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P0ABA0

- ATPF_ECOLI

UniProt

P0ABA0 - ATPF_ECOLI

Protein

ATP synthase subunit b

Gene

atpF

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    F1F0 ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F1 containing the extramembraneous catalytic core and F0 containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation.UniRule annotation
    Component of the F0 channel, it forms part of the peripheral stalk, linking F1 to F0.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei9 – 91Mutation prevents the formation of a functional proton pore, but has a small effect on the binding of F(1) to F(0)
    Sitei131 – 1311Required for proton pore formation, as well as F(1) to F(0) binding

    GO - Molecular functioni

    1. proton-transporting ATPase activity, rotational mechanism Source: EcoCyc
    2. proton-transporting ATP synthase activity, rotational mechanism Source: EcoCyc

    GO - Biological processi

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

    Keywords - Biological processi

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    BioCyciEcoCyc:ATPF-MONOMER.
    ECOL316407:JW3714-MONOMER.
    MetaCyc:ATPF-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 bUniRule annotation
    Alternative name(s):
    ATP synthase F(0) sector subunit bUniRule annotation
    ATPase subunit IUniRule annotation
    F-type ATPase subunit bUniRule annotation
    Short name:
    F-ATPase subunit bUniRule annotation
    Gene namesi
    Name:atpFUniRule annotation
    Synonyms:papF, uncF
    Ordered Locus Names:b3736, JW3714
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10103. atpF.

    Subcellular locationi

    Cell inner membrane UniRule annotation; Single-pass membrane protein UniRule annotation

    GO - Cellular componenti

    1. anchored component of membrane Source: EcoliWiki
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB-SubCell
    4. proton-transporting ATP synthase complex, coupling factor F(o) Source: EcoliWiki

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, CF(0), Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 156156ATP synthase subunit bPRO_0000082371Add
    BLAST

    Proteomic databases

    PaxDbiP0ABA0.
    PRIDEiP0ABA0.

    2D gel databases

    SWISS-2DPAGEP0ABA0.

    Expressioni

    Gene expression databases

    GenevestigatoriP0ABA0.

    Interactioni

    Subunit structurei

    F-type ATPases have 2 components, F1 - the catalytic core - and F0 - the membrane proton channel. F1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. F0 has three main subunits: a1, b2 and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F1 is attached to F0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.UniRule annotation

    Protein-protein interaction databases

    DIPiDIP-35994N.
    IntActiP0ABA0. 2 interactions.
    STRINGi511145.b3736.

    Structurei

    Secondary structure

    1
    156
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 2421
    Helixi26 – 338
    Helixi63 – 12058

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B9UNMR-A1-34[»]
    1L2PX-ray1.55A62-122[»]
    2KHKNMR-A30-82[»]
    ProteinModelPortaliP0ABA0.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ABA0.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei11 – 3121HelicalUniRule annotationAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase B chain family.UniRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0711.
    HOGENOMiHOG000015378.
    KOiK02109.
    OMAiRTIDKDA.
    OrthoDBiEOG6DNTDK.
    PhylomeDBiP0ABA0.

    Family and domain databases

    Gene3Di1.20.5.620. 1 hit.
    HAMAPiMF_01398. ATP_synth_b_bact.
    InterProiIPR028987. ATPase_B-like_membr.
    IPR002146. ATPase_F0-cplx_b/b'su_bac.
    IPR005864. ATPase_F0-cplx_bsu_bac.
    [Graphical view]
    PfamiPF00430. ATP-synt_B. 1 hit.
    [Graphical view]
    SUPFAMiSSF81573. SSF81573. 1 hit.
    TIGRFAMsiTIGR01144. ATP_synt_b. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0ABA0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNLNATILGQ AIAFVLFVLF CMKYVWPPLM AAIEKRQKEI ADGLASAERA    50
    HKDLDLAKAS ATDQLKKAKA EAQVIIEQAN KRRSQILDEA KAEAEQERTK 100
    IVAQAQAEIE AERKRAREEL RKQVAILAVA GAEKIIERSV DEAANSDIVD 150
    KLVAEL 156
    Length:156
    Mass (Da):17,264
    Last modified:July 21, 1986 - v1
    Checksum:i51A93C8BEE9AD9DF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331I → F in CAA23592. (PubMed:6277311)Curated
    Sequence conflicti62 – 621T → N in AAA24741. (PubMed:7686882)Curated
    Sequence conflicti72 – 721A → D in CAA23592. (PubMed:6277311)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01594 Genomic DNA. Translation: AAA24733.1.
    X01631 Genomic DNA. Translation: CAA25778.1.
    V00264 Genomic DNA. Translation: CAA23516.1.
    V00310 Genomic DNA. Translation: CAA23592.1.
    V00266 Genomic DNA. Translation: CAA23523.1.
    M25464 Genomic DNA. Translation: AAA83871.1.
    M10422 Genomic DNA. Translation: AAA24741.1.
    L10328 Genomic DNA. Translation: AAA62088.1.
    U00096 Genomic DNA. Translation: AAC76759.1.
    AP009048 Genomic DNA. Translation: BAE77552.1.
    M12212 Unassigned DNA. Translation: AAA20043.1.
    PIRiD93732. LWECB.
    RefSeqiNP_418192.1. NC_000913.3.
    YP_491693.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76759; AAC76759; b3736.
    BAE77552; BAE77552; BAE77552.
    GeneIDi12933115.
    948247.
    KEGGiecj:Y75_p3432.
    eco:b3736.
    PATRICi32122969. VBIEscCol129921_3860.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01594 Genomic DNA. Translation: AAA24733.1 .
    X01631 Genomic DNA. Translation: CAA25778.1 .
    V00264 Genomic DNA. Translation: CAA23516.1 .
    V00310 Genomic DNA. Translation: CAA23592.1 .
    V00266 Genomic DNA. Translation: CAA23523.1 .
    M25464 Genomic DNA. Translation: AAA83871.1 .
    M10422 Genomic DNA. Translation: AAA24741.1 .
    L10328 Genomic DNA. Translation: AAA62088.1 .
    U00096 Genomic DNA. Translation: AAC76759.1 .
    AP009048 Genomic DNA. Translation: BAE77552.1 .
    M12212 Unassigned DNA. Translation: AAA20043.1 .
    PIRi D93732. LWECB.
    RefSeqi NP_418192.1. NC_000913.3.
    YP_491693.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B9U NMR - A 1-34 [» ]
    1L2P X-ray 1.55 A 62-122 [» ]
    2KHK NMR - A 30-82 [» ]
    ProteinModelPortali P0ABA0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35994N.
    IntActi P0ABA0. 2 interactions.
    STRINGi 511145.b3736.

