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    atpD ATP synthase F1 complex subunit beta [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948244, updated on 3-Dec-2024

    Summary

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    Official Symbol
    atpD
    Official Full Name
    ATP synthase F1 complex subunit beta
    Primary source
    ECOCYC:EG10101
    Locus tag
    b3732
    See related
    ASAP:ABE-0012208
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    ECK3725; papB; uncD
    Summary
    Binds TrxA (Kumar, 2004). [More information is available at EcoGene: EG10101]. The beta subunit contains the catalytic site. [More information is available at EcoCyc: EG10101].
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    Genomic context

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    Sequence:
    NC_000913.3 (3915993..3917375, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene fused N-acetylglucosamine-1-phosphate uridyltransferase and glucosamine-1-phosphate acetyltransferase Neighboring gene ATP synthase F1 complex subunit epsilon Neighboring gene ATP synthase F1 complex subunit gamma Neighboring gene ATP synthase F1 complex subunit alpha

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Complementation of mutants in the Escherichia coli proton-translocating ATPase by cloned DNA from Bacillus megaterium. Hawthorne CA, et al. J Biol Chem, 1986 Apr 25. PMID 2870065
    2. The Escherichia coli F1-ATPase mutant beta Tyr-297-->Cys: functional studies and asymmetry of the enzyme under various nucleotide conditions based on reaction of the introduced Cys with N-ethylmaleimide and 7-chloro-4-nitrobenzofurazan. Haughton MA, et al. Biochim Biophys Acta, 1996 Sep 12. PMID 8816947
    3. A mutation in which alanine 128 Is replaced by aspartic acid abolishes dimerization of the b-subunit of the F0F1-ATPase from Escherichia coli. Howitt SM, et al. J Biol Chem, 1996 Mar 22. PMID 8636135
    4. Beta subunit Glu-185 of Escherichia coli H(+)-ATPase (ATP synthase) is an essential residue for cooperative catalysis. Omote H, et al. J Biol Chem, 1995 Oct 27. PMID 7592742
    5. Mutagenesis of residue betaArg-246 in the phosphate-binding subdomain of catalytic sites of Escherichia coli F1-ATPase. Ahmad Z, et al. J Biol Chem, 2004 Jul 23. PMID 15150266

    See all (87) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The results show that beta/gamma rotor-stator interactions near the gamma carboxyl terminus and at the gammaMet23-betaDELSEED both contribute to formation of the rate-limiting transition state of rotational catalysis.
      Title: Binding of phytopolyphenol piceatannol disrupts β/γ subunit interactions and rate-limiting step of steady-state rotational catalysis in Escherichia coli F1-ATPase.
    2. the interaction of F(0)F(1) ATP synthase with FliG is important for the function of the switch of bacterial flagella
      Title: Energy complexes are apparently associated with the switch-motor complex of bacterial flagella.
    3. Homology modeling indicates that the amino acid replacement induces a hydrophobic network, in which the betaMet159, betaIle163, and betaAla167 residues of the beta subunit are involved together with the mutant betaPhe174.
      Title: Roles of the beta subunit hinge domain in ATP synthase F(1) sector: hydrophobic network formed by introduced betaPhe174 inhibits subunit rotation.
    4. The authors identified a knockout of atpD, coding for a component of the F(o)F(1) ATPase, as defective in Ca(2+) efflux.
      Title: ATP regulates calcium efflux and growth in E. coli.
    5. These results imply that the polypeptide in the b N-terminus position is more important for F1 binding than the one in the b C-terminus position and illustrate the significance of the asymmetry of the b dimer in the enzyme.
      Title: Role of the asymmetry of the homodimeric b2 stator stalk in the interaction with the F1 sector of Escherichia coli ATP synthase.
    6. N-terminus verified by Edman degradation on mature peptide
      Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP hydrolysis activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    contributes_to proton-transporting ATP synthase activity, rotational mechanism IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    contributes_to proton-transporting ATP synthase activity, rotational mechanism IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables proton-transporting ATP synthase activity, rotational mechanism IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables proton-transporting ATPase activity, rotational mechanism IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables proton-transporting ATPase activity, rotational mechanism IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in ATP biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in proton motive force-driven ATP synthesis IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in proton motive force-driven plasma membrane ATP synthesis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in proton transmembrane transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in membrane HDA PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in plasma membrane NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    part_of proton-transporting ATP synthase complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of proton-transporting ATP synthase complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    part_of proton-transporting ATP synthase complex, catalytic core F(1) IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of proton-transporting ATP synthase complex, catalytic core F(1) IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of proton-transporting ATP synthase complex, catalytic core F(1) IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    ATP synthase F1 complex subunit beta
    NP_418188.1

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      3915993..3917375 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418188.1 ATP synthase F1 complex subunit beta [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418188.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A7L7EFL4, A0AAN3GZ41
      Conserved Domains (1) summary
      PRK09280
      Location:1 → 460
      PRK09280; F0F1 ATP synthase subunit beta; Validated
    Nucleotide Protein
    Heading Accession and Version

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