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P0ABB4

- ATPB_ECOLI

UniProt

P0ABB4 - ATPB_ECOLI

Protein

ATP synthase subunit beta

Gene

atpD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

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

    GO - Biological processi

    1. ATP hydrolysis coupled proton transport Source: InterPro
    2. plasma membrane ATP synthesis coupled proton transport Source: UniProtKB-HAMAP

    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: 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

    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.

    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

    1
    460
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ABB4.

    Family & Domainsi

    Sequence similaritiesi

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

    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

    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: October 1, 2014
    This is version 91 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