJG; EM; 10.70 A; AD/AE/AF/D/E/F=47-528.
DR PDB; 7AJH; EM; 9.70 A; AD/AE/AF/D/E/F=47-528.
DR PDB; 7AJI; EM; 11.40 A; AD/AE/AF/D/E/F=47-528.
DR PDB; 7AJJ; EM; 13.10 A; AD/AE/AF/D/E/F=47-528.
DR PDBsum; 1BMF; -.
DR PDBsum; 1COW; -.
DR PDBsum; 1E1Q; -.
DR PDBsum; 1E1R; -.
DR PDBsum; 1E79; -.
DR PDBsum; 1EFR; -.
DR PDBsum; 1H8E; -.
DR PDBsum; 1H8H; -.
DR PDBsum; 1NBM; -.
DR PDBsum; 1OHH; -.
DR PDBsum; 1QO1; -.
DR PDBsum; 1W0J; -.
DR PDBsum; 1W0K; -.
DR PDBsum; 2CK3; -.
DR PDBsum; 2JDI; -.
DR PDBsum; 2JIZ; -.
DR PDBsum; 2JJ1; -.
DR PDBsum; 2JJ2; -.
DR PDBsum; 2V7Q; -.
DR PDBsum; 2W6E; -.
DR PDBsum; 2W6F; -.
DR PDBsum; 2W6G; -.
DR PDBsum; 2W6H; -.
DR PDBsum; 2W6I; -.
DR PDBsum; 2W6J; -.
DR PDBsum; 2WSS; -.
DR PDBsum; 2XND; -.
DR PDBsum; 4ASU; -.
DR PDBsum; 4TSF; -.
DR PDBsum; 4TT3; -.
DR PDBsum; 4YXW; -.
DR PDBsum; 4Z1M; -.
DR PDBsum; 5ARA; -.
DR PDBsum; 5ARE; -.
DR PDBsum; 5ARH; -.
DR PDBsum; 5ARI; -.
DR PDBsum; 5FIJ; -.
DR PDBsum; 5FIK; -.
DR PDBsum; 5FIL; -.
DR PDBsum; 6YY0; -.
DR PDBsum; 6Z1R; -.
DR PDBsum; 6Z1U; -.
DR PDBsum; 6ZPO; -.
DR PDBsum; 6ZQM; -.
DR PDBsum; 6ZQN; -.
DR PDBsum; 7AJB; -.
DR PDBsum; 7AJC; -.
DR PDBsum; 7AJD; -.
DR PDBsum; 7AJE; -.
DR PDBsum; 7AJF; -.
DR PDBsum; 7AJG; -.
DR PDBsum; 7AJH; -.
DR PDBsum; 7AJI; -.
DR PDBsum; 7AJJ; -.
DR AlphaFoldDB; P00829; -.
DR SMR; P00829; -.
DR CORUM; P00829; -.
DR DIP; DIP-35476N; -.
DR IntAct; P00829; 10.
DR MINT; P00829; -.
DR STRING; 9913.ENSBTAP00000017710; -.
DR BindingDB; P00829; -.
DR ChEMBL; CHEMBL612444; -.
DR PaxDb; P00829; -.
DR PeptideAtlas; P00829; -.
DR PRIDE; P00829; -.
DR GeneID; 327675; -.
DR KEGG; bta:327675; -.
DR CTD; 506; -.
DR eggNOG; KOG1350; Eukaryota.
DR HOGENOM; CLU_022398_0_2_1; -.
DR InParanoid; P00829; -.
DR OrthoDB; 495235at2759; -.
DR TreeFam; TF105640; -.
DR EvolutionaryTrace; P00829; -.
DR PRO; PR:P00829; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:UniProtKB.
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; IEA:UniProtKB-EC.
