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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
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