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P0ABB0

- ATPA_ECOLI

UniProt

P0ABB0 - ATPA_ECOLI

Protein

ATP synthase subunit alpha

Gene

atpA

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 93 (01 Oct 2014)
      Sequence version 1 (08 Nov 2005)
      Previous versions | rss
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    Functioni

    Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei373 – 3731Required for activity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi169 – 1768ATPCurated

    GO - Molecular functioni

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

    GO - Biological processi

    1. ATP hydrolysis coupled proton transport Source: InterPro
    2. ATP synthesis coupled proton transport Source: EcoliWiki
    3. 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:ATPA-MONOMER.
    ECOL316407:JW3712-MONOMER.
    MetaCyc:ATPA-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 alphaUniRule annotation (EC:3.6.3.14UniRule annotation)
    Alternative name(s):
    ATP synthase F1 sector subunit alphaUniRule annotation
    F-ATPase subunit alphaUniRule annotation
    Gene namesi
    Name:atpAUniRule annotation
    Synonyms:papA, uncA
    Ordered Locus Names:b3734, JW3712
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10098. atpA.

    Subcellular locationi

    Cell inner membrane 1 PublicationUniRule annotation; Peripheral membrane protein 1 PublicationUniRule annotation

    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
    Mutagenesisi175 – 1751K → E: Reduced activity and reduced ATP-binding. 1 Publication
    Mutagenesisi175 – 1751K → I: Reduced activity and loss of ATP-binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 513513ATP synthase subunit alphaPRO_0000144325Add
    BLAST

    Proteomic databases

    PaxDbiP0ABB0.
    PRIDEiP0ABB0.

    2D gel databases

    SWISS-2DPAGEP0ABB0.

    Expressioni

    Gene expression databases

    GenevestigatoriP0ABB0.

    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.UniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    atpDP0ABB410EBI-368707,EBI-368783

    Protein-protein interaction databases

    DIPiDIP-31845N.
    IntActiP0ABB0. 28 interactions.
    MINTiMINT-1251537.
    STRINGi511145.b3734.

    Structurei

    Secondary structure

    1
    513
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 358
    Beta strandi38 – 436
    Beta strandi52 – 554
    Turni56 – 583
    Beta strandi59 – 668
    Beta strandi71 – 777
    Beta strandi87 – 893
    Beta strandi94 – 985
    Helixi101 – 1033
    Beta strandi107 – 1093
    Beta strandi126 – 1305
    Beta strandi136 – 1383
    Helixi151 – 1566
    Beta strandi166 – 1749
    Helixi175 – 18410
    Beta strandi187 – 1904
    Beta strandi192 – 1998
    Helixi202 – 21514
    Beta strandi221 – 2266
    Helixi232 – 25120
    Beta strandi255 – 2617
    Helixi263 – 27614
    Helixi290 – 2989
    Beta strandi302 – 3043
    Helixi306 – 3138
    Beta strandi322 – 3265
    Beta strandi329 – 3313
    Helixi333 – 3353
    Helixi340 – 3489
    Beta strandi349 – 3557
    Helixi357 – 3604
    Turni370 – 3723
    Beta strandi374 – 3774
    Helixi378 – 3814
    Helixi384 – 40724
    Helixi415 – 43016
    Helixi443 – 45210
    Turni455 – 4595
    Helixi462 – 47514
    Helixi477 – 4793
    Helixi481 – 4899
    Helixi494 – 50714

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D8SX-ray4.40A/B/C1-513[»]
    3OAAX-ray3.26A/B/C/I/J/K/Q/R/S/Y/Z/a1-513[»]
    ProteinModelPortaliP0ABB0.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ABB0.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0056.
    HOGENOMiHOG000130111.
    KOiK02111.
    OMAiNDEIKDT.
    OrthoDBiEOG67X1S1.
    PhylomeDBiP0ABB0.

