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P0ABA4

- ATPD_ECOLI

UniProt

P0ABA4 - ATPD_ECOLI

Protein

ATP synthase subunit delta

Gene

atpH

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    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.
    This protein is part of the stalk that links CF0 to CF1. It either transmits conformational changes from CF0 to CF1 or is implicated in proton conduction.

    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:ATPH-MONOMER.
    ECOL316407:JW3713-MONOMER.
    MetaCyc:ATPH-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 deltaUniRule annotation
    Alternative name(s):
    ATP synthase F(1) sector subunit deltaUniRule annotation
    F-type ATPase subunit deltaUniRule annotation
    Short name:
    F-ATPase subunit deltaUniRule annotation
    Gene namesi
    Name:atpHUniRule annotation
    Synonyms:papE, uncH
    Ordered Locus Names:b3735, JW3713
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10105. atpH.

    Subcellular locationi

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

    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
    Chaini1 – 177177ATP synthase subunit deltaPRO_0000193462Add
    BLAST

    Proteomic databases

    PaxDbiP0ABA4.
    PRIDEiP0ABA4.

    Expressioni

    Gene expression databases

    GenevestigatoriP0ABA4.

    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.1 PublicationUniRule annotation

    Protein-protein interaction databases

    DIPiDIP-47921N.
    IntActiP0ABA4. 13 interactions.
    STRINGi511145.b3735.

    Structurei

    Secondary structure

    1
    177
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 2117
    Helixi25 – 3915
    Helixi42 – 487
    Helixi54 – 6512
    Helixi71 – 8212
    Helixi86 – 883
    Helixi89 – 10517

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ABVNMR-A2-135[»]
    2A7UNMR-B2-135[»]
    ProteinModelPortaliP0ABA4.
    SMRiP0ABA4. Positions 2-135.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ABA4.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase delta chain family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0712.
    HOGENOMiHOG000075824.
    KOiK02113.
    OMAiCGEQINE.
    OrthoDBiEOG6DNTDK.
    PhylomeDBiP0ABA4.

    Family and domain databases

    Gene3Di1.10.520.20. 1 hit.
    HAMAPiMF_01416. ATP_synth_delta_bact.
    InterProiIPR020781. ATPase_OSCP/d_CS.
    IPR026015. ATPase_OSCP/delta_N.
    IPR000711. ATPase_OSCP/dsu.
    [Graphical view]
    PANTHERiPTHR11910. PTHR11910. 1 hit.
    PfamiPF00213. OSCP. 1 hit.
    [Graphical view]
    PRINTSiPR00125. ATPASEDELTA.
    SUPFAMiSSF47928. SSF47928. 1 hit.
    TIGRFAMsiTIGR01145. ATP_synt_delta. 1 hit.
    PROSITEiPS00389. ATPASE_DELTA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0ABA4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEFITVARP YAKAAFDFAV EHQSVERWQD MLAFAAEVTK NEQMAELLSG    50
    ALAPETLAES FIAVCGEQLD ENGQNLIRVM AENGRLNALP DVLEQFIHLR 100
    AVSEATAEVD VISAAALSEQ QLAKISAAME KRLSRKVKLN CKIDKSVMAG 150
    VIIRAGDMVI DGSVRGRLER LADVLQS 177
    Length:177
    Mass (Da):19,332
    Last modified:July 21, 1986 - v1
    Checksum:i6AFD9552A79C81A5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti82 – 821E → D in AAA20044. (PubMed:6458296)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01594 Genomic DNA. Translation: AAA24734.1.
    M12212 Unassigned DNA. Translation: AAA20044.1.
    X01631 Genomic DNA. Translation: CAA25779.1.
    V00266 Genomic DNA. Translation: CAA23524.1.
    V00264 Genomic DNA. Translation: CAA23517.1.
    M25464 Genomic DNA. Translation: AAA83872.1.
    L10328 Genomic DNA. Translation: AAA62087.1.
    U00096 Genomic DNA. Translation: AAC76758.1.
    AP009048 Genomic DNA. Translation: BAE77553.1.
    PIRiA93732. PWECD.
    RefSeqiNP_418191.1. NC_000913.3.
    YP_491694.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76758; AAC76758; b3735.
    BAE77553; BAE77553; BAE77553.
    GeneIDi12933117.
    948254.
    KEGGiecj:Y75_p3433.
    eco:b3735.
    PATRICi32122967. VBIEscCol129921_3859.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01594 Genomic DNA. Translation: AAA24734.1 .
    M12212 Unassigned DNA. Translation: AAA20044.1 .
    X01631 Genomic DNA. Translation: CAA25779.1 .
    V00266 Genomic DNA. Translation: CAA23524.1 .
    V00264 Genomic DNA. Translation: CAA23517.1 .
    M25464 Genomic DNA. Translation: AAA83872.1 .
    L10328 Genomic DNA. Translation: AAA62087.1 .
    U00096 Genomic DNA. Translation: AAC76758.1 .
    AP009048 Genomic DNA. Translation: BAE77553.1 .
    PIRi A93732. PWECD.
    RefSeqi NP_418191.1. NC_000913.3.
    YP_491694.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ABV NMR - A 2-135 [» ]
    2A7U NMR - B 2-135 [» ]
    ProteinModelPortali P0ABA4.
    SMRi P0ABA4. Positions 2-135.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-47921N.
    IntActi P0ABA4. 13 interactions.
    STRINGi 511145.b3735.

