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Protein

ATP synthase subunit beta

Gene

atpD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi150 – 1578ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ATPD-MONOMER.
ECOL316407:JW3710-MONOMER.
MetaCyc:ATPD-MONOMER.

Protein family/group databases

TCDBi3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit betaUniRule annotation (EC:3.6.3.14UniRule annotation)
Alternative name(s):
ATP synthase F1 sector subunit betaUniRule annotation
F-ATPase subunit betaUniRule annotation
Gene namesi
Name:atpDUniRule annotation
Synonyms:papB, uncD
Ordered Locus Names:b3732, JW3710
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10101. atpD.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
  • proton-transporting ATP synthase complex, catalytic core F(1) Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, CF(1), Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi157 – 1571T → A or C: Impairs ATPase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 460459ATP synthase subunit betaPRO_0000144437Add
BLAST

Proteomic databases

PaxDbiP0ABB4.
PRIDEiP0ABB4.

2D gel databases

SWISS-2DPAGEP0ABB4.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a1, b2 and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF1 is attached to CF0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.

Binary interactionsi

WithEntry#Exp.IntActNotes
atpAP0ABB010EBI-368783,EBI-368707

Protein-protein interaction databases

DIPiDIP-31846N.
IntActiP0ABB4. 31 interactions.
MINTiMINT-1251407.
STRINGi511145.b3732.

Structurei

Secondary structure

1
460
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Beta strandi13 – 175Combined sources
Beta strandi29 – 335Combined sources
Beta strandi38 – 469Combined sources
Beta strandi48 – 5811Combined sources
Beta strandi68 – 714Combined sources
Beta strandi73 – 753Combined sources
Turni82 – 865Combined sources
Beta strandi97 – 993Combined sources
Beta strandi108 – 1103Combined sources
Helixi132 – 1365Combined sources
Beta strandi145 – 1506Combined sources
Helixi156 – 16914Combined sources
Beta strandi175 – 1795Combined sources
Helixi184 – 19613Combined sources
Helixi198 – 2003Combined sources
Beta strandi203 – 2075Combined sources
Helixi214 – 23118Combined sources
Turni232 – 2354Combined sources
Beta strandi237 – 2437Combined sources
Helixi245 – 25814Combined sources
Helixi265 – 2673Combined sources
Helixi272 – 28110Combined sources
Beta strandi290 – 2989Combined sources
Helixi300 – 3023Combined sources
Helixi307 – 3137Combined sources
Beta strandi317 – 3226Combined sources
Helixi324 – 3285Combined sources
Turni337 – 3393Combined sources
Helixi347 – 3504Combined sources
Helixi352 – 37726Combined sources
Helixi380 – 3823Combined sources
Helixi387 – 40014Combined sources
Turni407 – 4115Combined sources
Helixi421 – 43111Combined sources
Turni432 – 4343Combined sources
Helixi435 – 4384Combined sources
Helixi441 – 4444Combined sources
Helixi450 – 45910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8SX-ray4.40D/E/F1-460[»]
3OAAX-ray3.26D/E/F/L/M/N/T/U/V/b/c/d2-460[»]
ProteinModelPortaliP0ABB4.
SMRiP0ABB4. Positions 3-460.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABB4.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0055.
HOGENOMiHOG000009605.
InParanoidiP0ABB4.
KOiK02112.
OMAiQQGIYPA.
OrthoDBiEOG6HQSP3.
PhylomeDBiP0ABB4.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR15184:SF8. PTHR15184:SF8. 1 hit.
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ABB4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATGKIVQVI GAVVDVEFPQ DAVPRVYDAL EVQNGNERLV LEVQQQLGGG
60 70 80 90 100
IVRTIAMGSS DGLRRGLDVK DLEHPIEVPV GKATLGRIMN VLGEPVDMKG
110 120 130 140 150
EIGEEERWAI HRAAPSYEEL SNSQELLETG IKVIDLMCPF AKGGKVGLFG
160 170 180 190 200
GAGVGKTVNM MELIRNIAIE HSGYSVFAGV GERTREGNDF YHEMTDSNVI
210 220 230 240 250
DKVSLVYGQM NEPPGNRLRV ALTGLTMAEK FRDEGRDVLL FVDNIYRYTL
260 270 280 290 300
AGTEVSALLG RMPSAVGYQP TLAEEMGVLQ ERITSTKTGS ITSVQAVYVP
310 320 330 340 350
ADDLTDPSPA TTFAHLDATV VLSRQIASLG IYPAVDPLDS TSRQLDPLVV
360 370 380 390 400
GQEHYDTARG VQSILQRYQE LKDIIAILGM DELSEEDKLV VARARKIQRF
410 420 430 440 450
LSQPFFVAEV FTGSPGKYVS LKDTIRGFKG IMEGEYDHLP EQAFYMVGSI
460
EEAVEKAKKL
Length:460
Mass (Da):50,325
Last modified:January 23, 2007 - v2
Checksum:i18DB33154B1AE6FE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01631 Genomic DNA. Translation: CAA25782.1.
V00267 Genomic DNA. Translation: CAA23527.1.
M25464 Genomic DNA. Translation: AAA83875.1.
J01594 Genomic DNA. Translation: AAA24737.1.
V00311 Genomic DNA. Translation: CAA23594.1.
V00312 Genomic DNA. Translation: CAA23598.1.
L10328 Genomic DNA. Translation: AAA62084.1.
U00096 Genomic DNA. Translation: AAC76755.1.
AP009048 Genomic DNA. Translation: BAE77556.1.
PIRiA93742. PWECB.
RefSeqiNP_418188.1. NC_000913.3.
WP_000190506.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC76755; AAC76755; b3732.
BAE77556; BAE77556; BAE77556.
GeneIDi948244.
KEGGieco:b3732.
PATRICi32122961. VBIEscCol129921_3856.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01631 Genomic DNA. Translation: CAA25782.1.
V00267 Genomic DNA. Translation: CAA23527.1.
M25464 Genomic DNA. Translation: AAA83875.1.
J01594 Genomic DNA. Translation: AAA24737.1.
V00311 Genomic DNA. Translation: CAA23594.1.
V00312 Genomic DNA. Translation: CAA23598.1.
L10328 Genomic DNA. Translation: AAA62084.1.
U00096 Genomic DNA. Translation: AAC76755.1.
AP009048 Genomic DNA. Translation: BAE77556.1.
PIRiA93742. PWECB.
RefSeqiNP_418188.1. NC_000913.3.
WP_000190506.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8SX-ray4.40D/E/F1-460[»]
3OAAX-ray3.26D/E/F/L/M/N/T/U/V/b/c/d2-460[»]
ProteinModelPortaliP0ABB4.
SMRiP0ABB4. Positions 3-460.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-31846N.
IntActiP0ABB4. 31 interactions.
MINTiMINT-1251407.
STRINGi511145.b3732.

