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atpD [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948244, updated on 11-Sep-2024

Summary

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Official Symbol
atpD
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. Binding of phytopolyphenol piceatannol disrupts β/γ subunit interactions and rate-limiting step of steady-state rotational catalysis in Escherichia coli F1-ATPase. Sekiya M, et al. J Biol Chem, 2012 Jun 29. PMID 22582396, Free PMC Article
  2. Roles of the beta subunit hinge domain in ATP synthase F(1) sector: hydrophobic network formed by introduced betaPhe174 inhibits subunit rotation. Nakanishi-Matsui M, et al. Biochem Biophys Res Commun, 2010 Apr 30. PMID 20331967
  3. ATP regulates calcium efflux and growth in E. coli. Naseem R, et al. J Mol Biol, 2009 Aug 7. PMID 19481094
  4. Studies of nucleotide binding to the catalytic sites of Escherichia coli betaY331W-F1-ATPase using fluorescence quenching. Bulygin VV, et al. Proc Natl Acad Sci U S A, 2007 Mar 13. PMID 17360523, Free PMC Article
  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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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
    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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