    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.

    Proteomic databases

    PaxDbi P0ABA4.
    PRIDEi P0ABA4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76758 ; AAC76758 ; b3735 .
    BAE77553 ; BAE77553 ; BAE77553 .
    GeneIDi 12933117.
    948254.
    KEGGi ecj:Y75_p3433.
    eco:b3735.
    PATRICi 32122967. VBIEscCol129921_3859.

    Organism-specific databases

    EchoBASEi EB0103.
    EcoGenei EG10105. atpH.

    Phylogenomic databases

    eggNOGi COG0712.
    HOGENOMi HOG000075824.
    KOi K02113.
    OMAi CGEQINE.
    OrthoDBi EOG6DNTDK.
    PhylomeDBi P0ABA4.

    Enzyme and pathway databases

    BioCyci EcoCyc:ATPH-MONOMER.
    ECOL316407:JW3713-MONOMER.
    MetaCyc:ATPH-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0ABA4.
    PROi P0ABA4.

    Gene expression databases

    Genevestigatori P0ABA4.

    Family and domain databases

    Gene3Di 1.10.520.20. 1 hit.
    HAMAPi MF_01416. ATP_synth_delta_bact.
    InterProi IPR020781. ATPase_OSCP/d_CS.
    IPR026015. ATPase_OSCP/delta_N.
    IPR000711. ATPase_OSCP/dsu.
    [Graphical view ]
    PANTHERi PTHR11910. PTHR11910. 1 hit.
    Pfami PF00213. OSCP. 1 hit.
    [Graphical view ]
    PRINTSi PR00125. ATPASEDELTA.
    SUPFAMi SSF47928. SSF47928. 1 hit.
    TIGRFAMsi TIGR01145. ATP_synt_delta. 1 hit.
    PROSITEi PS00389. ATPASE_DELTA. 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 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].
    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. "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.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    8. "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.
    9. Cited for: SUBUNIT, SUBCELLULAR LOCATION.
      Strain: BL21-DE3.
    10. "Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase."
      Wilkens S., Dunn S.D., Chandler J., Dahlquist F.W., Capaldi R.A.
      Nat. Struct. Biol. 4:198-201(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-135.

    Entry informationi

    Entry nameiATPD_ECOLI
    AccessioniPrimary (citable) accession number: P0ABA4
    Secondary accession number(s): P00831, Q2M853
    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