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

Gene ID: 948253, updated on 19-Sep-2024

Summary

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Official Symbol
atpE
Official Full Name
ATP synthase Fo complex subunit c
Primary source
ECOCYC:EG10102
Locus tag
b3737
See related
ASAP:ABE-0012220
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
ECK3730; papH; uncE
Summary
The c subunit of the F0 complex of ATP synthase is absolutely required for proton translocation and is also necessary for binding of the F-1 complex. [More information is available at EcoCyc: EG10102].
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Genomic context

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Sequence:
NC_000913.3 (3920950..3921189, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene ATP synthase F1 complex subunit delta Neighboring gene ATP synthase Fo complex subunit b Neighboring gene ATP synthase Fo complex subunit a Neighboring gene ATP synthase accessory factor AtpI

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. Tracking protons from respiratory chain complexes to ATP synthase c-subunit: The critical role of serine and threonine residues. Panfoli I, et al. Biochem Biophys Res Commun, 2017 Jan 22. PMID 27890618
  2. Structure of Ala(20) --> Pro/Pro(64) --> Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helices. Dmitriev OY, et al. J Biol Chem, 2001 Jul 20. PMID 11331283
  3. The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10. Jiang W, et al. Proc Natl Acad Sci U S A, 2001 Apr 24. PMID 11320246, Free PMC Article
  4. Introduction of a carboxyl group in the first transmembrane helix of Escherichia coli F1Fo ATPase subunit c and cytoplasmic pH regulation. Jones PC. J Bacteriol, 2001 Mar. PMID 11160082, Free PMC Article
  5. Phospholipids occupy the internal lumen of the c ring of the ATP synthase of Escherichia coli. Oberfeld B, et al. Biochemistry, 2006 Feb 14. PMID 16460030

See all (96) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. This study analyzed in detail the H+ pathway in the perspective to update the chemiosmotic theory. The study is based on structural computer simulations on the subunit a/c complex of E. coli. This study allowed to identify a plausible H+ pathway taking into consideration the hydrogen-bonded chain mechanism, thereby excluding the contribution of water molecules.
    Title: Tracking protons from respiratory chain complexes to ATP synthase c-subunit: The critical role of serine and threonine residues.
  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. characterization of the monomer and ring presented in this work sheds light into the structural dynamics of the c-subunit and its functional relevance.
    Title: Simulations of the c-subunit of ATP-synthase reveal helix rearrangements.
  4. Cross-linking pattern stop sharply with a c10 oligomer irrespective of the presence or absence of the other subunits of the ATP synthase complex.
    Title: Constant c10 ring stoichiometry in the Escherichia coli ATP synthase analyzed by cross-linking.
  5. The 4D and 5D spectral information obtained rapidly from GFT and G(2)FT NMR experiments enables one to efficiently obtain (nearly) complete resonance assignments of membrane proteins.
    Title: GFT projection NMR based resonance assignment of membrane proteins: application to subunit C of E. coli F(1)F (0) ATP synthase in LPPG micelles.
  6. The polar loop of subunit c of the Escherichia coli ATP synthase stabilizes the hairpin structure of this protein.
    Title: The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c.
  7. N-terminus verified by Edman degradation on complete protein
    Title: Amino acid replacement in dicyclohexylcarbodiimide-reactive proteins from mutant strains of Escherichia coli defective in the energy-transducing ATPase complex.
  8. Two mutants of F(0) subunit C unable to form a functional F(1)F(0) ATPase interact with YidC, require YidC for membrane insertion, but fail to oligomerize.
    Title: YidC-mediated membrane insertion of assembly mutants of subunit c of the F1F0 ATPase.
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 lipid binding IEA
Inferred from Electronic Annotation
more info
  
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 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 IBA
Inferred from Biological aspect of Ancestor
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 
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 c
NP_418193.1

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
    3920950..3921189 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_418193.1 ATP synthase Fo complex subunit c [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_418193.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8S0FIG7
    Conserved Domains (1) summary
    PRK06876
    Location:2 → 79
    PRK06876; F0F1 ATP synthase subunit C; Validated
Nucleotide Protein
Heading Accession and Version

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