    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 P0ABA0.

    Proteomic databases

    PaxDbi P0ABA0.
    PRIDEi P0ABA0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76759 ; AAC76759 ; b3736 .
    BAE77552 ; BAE77552 ; BAE77552 .
    GeneIDi 12933115.
    948247.
    KEGGi ecj:Y75_p3432.
    eco:b3736.
    PATRICi 32122969. VBIEscCol129921_3860.

    Organism-specific databases

    EchoBASEi EB0101.
    EcoGenei EG10103. atpF.

    Phylogenomic databases

    eggNOGi COG0711.
    HOGENOMi HOG000015378.
    KOi K02109.
    OMAi RTIDKDA.
    OrthoDBi EOG6DNTDK.
    PhylomeDBi P0ABA0.

    Enzyme and pathway databases

    BioCyci EcoCyc:ATPF-MONOMER.
    ECOL316407:JW3714-MONOMER.
    MetaCyc:ATPF-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0ABA0.
    PROi P0ABA0.

    Gene expression databases

    Genevestigatori P0ABA0.

    Family and domain databases

    Gene3Di 1.20.5.620. 1 hit.
    HAMAPi MF_01398. ATP_synth_b_bact.
    InterProi IPR028987. ATPase_B-like_membr.
    IPR002146. ATPase_F0-cplx_b/b'su_bac.
    IPR005864. ATPase_F0-cplx_bsu_bac.
    [Graphical view ]
    Pfami PF00430. ATP-synt_B. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81573. SSF81573. 1 hit.
    TIGRFAMsi TIGR01144. ATP_synt_b. 1 hit.
    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 promoter and the genes for the membrane proteins, and the delta subunit of Escherichia coli ATP-synthase."
      Gay N.J., Walker J.E.
      Nucleic Acids Res. 9:3919-3926(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Nucleotide sequence of the genes for F0 components of the proton-translocating ATPase from Escherichia coli: prediction of the primary structure of F0 subunits."
      Kanazawa H., Mabuchi K., Kayano T., Noumi T., Sekiya T., Futai M.
      Biochem. Biophys. Res. Commun. 103:613-620(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit delta of the membrane bound ATP synthase of Escherichia coli."
      Nielsen J., Hansen F.G., Hoppe J., Friedl P., von Meyenburg K.
      Mol. Gen. Genet. 184:33-39(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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].
    6. "Role of the b subunit of the Escherichia coli proton-translocating ATPase. A mutagenic analysis."
      Porter A.C.G., Kumamoto C., Aldape K., Simoni R.D.
      J. Biol. Chem. 260:8182-8187(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "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.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    9. "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.
    10. "Nucleotide sequence of the gene coding for the delta subunit of proton translocating ATPase of Escherichia coli."
      Mabuchi K., Kanazawa H., Kayano T., Futai M.
      Biochem. Biophys. Res. Commun. 102:172-179(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 132-156.
    11. "Targeted mutagenesis of the b subunit of F1F0 ATP synthase in Escherichia coli: Glu-77 through Gln-85."
      McCormick K.A., Cain B.D.
      J. Bacteriol. 173:7240-7248(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
      Strain: BL21-DE3.
    13. "Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase."
      Dmitriev O., Jones P.C., Jiang W., Fillingame R.H.
      J. Biol. Chem. 274:15598-15604(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-34.

    Entry informationi

    Entry nameiATPF_ECOLI
    AccessioniPrimary (citable) accession number: P0ABA0
    Secondary accession number(s): P00859, Q2M854
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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