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P0A6E6

- ATPE_ECOLI

UniProt

P0A6E6 - ATPE_ECOLI

Protein

ATP synthase epsilon chain

Gene

atpC

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

    Produces ATP from ADP in the presence of a proton gradient across the membrane.

    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: 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:ATPC-MONOMER.
    ECOL316407:JW3709-MONOMER.
    MetaCyc:ATPC-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 epsilon chain
    Alternative name(s):
    ATP synthase F1 sector epsilon subunit
    F-ATPase epsilon subunit
    Gene namesi
    Name:atpC
    Synonyms:papG, uncC
    Ordered Locus Names:b3731, JW3709
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10100. atpC.

    Subcellular locationi

    Cell inner membrane 2 Publications; Peripheral membrane protein 2 Publications

    GO - Cellular componenti

    1. plasma membrane Source: UniProtKB-SubCell
    2. proton-transporting ATP synthase complex, catalytic core F(1) Source: EcoliWiki

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, CF(1), Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 139138ATP synthase epsilon chainPRO_0000188132Add
    BLAST

    Proteomic databases

    PaxDbiP0A6E6.
    PRIDEiP0A6E6.

    2D gel databases

    SWISS-2DPAGEP0A6E6.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A6E6.

    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: a, b and c.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    atpGP0ABA64EBI-544362,EBI-544306

    Protein-protein interaction databases

    DIPiDIP-47828N.
    IntActiP0A6E6. 7 interactions.
    STRINGi511145.b3731.

    Structurei

    Secondary structure

    1
    139
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 139
    Beta strandi15 – 3521
    Beta strandi42 – 465
    Beta strandi48 – 558
    Turni56 – 583
    Beta strandi60 – 656
    Beta strandi68 – 725
    Beta strandi77 – 815
    Helixi88 – 10316
    Beta strandi110 – 1123
    Helixi115 – 13319
    Helixi134 – 1374

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AQTX-ray2.30A4-139[»]
    1BSHNMR-A2-139[»]
    1BSNNMR-A2-139[»]
    1FS0X-ray2.10E2-139[»]
    1QO1X-ray3.90J4-139[»]
    3OAAX-ray3.26H/P/X/f2-139[»]
    ProteinModelPortaliP0A6E6.
    SMRiP0A6E6. Positions 2-139.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6E6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase epsilon chain family.Curated

    Phylogenomic databases

    eggNOGiCOG0355.
    HOGENOMiHOG000216025.
    KOiK02114.
    OMAiHIFNGEV.
    OrthoDBiEOG690MN9.
    PhylomeDBiP0A6E6.

    Family and domain databases

    Gene3Di2.60.15.10. 1 hit.
    HAMAPiMF_00530. ATP_synth_epsil_bac.
    InterProiIPR001469. ATPase_F1-cplx_dsu/esu.
    IPR020546. ATPase_F1-cplx_dsu/esu_N.
    IPR020547. ATPase_F1_dsu/esu_C.
    [Graphical view]
    PANTHERiPTHR13822. PTHR13822. 1 hit.
    PfamiPF00401. ATP-synt_DE. 1 hit.
    PF02823. ATP-synt_DE_N. 1 hit.
    [Graphical view]
    ProDomiPD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF46604. SSF46604. 1 hit.
    SSF51344. SSF51344. 1 hit.
    TIGRFAMsiTIGR01216. ATP_synt_epsi. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A6E6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMTYHLDVV SAEQQMFSGL VEKIQVTGSE GELGIYPGHA PLLTAIKPGM    50
    IRIVKQHGHE EFIYLSGGIL EVQPGNVTVL ADTAIRGQDL DEARAMEAKR 100
    KAEEHISSSH GDVDYAQASA ELAKAIAQLR VIELTKKAM 139
    Length:139
    Mass (Da):15,068
    Last modified:January 23, 2007 - v2
    Checksum:i5EFF7DE911745A62
    GO

