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P0AB98

- ATP6_ECOLI

UniProt

P0AB98 - ATP6_ECOLI

Protein

ATP synthase subunit a

Gene

atpB

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 90 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.

    GO - Molecular functioni

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

    GO - Biological processi

    1. plasma membrane ATP synthesis coupled proton transport Source: EcoCyc

    Keywords - Biological processi

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    BioCyciEcoCyc:ATPB-MONOMER.
    ECOL316407:JW3716-MONOMER.
    MetaCyc:ATPB-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 aUniRule annotation
    Alternative name(s):
    ATP synthase F0 sector subunit aUniRule annotation
    F-ATPase subunit 6UniRule annotation
    Gene namesi
    Name:atpBUniRule annotation
    Synonyms:papD, uncB
    Ordered Locus Names:b3738, JW3716
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10099. atpB.

    Subcellular locationi

    Cell inner membrane 1 PublicationUniRule annotation; Multi-pass membrane protein 1 PublicationUniRule annotation

    GO - Cellular componenti

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

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi206 – 2061S → L: Reduced activity.
    Mutagenesisi207 – 2071L → Y or F: No change in activity.
    Mutagenesisi210 – 2101R → K, I, V or E: Completely defective.
    Mutagenesisi214 – 2141N → H: Completely defective.
    Mutagenesisi214 – 2141N → V: Reduced activity.
    Mutagenesisi217 – 2171A → H: Reduced activity.
    Mutagenesisi217 – 2171A → R: Completely defective.
    Mutagenesisi245 – 2451H → Y: Reduced activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 271271ATP synthase subunit aPRO_0000082053Add
    BLAST

    Expressioni

    Gene expression databases

    GenevestigatoriP0AB98.

    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.

    Protein-protein interaction databases

    DIPiDIP-47956N.
    IntActiP0AB98. 2 interactions.
    MINTiMINT-1300501.
    STRINGi511145.b3738.

    Structurei

    Secondary structure

    1
    271
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi97 – 12529
    Helixi135 – 16632
    Helixi202 – 22827
    Beta strandi229 – 2313
    Helixi233 – 26331

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C17NMR-M95-271[»]
    ProteinModelPortaliP0AB98.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AB98.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3939PeriplasmicCuratedAdd
    BLAST
    Topological domaini61 – 9939CytoplasmicCuratedAdd
    BLAST
    Topological domaini121 – 14525PeriplasmicCuratedAdd
    BLAST
    Topological domaini167 – 21953CytoplasmicCuratedAdd
    BLAST
    Topological domaini241 – 2411PeriplasmicCurated
    Topological domaini263 – 2719CytoplasmicCurated

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei40 – 6021HelicalCuratedAdd
    BLAST
    Transmembranei100 – 12021HelicalCuratedAdd
    BLAST
    Transmembranei146 – 16621HelicalCuratedAdd
    BLAST
    Transmembranei220 – 24021HelicalCuratedAdd
    BLAST
    Transmembranei242 – 26221HelicalCuratedAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase A chain family.UniRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0356.
    HOGENOMiHOG000253872.
    KOiK02108.
    OMAiSFWVLNI.
    OrthoDBiEOG6K4054.
    PhylomeDBiP0AB98.