    Family and domain databases

    Gene3Di2.40.30.20. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_01346. ATP_synth_alpha_bact.
    InterProiIPR020003. ATPase_a/bsu_AS.
    IPR023366. ATPase_asu-like.
    IPR005294. ATPase_F1-cplx_asu.
    IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR004100. ATPase_F1_a/bsu_N.
    IPR018538. HAS-barrel.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR15184:SF3. PTHR15184:SF3. 1 hit.
    PfamiPF00006. ATP-synt_ab. 1 hit.
    PF00306. ATP-synt_ab_C. 1 hit.
    PF09378. HAS-barrel. 1 hit.
    [Graphical view]
    SUPFAMiSSF47917. SSF47917. 1 hit.
    SSF50615. SSF50615. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00962. atpA. 1 hit.
    PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0ABB0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQLNSTEISE LIKQRIAQFN VVSEAHNEGT IVSVSDGVIR IHGLADCMQG    50
    EMISLPGNRY AIALNLERDS VGAVVMGPYA DLAEGMKVKC TGRILEVPVG 100
    RGLLGRVVNT LGAPIDGKGP LDHDGFSAVE AIAPGVIERQ SVDQPVQTGY 150
    KAVDSMIPIG RGQRELIIGD RQTGKTALAI DAIINQRDSG IKCIYVAIGQ 200
    KASTISNVVR KLEEHGALAN TIVVVATASE SAALQYLAPY AGCAMGEYFR 250
    DRGEDALIIY DDLSKQAVAY RQISLLLRRP PGREAFPGDV FYLHSRLLER 300
    AARVNAEYVE AFTKGEVKGK TGSLTALPII ETQAGDVSAF VPTNVISITD 350
    GQIFLETNLF NAGIRPAVNP GISVSRVGGA AQTKIMKKLS GGIRTALAQY 400
    RELAAFSQFA SDLDDATRKQ LDHGQKVTEL LKQKQYAPMS VAQQSLVLFA 450
    AERGYLADVE LSKIGSFEAA LLAYVDRDHA PLMQEINQTG GYNDEIEGKL 500
    KGILDSFKAT QSW 513
    Length:513
    Mass (Da):55,222
    Last modified:November 8, 2005 - v1
    Checksum:iDD1F3859375E9103
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti91 – 911T → I in AAA83873. (PubMed:6301339)Curated
    Sequence conflicti239 – 2446PYAGCA → RMPVAL in CAA25780. (PubMed:6301339)Curated
    Sequence conflicti239 – 2446PYAGCA → RMPVAL in AAA24735. (PubMed:6301339)Curated
    Sequence conflicti300 – 3023RAA → MLQ in CAA23519. (PubMed:6272228)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01631 Genomic DNA. Translation: CAA25780.1. Sequence problems.
    J01594 Genomic DNA. Translation: AAA24735.1. Sequence problems.
    V00265 Genomic DNA. Translation: CAA23519.1. Sequence problems.
    V00312 Genomic DNA. Translation: CAA23596.1. Sequence problems.
    M12212 Unassigned DNA. Translation: AAA20045.1.
    M25464 Genomic DNA. Translation: AAA83873.1.
    L10328 Genomic DNA. Translation: AAA62086.1.
    U00096 Genomic DNA. Translation: AAC76757.1.
    AP009048 Genomic DNA. Translation: BAE77554.1.
    V00266 Genomic DNA. Translation: CAA23525.1.
    PIRiG65176. PWECA.
    RefSeqiNP_418190.1. NC_000913.3.
    YP_491695.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76757; AAC76757; b3734.
    BAE77554; BAE77554; BAE77554.
    GeneIDi12932824.
    948242.
    KEGGiecj:Y75_p3434.
    eco:b3734.
    PATRICi32122965. VBIEscCol129921_3858.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01631 Genomic DNA. Translation: CAA25780.1 . Sequence problems.
    J01594 Genomic DNA. Translation: AAA24735.1 . Sequence problems.
    V00265 Genomic DNA. Translation: CAA23519.1 . Sequence problems.
    V00312 Genomic DNA. Translation: CAA23596.1 . Sequence problems.
    M12212 Unassigned DNA. Translation: AAA20045.1 .
    M25464 Genomic DNA. Translation: AAA83873.1 .
    L10328 Genomic DNA. Translation: AAA62086.1 .
    U00096 Genomic DNA. Translation: AAC76757.1 .
    AP009048 Genomic DNA. Translation: BAE77554.1 .
    V00266 Genomic DNA. Translation: CAA23525.1 .
    PIRi G65176. PWECA.
    RefSeqi NP_418190.1. NC_000913.3.
    YP_491695.1. 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 A/B/C 1-513 [» ]
    3OAA X-ray 3.26 A/B/C/I/J/K/Q/R/S/Y/Z/a 1-513 [» ]
    ProteinModelPortali P0ABB0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-31845N.
    IntActi P0ABB0. 28 interactions.
    MINTi MINT-1251537.
    STRINGi 511145.b3734.