    Sequence cautioni

    The sequence CAA23528.1 differs from that shown. Reason: Frameshift at position 132.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131E → K AA sequence (PubMed:9868784)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01594 Genomic DNA. Translation: AAA24738.1.
    X01631 Genomic DNA. Translation: CAA25783.1.
    V00311 Genomic DNA. Translation: CAA23595.1.
    M25464 Genomic DNA. Translation: AAA83876.1.
    V00267 Genomic DNA. Translation: CAA23528.1. Frameshift.
    L10328 Genomic DNA. Translation: AAA62083.1.
    U00096 Genomic DNA. Translation: AAC76754.1.
    AP009048 Genomic DNA. Translation: BAE77557.1.
    PIRiB90106. PWECE.
    RefSeqiNP_418187.1. NC_000913.3.
    YP_491698.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76754; AAC76754; b3731.
    BAE77557; BAE77557; BAE77557.
    GeneIDi12932183.
    948245.
    KEGGiecj:Y75_p3437.
    eco:b3731.
    PATRICi32122959. VBIEscCol129921_3855.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01594 Genomic DNA. Translation: AAA24738.1 .
    X01631 Genomic DNA. Translation: CAA25783.1 .
    V00311 Genomic DNA. Translation: CAA23595.1 .
    M25464 Genomic DNA. Translation: AAA83876.1 .
    V00267 Genomic DNA. Translation: CAA23528.1 . Frameshift.
    L10328 Genomic DNA. Translation: AAA62083.1 .
    U00096 Genomic DNA. Translation: AAC76754.1 .
    AP009048 Genomic DNA. Translation: BAE77557.1 .
    PIRi B90106. PWECE.
    RefSeqi NP_418187.1. NC_000913.3.
    YP_491698.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AQT X-ray 2.30 A 4-139 [» ]
    1BSH NMR - A 2-139 [» ]
    1BSN NMR - A 2-139 [» ]
    1FS0 X-ray 2.10 E 2-139 [» ]
    1QO1 X-ray 3.90 J 4-139 [» ]
    3OAA X-ray 3.26 H/P/X/f 2-139 [» ]
    ProteinModelPortali P0A6E6.
    SMRi P0A6E6. Positions 2-139.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-47828N.
    IntActi P0A6E6. 7 interactions.
    STRINGi 511145.b3731.

    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 P0A6E6.

    Proteomic databases

    PaxDbi P0A6E6.
    PRIDEi P0A6E6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76754 ; AAC76754 ; b3731 .
    BAE77557 ; BAE77557 ; BAE77557 .
    GeneIDi 12932183.
    948245.
    KEGGi ecj:Y75_p3437.
    eco:b3731.
    PATRICi 32122959. VBIEscCol129921_3855.

    Organism-specific databases

    EchoBASEi EB0098.
    EcoGenei EG10100. atpC.

    Phylogenomic databases

    eggNOGi COG0355.
    HOGENOMi HOG000216025.
    KOi K02114.
    OMAi HIFNGEV.
    OrthoDBi EOG690MN9.
    PhylomeDBi P0A6E6.

    Enzyme and pathway databases

    BioCyci EcoCyc:ATPC-MONOMER.
    ECOL316407:JW3709-MONOMER.
    MetaCyc:ATPC-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A6E6.
    PROi P0A6E6.

    Gene expression databases

    Genevestigatori P0A6E6.

    Family and domain databases

    Gene3Di 2.60.15.10. 1 hit.
    HAMAPi MF_00530. ATP_synth_epsil_bac.
    InterProi IPR001469. ATPase_F1-cplx_dsu/esu.
    IPR020546. ATPase_F1-cplx_dsu/esu_N.
    IPR020547. ATPase_F1_dsu/esu_C.
    [Graphical view ]
    PANTHERi PTHR13822. PTHR13822. 1 hit.
    Pfami PF00401. ATP-synt_DE. 1 hit.
    PF02823. ATP-synt_DE_N. 1 hit.
    [Graphical view ]
    ProDomi PD000944. ATPase_F1-cplx_dsu/esu. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF46604. SSF46604. 1 hit.
    SSF51344. SSF51344. 1 hit.
    TIGRFAMsi TIGR01216. ATP_synt_epsi. 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. "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].
    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. "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].
    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. "Small genes/gene-products in Escherichia coli K-12."
      Wasinger V.C., Humphery-Smith I.
      FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21.
      Strain: K12.
    9. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
      Submitted (FEB-1996) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-9.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    10. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
      Strain: BL21-DE3.
    11. "Membrane localization of small proteins in Escherichia coli."
      Fontaine F., Fuchs R.T., Storz G.
      J. Biol. Chem. 286:32464-32474(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
      Strain: K12 / MG1655 / ATCC 47076.
    12. "Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy."
      Wilkens S., Dahlquist F.W., McIntosh L.P., Donaldson L.W., Capaldi R.A.
      Nat. Struct. Biol. 2:961-967(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    13. "Solution structure of the epsilon subunit of the F1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex."
      Wilkens S., Capaldi R.A.
      J. Biol. Chem. 273:26645-26651(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    14. "Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli."
      Uhlin U., Cox G.B., Guss J.M.
      Structure 5:1219-1230(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

    Entry informationi

    Entry nameiATPE_ECOLI
    AccessioniPrimary (citable) accession number: P0A6E6
    Secondary accession number(s): P00832, Q2M849
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 95 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