ATPB_ECOLI
ID ATPB_ECOLI Reviewed; 460 AA.
AC P0ABB4; P00824; Q2M850;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=ATP synthase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
GN Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347}; Synonyms=papB, uncD;
GN OrderedLocusNames=b3732, JW3710;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6395859; DOI=10.1042/bj2240799;
RA Walker J.E., Gay N.J., Saraste M., Eberle A.N.;
RT "DNA sequence around the Escherichia coli unc operon. Completion of the
RT sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and
RT phoS.";
RL Biochem. J. 224:799-815(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6272217; DOI=10.1093/nar/9.20.5287;
RA Saraste M., Gay N.J., Eberle A., Runswick M.J., Walker J.E.;
RT "The atp operon: nucleotide sequence of the genes for the gamma, beta, and
RT epsilon subunits of Escherichia coli ATP synthase.";
RL Nucleic Acids Res. 9:5287-5296(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6301339; DOI=10.1111/j.1749-6632.1982.tb25731.x;
RA Kanazawa H., Futai M.;
RT "Structure and function of H+-ATPase: what we have learned from Escherichia
RT coli H+-ATPase.";
RL Ann. N. Y. Acad. Sci. 402:45-64(1982).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6285901; DOI=10.1016/0006-291x(82)90922-6;
RA Kanazawa H., Kayano T., Kiyasu T., Futai M.;
RT "Nucleotide sequence of the genes for beta and epsilon subunits of proton-
RT translocating ATPase from Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 105:1257-1264(1982).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RX PubMed=6277310; DOI=10.1016/0006-291x(81)90494-0;
RA Kanazawa H., Kayano T., Mabuchi K., Futai M.;
RT "Nucleotide sequence of the genes coding for alpha, beta and gamma subunits
RT of the proton-translocating ATPase of Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 103:604-612(1981).
RN [9]
RP PROTEIN SEQUENCE OF 325-359.
RX PubMed=2889623; DOI=10.1016/0014-5793(87)80326-5;
RA Wise J.G., Hicke B.J., Boyer P.D.;
RT "Catalytic and noncatalytic nucleotide binding sites of the Escherichia
RT coli F1 ATPase. Amino acid sequences of beta-subunit tryptic peptides
RT labeled with 2-azido-ATP.";
RL FEBS Lett. 223:395-401(1987).
RN [10]
RP PROTEIN SEQUENCE OF 2-24.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [11]
RP PROTEIN SEQUENCE OF 2-12.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [12]
RP MUTAGENESIS.
RX PubMed=1832155; DOI=10.1016/s0021-9258(18)55304-7;
RA Iwamoto A., Omote H., Hanada H., Tomioka N., Itai A., Maeda M., Futai M.;
RT "Mutations in Ser174 and the glycine-rich sequence (Gly149, Gly150, and
RT Thr156) in the beta subunit of Escherichia coli H(+)-ATPase.";
RL J. Biol. Chem. 266:16350-16355(1991).
RN [13]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (4.4 ANGSTROMS).
RX PubMed=10570135; DOI=10.1073/pnas.96.24.13697;
RA Hausrath A.C., Grueber G., Matthews B.W., Capaldi R.A.;
RT "Structural features of the gamma subunit of the Escherichia coli F(1)
RT ATPase revealed by a 4.4-A resolution map obtained by X-ray
RT crystallography.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13697-13702(1999).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The catalytic sites are hosted primarily by the
CC 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 Evidence={ECO:0000255|HAMAP-Rule:MF_01347};
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(1), b(2) and c(9-12). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. CF(1) is
CC attached to CF(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta and b chains.
CC -!- INTERACTION:
CC P0ABB4; P0ABB0: atpA; NbExp=13; IntAct=EBI-368783, EBI-368707;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR EMBL; X01631; CAA25782.1; -; Genomic_DNA.
DR EMBL; V00267; CAA23527.1; -; Genomic_DNA.
DR EMBL; M25464; AAA83875.1; -; Genomic_DNA.
DR EMBL; J01594; AAA24737.1; -; Genomic_DNA.
DR EMBL; V00311; CAA23594.1; -; Genomic_DNA.
DR EMBL; V00312; CAA23598.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62084.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76755.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77556.1; -; Genomic_DNA.
DR PIR; A93742; PWECB.
DR RefSeq; NP_418188.1; NC_000913.3.
DR RefSeq; WP_000190506.1; NZ_STEB01000015.1.
DR PDB; 1D8S; X-ray; 4.40 A; D/E/F=1-460.
DR PDB; 3OAA; X-ray; 3.26 A; D/E/F/L/M/N/T/U/V/b/c/d=2-460.
DR PDB; 5T4O; EM; 6.90 A; D/E/F=1-460.
DR PDB; 5T4P; EM; 7.77 A; D/E/F=1-460.
DR PDB; 5T4Q; EM; 8.53 A; D/E/F=1-460.
DR PDB; 6OQR; EM; 3.10 A; D/E/F=1-460.
