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

Gene ID: 948242, updated on 23-Nov-2023

Summary

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Gene symbol
atpA
Gene description
ATP synthase F1 complex subunit alpha
Primary source
ASAP:ABE-0012213
Locus tag
b3734
See related
ECOCYC:EG10098
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. 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
  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. 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
  4. [Cloning and sequencing of the papA gene from uropathogenic Escherichia coli 4030 strain]. Wu Q, et al. Wei Sheng Yan Jiu, 2008 Sep. PMID 19069657
  5. Intrinsic uncoupling in the ATP synthase of Escherichia coli. D'Alessandro M, et al. Biochim Biophys Acta, 2008 Dec. PMID 18952048

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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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 adenyl ribonucleotide binding IEA
Inferred from Electronic Annotation
more info
  
enables nucleotide 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 ATP metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in monoatomic ion transport 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 membrane IEA
Inferred from Electronic Annotation
more info
  
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

    UniProtKB/TrEMBL
    A0A5B9ADW5
    Conserved Domains (1) summary
    PRK09281
    Location:1 → 510
    PRK09281; F0F1 ATP synthase subunit alpha; Validated
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

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Other Literature Sources
Molecular Biology Databases
Research Materials