    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 P0ABB0.

    Proteomic databases

    PaxDbi P0ABB0.
    PRIDEi P0ABB0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76757 ; AAC76757 ; b3734 .
    BAE77554 ; BAE77554 ; BAE77554 .
    GeneIDi 12932824.
    948242.
    KEGGi ecj:Y75_p3434.
    eco:b3734.
    PATRICi 32122965. VBIEscCol129921_3858.

    Organism-specific databases

    EchoBASEi EB0096.
    EcoGenei EG10098. atpA.

    Phylogenomic databases

    eggNOGi COG0056.
    HOGENOMi HOG000130111.
    KOi K02111.
    OMAi NDEIKDT.
    OrthoDBi EOG67X1S1.
    PhylomeDBi P0ABB0.

    Enzyme and pathway databases

    BioCyci EcoCyc:ATPA-MONOMER.
    ECOL316407:JW3712-MONOMER.
    MetaCyc:ATPA-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0ABB0.
    PROi P0ABB0.

    Gene expression databases

    Genevestigatori P0ABB0.

    Family and domain databases

    Gene3Di 2.40.30.20. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPi MF_01346. ATP_synth_alpha_bact.
    InterProi IPR020003. ATPase_a/bsu_AS.
    IPR023366. ATPase_asu-like.
    IPR005294. ATPase_F1-cplx_asu.
    IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR004100. ATPase_F1_a/bsu_N.
    IPR018538. HAS-barrel.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR15184:SF3. PTHR15184:SF3. 1 hit.
    Pfami PF00006. ATP-synt_ab. 1 hit.
    PF00306. ATP-synt_ab_C. 1 hit.
    PF09378. HAS-barrel. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47917. SSF47917. 1 hit.
    SSF50615. SSF50615. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00962. atpA. 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 region encoding the alpha-subunit of Escherichia coli ATP-synthase."
      Gay N.J., Walker J.E.
      Nucleic Acids Res. 9:2187-2194(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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].
    4. "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].
    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. "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] OF 1-50.
    9. "Isolation of a fourth cysteinyl-containing peptide of the alpha-subunit of the F1 ATPase from Escherichia coli necessitates revision of the DNA sequence."
      Slan-Lotter H., Clarke D.M., Bragg P.D.
      FEBS Lett. 197:121-124(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 239-244.
    10. Cited for: PROTEIN SEQUENCE OF 1-8.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    11. "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 1-12.
      Strain: K12 / EMG2.
    12. "Directed mutagenesis of the strongly conserved lysine 175 in the proposed nucleotide-binding domain of alpha-subunit from Escherichia coli F1-ATPase."
      Rao R., Pagan J., Senior A.E.
      J. Biol. Chem. 263:15957-15963(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-175.
    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. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
      Strain: BL21-DE3.
    15. "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) OF AN ALPHA(3)/BETA (3)/GAMMA/EPSILON COMPLEX.

    Entry informationi

    Entry nameiATPA_ECOLI
    AccessioniPrimary (citable) accession number: P0ABB0
    Secondary accession number(s): P00822, Q2M852, Q47249
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: November 8, 2005
    Last modified: October 1, 2014
    This is version 93 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, 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