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

    Gene ID: 948252, updated on 3-Dec-2024

    Summary

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    Official Symbol
    atpB
    Official Full Name
    ATP synthase Fo complex subunit a
    Primary source
    ECOCYC:EG10099
    Locus tag
    b3738
    See related
    ASAP:ABE-0012222
    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
    ECK3731; papD; uncB
    Summary
    The a subunit of the F0 complex plays a critical role in the proton translocation mechanism . [More information is available at EcoCyc: EG10099].
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    Genomic context

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    Sequence:
    NC_000913.3 (3921236..3922051, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene ATP synthase Fo complex subunit b Neighboring gene ATP synthase Fo complex subunit c Neighboring gene ATP synthase accessory factor AtpI Neighboring gene 16S rRNA m(7)G527 methyltransferase

    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. Transmembrane topology of Escherichia coli H(+)-ATPase (ATP synthase) subunit a. Yamada H, et al. FEBS Lett, 1996 Jul 15. PMID 8706824
    2. Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR. Bann JG, et al. Biochemistry, 2004 Nov 2. PMID 15504040
    3. The ion channel of F-ATP synthase is the target of toxic organotin compounds. von Ballmoos C, et al. Proc Natl Acad Sci U S A, 2004 Aug 3. PMID 15277681, Free PMC Article
    4. Backbone 1H, 15N and 13C assignments for the subunit a of the E. coli ATP synthase. Dmitriev OY, et al. J Biomol NMR, 2004 Jul. PMID 15213458
    5. The role of transmembrane span 2 in the structure and function of subunit a of the ATP synthase from Escherichia coli. DeLeon-Rangel J, et al. Arch Biochem Biophys, 2003 Oct 1. PMID 13679083

    See all (89) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. 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.
    2. Interaction with monomeric subunit c drives insertion of ATP synthase subunit a into the membrane and primes a-c complex formation
      Title: Interaction with monomeric subunit c drives insertion of ATP synthase subunit a into the membrane and primes a-c complex formation.
    3. helices fold back on themselves in a chloroform-methanol-H2O (4:4:1) solvent mixture and then pack at an angle such that the cytoplasmic ends of the polypeptide backbone are significantly displaced from each other.
      Title: Interaction of transmembrane helices in ATP synthase subunit a in solution as revealed by spin label difference NMR.
    4. Data indicate that both the N- and C-terminal domains of PapD must fold into a native conformation prior to the formation of domain-domain interactions.
      Title: Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
    5. NMR assignments for the subunit a of the E. coli ATP synthase
      Title: Backbone 1H, 15N and 13C assignments for the subunit a of the E. coli ATP synthase.
    6. molecular probes defined five transmembrane helices, the orientation of the protein in the membrane, and information about the relative exposure of the loops connecting these helices
      Title: Structure and function of subunit a of the ATP synthase of Escherichia coli.
    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 IBA
    Inferred from Biological aspect of Ancestor
    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 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 IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within proton motive force-driven plasma membrane ATP synthesis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    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
    is_active_in plasma membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in plasma membrane IDA
    Inferred from Direct Assay
    more info
    		 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 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 a
    NP_418194.1

    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
      3921236..3922051 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418194.1 ATP synthase Fo complex subunit a [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418194.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A6N0IK99
      Conserved Domains (1) summary
      PRK05815
      Location:38 → 271
      PRK05815; F0F1 ATP synthase subunit A; Validated
    Nucleotide Protein
    Heading Accession and Version

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