DR PDB; 6OQS; EM; 3.30 A; D/E/F=1-460.
DR PDB; 6OQT; EM; 3.10 A; D/E/F=1-460.
DR PDB; 6OQU; EM; 3.20 A; D/E/F=1-460.
DR PDB; 6OQV; EM; 3.30 A; D/E/F=1-460.
DR PDB; 6OQW; EM; 3.10 A; D/E/F=1-460.
DR PDB; 6PQV; EM; 3.30 A; D/E/F=1-460.
DR PDB; 6WNQ; EM; 3.40 A; D/E/F=1-460.
DR PDB; 6WNR; EM; 3.30 A; D/E/F=1-460.
DR PDBsum; 1D8S; -.
DR PDBsum; 3OAA; -.
DR PDBsum; 5T4O; -.
DR PDBsum; 5T4P; -.
DR PDBsum; 5T4Q; -.
DR PDBsum; 6OQR; -.
DR PDBsum; 6OQS; -.
DR PDBsum; 6OQT; -.
DR PDBsum; 6OQU; -.
DR PDBsum; 6OQV; -.
DR PDBsum; 6OQW; -.
DR PDBsum; 6PQV; -.
DR PDBsum; 6WNQ; -.
DR PDBsum; 6WNR; -.
DR AlphaFoldDB; P0ABB4; -.
DR SMR; P0ABB4; -.
DR BioGRID; 852546; 3.
DR ComplexPortal; CPX-4022; ATP synthase complex.
DR DIP; DIP-31846N; -.
DR IntAct; P0ABB4; 31.
DR MINT; P0ABB4; -.
DR STRING; 511145.b3732; -.
DR TCDB; 3.A.2.1.1; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR CarbonylDB; P0ABB4; -.
DR SWISS-2DPAGE; P0ABB4; -.
DR jPOST; P0ABB4; -.
DR PaxDb; P0ABB4; -.
DR PRIDE; P0ABB4; -.
DR EnsemblBacteria; AAC76755; AAC76755; b3732.
DR EnsemblBacteria; BAE77556; BAE77556; BAE77556.
DR GeneID; 67417719; -.
DR GeneID; 948244; -.
DR KEGG; ecj:JW3710; -.
DR KEGG; eco:b3732; -.
DR PATRIC; fig|1411691.4.peg.2968; -.
DR EchoBASE; EB0099; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_6; -.
DR InParanoid; P0ABB4; -.
DR OMA; GFNMIMD; -.
DR PhylomeDB; P0ABB4; -.
DR BioCyc; EcoCyc:ATPD-MON; -.
DR BioCyc; MetaCyc:ATPD-MON; -.
DR BRENDA; 7.1.2.2; 2026.
DR EvolutionaryTrace; P0ABB4; -.
DR PRO; PR:P0ABB4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IPI:ComplexPortal.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IMP:EcoliWiki.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IMP:EcoCyc.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IMP:ComplexPortal.
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; Cell inner membrane;
KW Cell membrane; CF(1); Direct protein sequencing; Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Reference proteome;
KW Translocase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646, ECO:0000269|Ref.11"
FT CHAIN 2..460
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000144437"
FT BINDING 150..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT MUTAGEN 157
FT /note="T->A,C: Impairs ATPase activity."
FT /evidence="ECO:0000269|PubMed:1832155"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:6OQR"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:6OQS"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:6OQW"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:6OQW"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:6OQR"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 214..233
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:6OQW"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 290..298
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:6OQR"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:6OQR"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 352..370
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 372..378
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 387..400
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:6OQT"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 421..433
FT /evidence="ECO:0007829|PDB:6OQR"
FT TURN 434..438
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 450..458
FT /evidence="ECO:0007829|PDB:6OQR"
SQ SEQUENCE 460 AA; 50325 MW; 18DB33154B1AE6FE CRC64;
MATGKIVQVI GAVVDVEFPQ DAVPRVYDAL EVQNGNERLV LEVQQQLGGG IVRTIAMGSS
DGLRRGLDVK DLEHPIEVPV GKATLGRIMN VLGEPVDMKG EIGEEERWAI HRAAPSYEEL
SNSQELLETG IKVIDLMCPF AKGGKVGLFG GAGVGKTVNM MELIRNIAIE HSGYSVFAGV
GERTREGNDF YHEMTDSNVI DKVSLVYGQM NEPPGNRLRV ALTGLTMAEK FRDEGRDVLL
FVDNIYRYTL AGTEVSALLG RMPSAVGYQP TLAEEMGVLQ ERITSTKTGS ITSVQAVYVP
ADDLTDPSPA TTFAHLDATV VLSRQIASLG IYPAVDPLDS TSRQLDPLVV GQEHYDTARG
VQSILQRYQE LKDIIAILGM DELSEEDKLV VARARKIQRF LSQPFFVAEV FTGSPGKYVS
LKDTIRGFKG IMEGEYDHLP EQAFYMVGSI EEAVEKAKKL
