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

    Gene ID: 948253, updated on 3-Dec-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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