Protein family/group databases

TCDBi3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

2D gel databases

SWISS-2DPAGEP0ABB4.

Proteomic databases

PaxDbiP0ABB4.
PRIDEiP0ABB4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76755; AAC76755; b3732.
BAE77556; BAE77556; BAE77556.
GeneIDi948244.
KEGGieco:b3732.
PATRICi32122961. VBIEscCol129921_3856.

Organism-specific databases

EchoBASEiEB0099.
EcoGeneiEG10101. atpD.

Phylogenomic databases

eggNOGiCOG0055.
HOGENOMiHOG000009605.
InParanoidiP0ABB4.
KOiK02112.
OMAiQQGIYPA.
OrthoDBiEOG6HQSP3.
PhylomeDBiP0ABB4.

Enzyme and pathway databases

BioCyciEcoCyc:ATPD-MONOMER.
ECOL316407:JW3710-MONOMER.
MetaCyc:ATPD-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0ABB4.
PROiP0ABB4.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR15184:SF8. PTHR15184:SF8. 1 hit.
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS."
    Walker J.E., Gay N.J., Saraste M., Eberle A.N.
    Biochem. J. 224:799-815(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The atp operon: nucleotide sequence of the genes for the gamma, beta, and epsilon subunits of Escherichia coli ATP synthase."
    Saraste M., Gay N.J., Eberle A., Runswick M.J., Walker J.E.
    Nucleic Acids Res. 9:5287-5296(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Structure and function of H+-ATPase: what we have learned from Escherichia coli H+-ATPase."
    Kanazawa H., Futai M.
    Ann. N. Y. Acad. Sci. 402:45-64(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Nucleotide sequence of the genes for beta and epsilon subunits of proton-translocating ATPase from Escherichia coli."
    Kanazawa H., Kayano T., Kiyasu T., Futai M.
    Biochem. Biophys. Res. Commun. 105:1257-1264(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
    Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
    Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Nucleotide sequence of the genes coding for alpha, beta and gamma subunits of the proton-translocating ATPase of Escherichia coli."
    Kanazawa H., Kayano T., Mabuchi K., Futai M.
    Biochem. Biophys. Res. Commun. 103:604-612(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
  9. "Catalytic and noncatalytic nucleotide binding sites of the Escherichia coli F1 ATPase. Amino acid sequences of beta-subunit tryptic peptides labeled with 2-azido-ATP."
    Wise J.G., Hicke B.J., Boyer P.D.
    FEBS Lett. 223:395-401(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 325-359.
  10. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-24.
    Strain: K12 / EMG2.
  11. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
    Submitted (FEB-1996) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  12. "Mutations in Ser174 and the glycine-rich sequence (Gly149, Gly150, and Thr156) in the beta subunit of Escherichia coli H(+)-ATPase."
    Iwamoto A., Omote H., Hanada H., Tomioka N., Itai A., Maeda M., Futai M.
    J. Biol. Chem. 266:16350-16355(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  13. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  14. "Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by X-ray crystallography."
    Hausrath A.C., Grueber G., Matthews B.W., Capaldi R.A.
    Proc. Natl. Acad. Sci. U.S.A. 96:13697-13702(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.4 ANGSTROMS).

Entry informationi

Entry nameiATPB_ECOLI
AccessioniPrimary (citable) accession number: P0ABB4
Secondary accession number(s): P00824, Q2M850
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.