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P0ABB4

- ATPB_ECOLI

UniProt

P0ABB4 - ATPB_ECOLI

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Protein
ATP synthase subunit beta
Gene
atpD, papB, uncD, b3732, JW3710
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.UniRule annotation

Catalytic activityi

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi150 – 1578ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. protein binding Source: IntAct
  3. proton-transporting ATP synthase activity, rotational mechanism Source: UniProtKB-HAMAP
  4. proton-transporting ATPase activity, rotational mechanism Source: EcoCyc

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. plasma membrane ATP synthesis coupled proton transport Source: UniProtKB-HAMAP
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 beta (EC:3.6.3.14)
Alternative name(s):
ATP synthase F1 sector subunit beta
F-ATPase subunit beta
Gene namesi
Name:atpD
Synonyms:papB, uncD
Ordered Locus Names:b3732, JW3710
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10101. atpD.

Subcellular locationi

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. plasma membrane Source: UniProtKB-SubCell
  3. 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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 460459ATP synthase subunit betaUniRule annotation
PRO_0000144437Add
BLAST

Proteomic databases

PaxDbiP0ABB4.
PRIDEiP0ABB4.

2D gel databases

SWISS-2DPAGEP0ABB4.

Expressioni

Gene expression databases

GenevestigatoriP0ABB4.

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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP0ABB4.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0055.
HOGENOMiHOG000009605.
KOiK02112.
OMAiKYLSQPF.
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

MATGKIVQVI GAVVDVEFPQ DAVPRVYDAL EVQNGNERLV LEVQQQLGGG    50
IVRTIAMGSS DGLRRGLDVK DLEHPIEVPV GKATLGRIMN VLGEPVDMKG 100
EIGEEERWAI HRAAPSYEEL SNSQELLETG IKVIDLMCPF AKGGKVGLFG 150
GAGVGKTVNM MELIRNIAIE HSGYSVFAGV GERTREGNDF YHEMTDSNVI 200
DKVSLVYGQM NEPPGNRLRV ALTGLTMAEK FRDEGRDVLL FVDNIYRYTL 250
AGTEVSALLG RMPSAVGYQP TLAEEMGVLQ ERITSTKTGS ITSVQAVYVP 300
ADDLTDPSPA TTFAHLDATV VLSRQIASLG IYPAVDPLDS TSRQLDPLVV 350
GQEHYDTARG VQSILQRYQE LKDIIAILGM DELSEEDKLV VARARKIQRF 400
LSQPFFVAEV FTGSPGKYVS LKDTIRGFKG IMEGEYDHLP EQAFYMVGSI 450
EEAVEKAKKL 460
Length:460
Mass (Da):50,325
Last modified:January 23, 2007 - v2
Checksum:i18DB33154B1AE6FE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_491697.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76755; AAC76755; b3732.
BAE77556; BAE77556; BAE77556.
GeneIDi12932182.
948244.
KEGGiecj:Y75_p3436.
eco:b3732.
PATRICi32122961. VBIEscCol129921_3856.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A93742. PWECB.
RefSeqi NP_418188.1. NC_000913.3.
YP_491697.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D8S X-ray 4.40 D/E/F 1-460 [» ]
3OAA X-ray 3.26 D/E/F/L/M/N/T/U/V/b/c/d 2-460 [» ]
ProteinModelPortali P0ABB4.
SMRi P0ABB4. Positions 3-460.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-31846N.
IntActi P0ABB4. 31 interactions.
MINTi MINT-1251407.
STRINGi 511145.b3732.

Protein family/group databases

TCDBi 3.A.2.1.1. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

2D gel databases

SWISS-2DPAGE P0ABB4.

Proteomic databases

PaxDbi P0ABB4.
PRIDEi P0ABB4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76755 ; AAC76755 ; b3732 .
BAE77556 ; BAE77556 ; BAE77556 .
GeneIDi 12932182.
948244.
KEGGi ecj:Y75_p3436.
eco:b3732.
PATRICi 32122961. VBIEscCol129921_3856.

Organism-specific databases

EchoBASEi EB0099.
EcoGenei EG10101. atpD.

Phylogenomic databases

eggNOGi COG0055.
HOGENOMi HOG000009605.
KOi K02112.
OMAi KYLSQPF.
OrthoDBi EOG6HQSP3.
PhylomeDBi P0ABB4.

Enzyme and pathway databases

BioCyci EcoCyc:ATPD-MONOMER.
ECOL316407:JW3710-MONOMER.
MetaCyc:ATPD-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0ABB4.
PROi P0ABB4.

Gene expression databases

Genevestigatori P0ABB4.

Family and domain databases

Gene3Di 1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_01347. ATP_synth_beta_bact.
InterProi IPR003593. 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 ]
PANTHERi PTHR15184:SF8. PTHR15184:SF8. 1 hit.
Pfami PF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01039. atpD. 1 hit.
PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 90 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

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