    Family and domain databases

    Gene3Di1.20.120.220. 1 hit.
    HAMAPiMF_01393. ATP_synth_a_bact.
    InterProiIPR000568. ATPase_F0-cplx_asu.
    IPR023011. ATPase_F0-cplx_asu_AS.
    [Graphical view]
    PANTHERiPTHR11410. PTHR11410. 1 hit.
    PfamiPF00119. ATP-synt_A. 1 hit.
    [Graphical view]
    PRINTSiPR00123. ATPASEA.
    SUPFAMiSSF81336. SSF81336. 1 hit.
    TIGRFAMsiTIGR01131. ATP_synt_6_or_A. 1 hit.
    PROSITEiPS00449. ATPASE_A. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0AB98-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASENMTPQD YIGHHLNNLQ LDLRTFSLVD PQNPPATFWT INIDSMFFSV    50
    VLGLLFLVLF RSVAKKATSG VPGKFQTAIE LVIGFVNGSV KDMYHGKSKL 100
    IAPLALTIFV WVFLMNLMDL LPIDLLPYIA EHVLGLPALR VVPSADVNVT 150
    LSMALGVFIL ILFYSIKMKG IGGFTKELTL QPFNHWAFIP VNLILEGVSL 200
    LSKPVSLGLR LFGNMYAGEL IFILIAGLLP WWSQWILNVP WAIFHILIIT 250
    LQAFIFMVLT IVYLSMASEE H 271
    Length:271
    Mass (Da):30,303
    Last modified:July 21, 1986 - v1
    Checksum:i4933EAF09401566D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 711V → M in CAA23521. (PubMed:6272190)Curated
    Sequence conflicti179 – 1824TLQP → RCST in CAA23590. (PubMed:6277311)Curated
    Sequence conflicti188 – 1881F → S in AAA24740. (PubMed:2874137)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01594 Genomic DNA. Translation: AAA24731.1.
    X01631 Genomic DNA. Translation: CAA25776.1.
    V00264 Genomic DNA. Translation: CAA23514.1.
    V00266 Genomic DNA. Translation: CAA23520.1.
    V00266 Genomic DNA. Translation: CAA23521.1.
    V00310 Genomic DNA. Translation: CAA23590.1.
    M25464 Genomic DNA. Translation: AAA83869.2.
    M14019 Genomic DNA. Translation: AAA24740.1.
    L10328 Genomic DNA. Translation: AAA62090.1.
    U00096 Genomic DNA. Translation: AAC76761.1.
    AP009048 Genomic DNA. Translation: BAE77550.1.
    X01383 Genomic DNA. Translation: CAA25641.1.
    M29174 Genomic DNA. Translation: AAA24423.1.
    PIRiC93732. LWEC6.
    RefSeqiNP_418194.1. NC_000913.3.
    YP_491691.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76761; AAC76761; b3738.
    BAE77550; BAE77550; BAE77550.
    GeneIDi12933606.
    948252.
    KEGGiecj:Y75_p3430.
    eco:b3738.
    PATRICi32122973. VBIEscCol129921_3862.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01594 Genomic DNA. Translation: AAA24731.1 .
    X01631 Genomic DNA. Translation: CAA25776.1 .
    V00264 Genomic DNA. Translation: CAA23514.1 .
    V00266 Genomic DNA. Translation: CAA23520.1 .
    V00266 Genomic DNA. Translation: CAA23521.1 .
    V00310 Genomic DNA. Translation: CAA23590.1 .
    M25464 Genomic DNA. Translation: AAA83869.2 .
    M14019 Genomic DNA. Translation: AAA24740.1 .
    L10328 Genomic DNA. Translation: AAA62090.1 .
    U00096 Genomic DNA. Translation: AAC76761.1 .
    AP009048 Genomic DNA. Translation: BAE77550.1 .
    X01383 Genomic DNA. Translation: CAA25641.1 .
    M29174 Genomic DNA. Translation: AAA24423.1 .
    PIRi C93732. LWEC6.
    RefSeqi NP_418194.1. NC_000913.3.
    YP_491691.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C17 NMR - M 95-271 [» ]
    ProteinModelPortali P0AB98.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-47956N.
    IntActi P0AB98. 2 interactions.
    MINTi MINT-1300501.
    STRINGi 511145.b3738.

    Chemistry

    ChEMBLi CHEMBL1075074.

    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.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76761 ; AAC76761 ; b3738 .
    BAE77550 ; BAE77550 ; BAE77550 .
    GeneIDi 12933606.
    948252.
    KEGGi ecj:Y75_p3430.
    eco:b3738.
    PATRICi 32122973. VBIEscCol129921_3862.

    Organism-specific databases

    EchoBASEi EB0097.
    EcoGenei EG10099. atpB.