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; Acetylation; ATP synthesis; ATP-binding; CF(1);
KW Direct protein sequencing; Glycoprotein; Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transit peptide;
KW Translocase; Transport.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1827992"
FT CHAIN 47..528
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000002442"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12923572,
FT ECO:0000269|PubMed:8065448, ECO:0000269|PubMed:8790345,
FT ECO:0000269|PubMed:9687365, ECO:0007744|PDB:1BMF,
FT ECO:0007744|PDB:1COW, ECO:0007744|PDB:1E1Q,
FT ECO:0007744|PDB:1E1R, ECO:0007744|PDB:1E79,
FT ECO:0007744|PDB:1EFR, ECO:0007744|PDB:1H8E,
FT ECO:0007744|PDB:1H8H, ECO:0007744|PDB:1NBM,
FT ECO:0007744|PDB:1W0J, ECO:0007744|PDB:1W0K,
FT ECO:0007744|PDB:2CK3, ECO:0007744|PDB:2JIZ,
FT ECO:0007744|PDB:2JJ1, ECO:0007744|PDB:2JJ2,
FT ECO:0007744|PDB:2V7Q, ECO:0007744|PDB:2W6E,
FT ECO:0007744|PDB:2WSS, ECO:0007744|PDB:4ASU,
FT ECO:0007744|PDB:4TSF, ECO:0007744|PDB:4TT3,
FT ECO:0007744|PDB:4Z1M"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12923572,
FT ECO:0000269|PubMed:8065448, ECO:0000269|PubMed:8790345,
FT ECO:0000269|PubMed:9687365, ECO:0007744|PDB:1BMF,
FT ECO:0007744|PDB:1COW, ECO:0007744|PDB:1E1R,
FT ECO:0007744|PDB:1EFR, ECO:0007744|PDB:1H8H,
FT ECO:0007744|PDB:1NBM, ECO:0007744|PDB:1OHH,
FT ECO:0007744|PDB:2CK3, ECO:0007744|PDB:2JDI,
FT ECO:0007744|PDB:2JIZ, ECO:0007744|PDB:2JJ1,
FT ECO:0007744|PDB:2JJ2, ECO:0007744|PDB:2WSS,
FT ECO:0007744|PDB:2XND, ECO:0007744|PDB:4YXW"
FT MOD_RES 124
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 124
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 161
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 161
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 198
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06576"
FT MOD_RES 259
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 259
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 264
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 264
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06576"
FT MOD_RES 426
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06576"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10719"
FT MOD_RES 480
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 485
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 522
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 522
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT CARBOHYD 106
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VARIANT 49..50
FT /note="Missing (in some mature chains)"
FT CONFLICT 182
FT /note="I -> L (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="I -> D (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="Y -> I (in Ref. 5; CAA29094)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="L -> F (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="E -> Q (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="D -> N (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="T -> V (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="D -> N (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:4Z1M"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:1W0K"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 228..238
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 276..295
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 335..343
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 353..361
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 370..375
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:1W0K"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:1W0K"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:1W0K"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 415..441
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 450..463
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 472..475
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 484..496
FT /evidence="ECO:0007829|PDB:1W0K"
FT TURN 497..501
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:1W0K"
FT HELIX 513..522
FT /evidence="ECO:0007829|PDB:1W0K"
SQ SEQUENCE 528 AA; 56284 MW; 32218D14A5497F18 CRC64;
MLGLVGRVVA ASASGALRGL SPSAPLPQAQ LLLRAAPAAL QPARDYAAQA SPSPKAGATT
GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA QHLGESTVRT IAMDGTEGLV
RGQKVLDSGA PIRIPVGPET LGRIMNVIGE PIDERGPIKT KQFAAIHAEA PEFVEMSVEQ
EILVTGIKVV DLLAPYAKGG KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT
REGNDLYHEM IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD
VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK KGSITSVQAI
YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP LDSTSRIMDP NIVGSEHYDV
ARGVQKILQD YKSLQDIIAI LGMDELSEED KLTVSRARKI QRFLSQPFQV AEVFTGHLGK
LVPLKETIKG FQQILAGEYD HLPEQAFYMV GPIEEAVAKA DKLAEEHS
