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    atpF ATP synthase Fo complex subunit b [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948247, updated on 3-Dec-2024

    Summary

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    Official Symbol
    atpF
    Official Full Name
    ATP synthase Fo complex subunit b
    Primary source
    ECOCYC:EG10103
    Locus tag
    b3736
    See related
    ASAP:ABE-0012217
    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
    ECK3729; papF; uncF
    Summary
    The b subunit complex is involved in binding the F-1 complex to the F-O complex and is necessary for the assembly of the F-O complex. [More information is available at EcoCyc: EG10103].
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    Genomic context

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    Sequence:
    NC_000913.3 (3920418..3920888, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene ATP synthase F1 complex subunit alpha Neighboring gene ATP synthase F1 complex subunit delta Neighboring gene ATP synthase Fo complex subunit c Neighboring gene ATP synthase Fo complex subunit a

    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. Residue 249 in subunit beta regulates ADP inhibition and its phosphate modulation in Escherichia coli ATP synthase. Lapashina AS, et al. Biochim Biophys Acta Bioenerg, 2019 Mar 1. PMID 30528692
    2. Dimerization interactions of the b subunit of the Escherichia coli F1F0-ATPase. McLachlin DT, et al. J Biol Chem, 1997 Aug 22. PMID 9261132
    3. Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase. Dmitriev O, et al. J Biol Chem, 1999 May 28. PMID 10336456
    4. The dimerization domain of the b subunit of the Escherichia coli F(1)F(0)-ATPase. Revington M, et al. J Biol Chem, 1999 Oct 22. PMID 10521510
    5. Integration of b subunits of unequal lengths into F1F0-ATP synthase. Grabar TB, et al. J Biol Chem, 2003 Sep 12. PMID 12842903

    See all (89) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Mutation betaL249Q significantly enhanced ADP-inhibition in E. coli ATP synthase, increased the extent of ATP hydrolysis stimulation by sulfite, and rendered the ADP-inhibition sensitive to phosphate in the same manner as observed in FOF1 from mitochondria, chloroplasts, and most aerobic\photosynthetic bacteria.
      Title: Residue 249 in subunit beta regulates ADP inhibition and its phosphate modulation in Escherichia coli ATP synthase.
    2. Data indicate the juxtaposition of subunits b and a in the ATP synthase.
      Title: Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linking.
    3. The first solution structure of b30-82, including the tether region and part of the dimerization domain, has been solved by nuclear magnetic resonance, revealing an alpha-helix between residues 39 and 72.
      Title: Solution structure, determined by nuclear magnetic resonance, of the b30-82 domain of subunit b of Escherichia coli F1Fo ATP synthase.
    4. N-terminus verified by Edman degradation on complete protein
      Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
    5. the b subunit of ATP synthase serves an active function in energy coupling rather than just holding on to the F1 sector
      Title: Mutations in the dimerization domain of the b subunit from the Escherichia coli ATP synthase. Deletions disrupt function but not enzyme assembly.
    6. The results indicate a right-handed coiled-coil structure with intrinsic asymmetry, the two helices being offset rather than in register. A function for the right-handed coiled coil in rotational catalysis is proposed.
      Title: ATP synthase b subunit dimerization domain: a right-handed coiled coil with offset helices.
    7. subunit b dimer of the FOF1-ATP synthase interacts with F1-ATPase
      Title: The subunit b dimer of the FOF1-ATP synthase: interaction with F1-ATPase as deduced by site-specific spin-labeling.
    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 proton transmembrane transporter activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables proton-transporting ATP synthase activity, rotational mechanism IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables proton-transporting ATP synthase activity, rotational mechanism IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    contributes_to proton-transporting ATPase activity, rotational mechanism IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    contributes_to proton-transporting ATPase activity, rotational mechanism IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    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 plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in plasma membrane NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    located_in plasma membrane RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 
    part_of proton-transporting ATP synthase complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    part_of proton-transporting ATP synthase complex, coupling factor F(o) IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of proton-transporting ATP synthase complex, coupling factor F(o) IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of proton-transporting ATP synthase complex, coupling factor F(o) IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    ATP synthase Fo complex subunit b
    NP_418192.1

    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
      3920418..3920888 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418192.1 ATP synthase Fo complex subunit b [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418192.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376MF99
      Conserved Domains (1) summary
      PRK05759
      Location:1 → 156
      PRK05759; F0F1 ATP synthase subunit B; Validated
    Nucleotide Protein
    Heading Accession and Version

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