    Phylogenomic databases

    eggNOGi COG0356.
    HOGENOMi HOG000253872.
    KOi K02108.
    OMAi SFWVLNI.
    OrthoDBi EOG6K4054.
    PhylomeDBi P0AB98.

    Enzyme and pathway databases

    BioCyci EcoCyc:ATPB-MONOMER.
    ECOL316407:JW3716-MONOMER.
    MetaCyc:ATPB-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AB98.
    PROi P0AB98.

    Gene expression databases

    Genevestigatori P0AB98.

    Family and domain databases

    Gene3Di 1.20.120.220. 1 hit.
    HAMAPi MF_01393. ATP_synth_a_bact.
    InterProi IPR000568. ATPase_F0-cplx_asu.
    IPR023011. ATPase_F0-cplx_asu_AS.
    [Graphical view ]
    PANTHERi PTHR11410. PTHR11410. 1 hit.
    Pfami PF00119. ATP-synt_A. 1 hit.
    [Graphical view ]
    PRINTSi PR00123. ATPASEA.
    SUPFAMi SSF81336. SSF81336. 1 hit.
    TIGRFAMsi TIGR01131. ATP_synt_6_or_A. 1 hit.
    PROSITEi PS00449. ATPASE_A. 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 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. "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].
    4. "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].
    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. "Impaired proton conductivity resulting from mutations in the a subunit of F1F0 ATPase in Escherichia coli."
      Cai B.D., Simoni R.D.
      J. Biol. Chem. 261:10043-10050(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS.
    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. "Overproduction of subunit a of the F0 component of proton-translocating ATPase inhibits growth of Escherichia coli cells."
      Kanazawa H., Kiyasu T., Noumi T., Futai M.
      J. Bacteriol. 158:300-306(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-92.
    11. "The promoters of the atp operon of Escherichia coli K12."
      Nielsen J., Joergensen B.B., von Meyenburg K., Hansen F.G.
      Mol. Gen. Genet. 193:64-71(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
      Strain: K12.
    12. "Genetic evidence for interaction between the a and b subunits of the F0 portion of the Escherichia coli proton translocating ATPase."
      Kumamoto C.A., Simoni R.D.
      J. Biol. Chem. 261:10037-10042(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 235-271.
    13. "Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic analysis of the a subunit."
      Cain B.D., Simoni R.D.
      J. Biol. Chem. 264:3292-3300(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    14. "Temperature-sensitive mutations at the carboxy terminus of the alpha subunit of the Escherichia coli F1F0 ATP synthase."
      Vik S.B., Lee D., Marshall P.A.
      J. Bacteriol. 173:4544-4548(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    15. "A topological analysis of subunit alpha from Escherichia coli F1F0-ATP synthase predicts eight transmembrane segments."
      Lewis M.L., Chang J.A., Simoni R.D.
      J. Biol. Chem. 265:10541-10550(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY.
    16. "The transmembrane topology of the a subunit from the ATPase in Escherichia coli analyzed by PhoA protein fusions."
      Bjorbaek C., Foersom V., Michelsen O.
      FEBS Lett. 260:31-34(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY.
    17. "Transmembrane topology of Escherichia coli H(+)-ATPase (ATP synthase) subunit a."
      Yamada H., Moriyama Y., Maeda M., Futai M.
      FEBS Lett. 390:34-38(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY.
    18. "Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP synthase."
      Valiyaveetil F.I., Fillingame R.H.
      J. Biol. Chem. 273:16241-16247(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY.
    19. "Global topology analysis of the Escherichia coli inner membrane proteome."
      Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
      Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
      Strain: K12 / MG1655 / ATCC 47076.
    20. "Structural changes linked to proton translocation by subunit c of the ATP synthase."
      Rastogi V.K., Girvin M.E.
      Nature 402:263-268(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 95-271.

    Entry informationi

    Entry nameiATP6_ECOLI
    AccessioniPrimary (citable) accession number: P0AB98
    Secondary accession number(s): P00855
    , Q2M856, Q47065, Q47708
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally proposed to be encoded from either Met-1 or Val-71 (PID CAA23521); it is now thought to start of Met-1.1 Publication

    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