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

    Gene ID: 948242, updated on 3-Dec-2024

    Summary

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    Official Symbol
    atpA
    Official Full Name
    ATP synthase F1 complex subunit alpha
    Primary source
    ECOCYC:EG10098
    Locus tag
    b3734
    See related
    ASAP:ABE-0012213
    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
    ECK3727; papA; uncA
    Summary
    Binds TrxA (Kumar, 2004). [More information is available at EcoGene: EG10098]. The -subunit plays an essential role in the catalytic mechanism of the enzyme and in the binding and coupling between the F1 and F0 complexes. [More information is available at EcoCyc: EG10098].
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    Genomic context

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    Sequence:
    NC_000913.3 (3918316..3919857, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene ATP synthase F1 complex subunit beta Neighboring gene ATP synthase F1 complex subunit gamma Neighboring gene ATP synthase F1 complex subunit delta Neighboring gene ATP synthase Fo complex subunit b

    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. The atp operon: nucleotide sequence of the region encoding the alpha-subunit of Escherichia coli ATP-synthase. Gay NJ, et al. Nucleic Acids Res, 1981 May 11. PMID 6272228, Free PMC Article
    2. F1-ATPase of Escherichia coli: the ε- inhibited state forms after ATP hydrolysis, is distinct from the ADP-inhibited state, and responds dynamically to catalytic site ligands. Shah NB, et al. J Biol Chem, 2013 Mar 29. PMID 23400782, Free PMC Article
    3. Functional importance of αAsp-350 in the catalytic sites of Escherichia coli ATP synthase. Raheem S, et al. Arch Biochem Biophys, 2019 Sep 15. PMID 31330132, Free PMC Article
    4. Single molecule measurements of F1-ATPase reveal an interdependence between the power stroke and the dwell duration. Spetzler D, et al. Biochemistry, 2009 Aug 25. PMID 19610671, Free PMC Article
    5. Ultrafast purification and reconstitution of His-tagged cysteine-less Escherichia coli F1Fo ATP synthase. Ishmukhametov RR, et al. Biochim Biophys Acta, 2005 Jan 7. PMID 15620371

    See all (96) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Asp(350) residue is required for orthophosphate binding in the catalytic site of F1F0 ATP synthase.
      Title: Functional importance of αAsp-350 in the catalytic sites of Escherichia coli ATP synthase.
    2. in the F1-ATPase of Escherichia coli, the epsilon- inhibited state forms after ATP hydrolysis, is distinct from the ADP-inhibited state, and responds dynamically to catalytic site ligands
      Title: F1-ATPase of Escherichia coli: the ε- inhibited state forms after ATP hydrolysis, is distinct from the ADP-inhibited state, and responds dynamically to catalytic site ligands.
    3. UPEC4030 strain could contain an unknown papA variant or the novel genotype.
      Title: [Cloning and sequencing of the papA gene from uropathogenic Escherichia coli 4030 strain].
    4. The P pilus usher PapC R652 is important for high-affinity binding to the adhesin whereas F21 is important for limiting affinity for the PapA major rod subunit.
      Title: The differential affinity of the usher for chaperone-subunit complexes is required for assembly of complete pili.
    5. During assembly of ATP synthase, alpha/delta subunit interaction is an important facet of proton pumping stator subunit structure and function.
      Title: Assembly of the stator in Escherichia coli ATP synthase. Complexation of alpha subunit with other F1 subunits is prerequisite for delta subunit binding to the N-terminal region of alpha.
    6. 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.
    7. Cys substitutions were introduced into two different transmembrane helices (TMHs) of subunit a, and the proximity of the thiol side chains was tested via attempted oxidative cross-linking to form the disulfide bond.
      Title: Cross-linking between helices within subunit a of Escherichia coli ATP synthase defines the transmembrane packing of a four-helix bundle.
    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 ADP binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ATP binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ATP binding 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
    		  
    enables proton-transporting ATP synthase activity, rotational mechanism IEA
    Inferred from Electronic Annotation
    more info
    		  
    contributes_to proton-transporting ATPase activity, rotational mechanism IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables proton-transporting ATPase activity, rotational mechanism IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in ATP biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in proton motive force-driven ATP synthesis IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in proton motive force-driven ATP synthesis IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within proton motive force-driven 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
    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 alpha
    NP_418190.1

    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
      3918316..3919857 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418190.1 ATP synthase F1 complex subunit alpha [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418190.1

      Status: PROVISIONAL

      Conserved Domains (1) summary
      PRK09281
      Location:1 → 510
      PRK09281; F0F1 ATP synthase subunit alpha; Validated
    Nucleotide Protein
    Heading Accession and Version

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