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Q07232

- ATPB_BUCAP

UniProt

Q07232 - ATPB_BUCAP

Protein

ATP synthase subunit beta

Gene

atpD

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (15 Dec 1998)
      Previous versions | rss
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    Functioni

    Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.UniRule annotation

    Catalytic activityi

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi156 – 1638ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. proton-transporting ATP synthase activity, rotational mechanism Source: UniProtKB-HAMAP

    GO - Biological processi

    1. ATP hydrolysis coupled proton transport Source: InterPro
    2. 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

    BioCyciBAPH198804:GHMG-8-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase subunit betaUniRule annotation (EC:3.6.3.14UniRule annotation)
    Alternative name(s):
    ATP synthase F1 sector subunit betaUniRule annotation
    F-ATPase subunit betaUniRule annotation
    Gene namesi
    Name:atpDUniRule annotation
    Synonyms:uncD
    Ordered Locus Names:BUsg_008
    OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
    Taxonomic identifieri198804 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
    ProteomesiUP000000416: Chromosome

    Subcellular locationi

    Cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, CF(1), Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 466466ATP synthase subunit betaPRO_0000144427Add
    BLAST

    Proteomic databases

    PRIDEiQ07232.

    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

    Protein-protein interaction databases

    STRINGi198804.BUsg008.

    Structurei

    3D structure databases

    ProteinModelPortaliQ07232.
    SMRiQ07232. Positions 5-466.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0055.
    KOiK02112.
    OMAiKYLSQPF.
    OrthoDBiEOG6HQSP3.

    Family and domain databases

    Gene3Di1.10.1140.10. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_01347. ATP_synth_beta_bact.
    InterProiIPR003593. AAA+_ATPase.
    IPR020003. ATPase_a/bsu_AS.
    IPR005722. ATPase_F1-cplx_bsu.
    IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR004100. ATPase_F1_a/bsu_N.
    IPR024034. ATPase_F1_bsu/V1_C.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR15184:SF8. PTHR15184:SF8. 1 hit.
    PfamiPF00006. ATP-synt_ab. 1 hit.
    PF00306. ATP-synt_ab_C. 1 hit.
    PF02874. ATP-synt_ab_N. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF47917. SSF47917. 1 hit.
    SSF50615. SSF50615. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR01039. atpD. 1 hit.
    PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q07232-1 [UniParc]FASTAAdd to Basket

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    MIATGKIIQI IGAVVDVEFD QNSVPKIYNA LEVKNKKIQL ILEVQQQLGA    50
    GIVRTIAMGS TNGLKRGLIV IDLGHYIKVP VGQATLGRII NVLGKTIDNK 100
    GPLKNLDNSK LEYWEIHRSA PSYQEQASSQ EILETGIKVI DLICPFSKGG 150
    KVGLFGGAGV GKTVNMMELI RNIAIEHSGY SVFTGVGERT REGNDFYHEM 200
    KDSKVLDKVS LVYGQMNEPP GNRLRVAFTG LTIAEKFRDE GRDVLLFIDN 250
    IYRYTLAGTE VSALLGRMPS AVGYQPTLAE EMGLLQERIT STKEGSITSV 300
    QAVYVPADDL TDPSPATTFA HLDSTVTLSR QIAALGIYPA IDPLNSTSRQ 350
    LDPYIVGDEH YDTARGVQSI LQRYQELKDI IAILGMDELS QEDKILVSRA 400
    RKIQRFLSQP FFVAEVFTGF PGKYVSLKDN IRAFKGIIGG EFDNLPEQAF 450
    YMVGTIEEVI KKAKLL 466
    Length:466
    Mass (Da):51,349
    Last modified:December 15, 1998 - v2
    Checksum:iF0A1570A2DA470D9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti280 – 2801E → G(PubMed:7763501)Curated
    Sequence conflicti280 – 2801E → G1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF008210 Genomic DNA. Translation: AAC38110.1.
    AE013218 Genomic DNA. Translation: AAM67580.1.
    Z15147 Genomic DNA. Translation: CAA78853.1.
    AJ247128 Genomic DNA. Translation: CAB95753.1.
    PIRiS37647.
    RefSeqiNP_660369.1. NC_004061.1.
    WP_011053546.1. NC_004061.1.

    Genome annotation databases

    EnsemblBacteriaiAAM67580; AAM67580; BUsg_008.
    GeneIDi1005596.
    KEGGibas:BUsg008.
    PATRICi21246771. VBIBucAph100086_0008.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF008210 Genomic DNA. Translation: AAC38110.1 .
    AE013218 Genomic DNA. Translation: AAM67580.1 .
    Z15147 Genomic DNA. Translation: CAA78853.1 .
    AJ247128 Genomic DNA. Translation: CAB95753.1 .
    PIRi S37647.
    RefSeqi NP_660369.1. NC_004061.1.
    WP_011053546.1. NC_004061.1.

    3D structure databases

    ProteinModelPortali Q07232.
    SMRi Q07232. Positions 5-466.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 198804.BUsg008.

    Proteomic databases

    PRIDEi Q07232.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM67580 ; AAM67580 ; BUsg_008 .
    GeneIDi 1005596.
    KEGGi bas:BUsg008.
    PATRICi 21246771. VBIBucAph100086_0008.

    Phylogenomic databases

    eggNOGi COG0055.
    KOi K02112.
    OMAi KYLSQPF.
    OrthoDBi EOG6HQSP3.

    Enzyme and pathway databases

    BioCyci BAPH198804:GHMG-8-MONOMER.

    Family and domain databases

    Gene3Di 1.10.1140.10. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPi MF_01347. ATP_synth_beta_bact.
    InterProi IPR003593. AAA+_ATPase.
    IPR020003. ATPase_a/bsu_AS.
    IPR005722. ATPase_F1-cplx_bsu.
    IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
    IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
    IPR004100. ATPase_F1_a/bsu_N.
    IPR024034. ATPase_F1_bsu/V1_C.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR15184:SF8. PTHR15184:SF8. 1 hit.
    Pfami PF00006. ATP-synt_ab. 1 hit.
    PF00306. ATP-synt_ab_C. 1 hit.
    PF02874. ATP-synt_ab_N. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47917. SSF47917. 1 hit.
    SSF50615. SSF50615. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR01039. atpD. 1 hit.
    PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The (F1F0) ATP synthase of Buchnera aphidicola (endosymbiont of aphids): genetic analysis of the putative ATP operon."
      Clark M.A., Baumann P.
      Curr. Microbiol. 35:84-89(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequence analysis of a 34.7-kb DNA segment from the genome of Buchnera aphidicola (endosymbiont of aphids) containing groEL, dnaA, the atp operon, gidA, and rho."
      Clark M.A., Baumann L., Baumann P.
      Curr. Microbiol. 36:158-163(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Sg.
    4. "Aspects of energy-yielding metabolism in the aphid, Schizaphis graminum, and its endosymbiont: detection of gene fragments potentially coding for the ATP synthase beta-subunit and glyceraldehyde-3-phosphate dehydrogenase."
      Clark M.A., Baumann P.
      Curr. Microbiol. 26:233-237(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-314.
    5. "Effect of selection and random drift in the evolution of aphids endosymbionts."
      Latorre A., Buades C., Sabater B., Moya A.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-314.

    Entry informationi

    Entry nameiATPB_BUCAP
    AccessioniPrimary (citable) accession number: Q07232
    Secondary accession number(s): O51872, Q93V14
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 113 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

    Complete proteome

    Documents

    1. Buchnera aphidicola (subsp. Schizaphis graminum)
      Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3