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    focA formate channel FocA [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945513, updated on 17-Dec-2024

    Summary

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    Official Symbol
    focA
    Official Full Name
    formate channel FocA
    Primary source
    ECOCYC:EG11258
    Locus tag
    b0904
    See related
    ASAP:ABE-0003073
    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
    ECK0895; ycaE
    Summary
    FocA is a membrane protein with six TM regions. [More information is available at EcoGene: EG11258]. FocA is a putative formate transporter, possibly involved in both formate uptake and efflux. [More information is available at EcoCyc: EG11258].
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    Genomic context

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    Sequence:
    NC_000913.3 (953609..954466, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene pyruvate formate-lyase activating enzyme Neighboring gene pyruvate formate-lyase Neighboring gene ribosomal protein S12 methylthiotransferase accessory factor YcaO Neighboring gene DUF421 domain-containing protein YcaP

    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. Distinguishing functional from structural roles of conserved pore residues during formate translocation by the FocA anion channel. Kammel M, et al. Microbiologyopen, 2022 Aug. PMID 36031960, Free PMC Article
    2. Interplay between the Conserved Pore Residues Thr-91 and His-209 Controls Formate Translocation through the FocA Channel. Kammel M, et al. Microb Physiol, 2022. PMID 35390794
    3. Anaerobic Formate and Hydrogen Metabolism. Pinske C, et al. EcoSal Plus, 2016 Oct. PMID 27735784, Free PMC Article
    4. Pyruvate formate-lyase interacts directly with the formate channel FocA to regulate formate translocation. Doberenz C, et al. J Mol Biol, 2014 Jul 29. PMID 24887098, Free PMC Article
    5. Identification of key residues in the formate channel FocA that control import and export of formate. Hunger D, et al. Biol Chem, 2014 Jul. PMID 24659605

    See all (30) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Role of the Escherichia coli FocA and FocB formate channels in controlling proton/potassium fluxes and hydrogen production during osmotic stress in energy-limited, stationary phase fermenting cells.
      Title: Role of the Escherichia coli FocA and FocB formate channels in controlling proton/potassium fluxes and hydrogen production during osmotic stress in energy-limited, stationary phase fermenting cells.
    2. Distinguishing functional from structural roles of conserved pore residues during formate translocation by the FocA anion channel.
      Title: Distinguishing functional from structural roles of conserved pore residues during formate translocation by the FocA anion channel.
    3. Interplay between the Conserved Pore Residues Thr-91 and His-209 Controls Formate Translocation through the FocA Channel.
      Title: Interplay between the Conserved Pore Residues Thr-91 and His-209 Controls Formate Translocation through the FocA Channel.
    4. Our results suggest that regulation of formate translocation direction by FocA/FocB channels is important for maintaining internal pH and proton motive force by modulating H2 production.
      Title: pH and a mixed carbon-substrate spectrum influence FocA- and FocB-dependent, formate-driven H2 production in Escherichia coli.
    5. in vivo competitive assays showed that one of the second steps (focA) exhibited positive epistasis with the first, while another (dcuB) exhibited negative epistasis. The data shows that strong effect adaptive mutations continuously recur in gut commensal bacterial species.
      Title: A Mutational Hotspot and Strong Selection Contribute to the Order of Mutations Selected for during Escherichia coli Adaptation to the Gut.
    6. Highly conserved amino acid residues within FocA identified in structural studies are predicted to be important in the control of formate translocation.
      Title: Identification of key residues in the formate channel FocA that control import and export of formate.
    7. FocA has a strong preference for formate as a substrate in vivo and not other acidic fermentation products and the tight coupling between FocA and PflB synthesis ensures adequate substrate delivery to the appropriate formate dehydrogenase.
      Title: Coordination of FocA and pyruvate formate-lyase synthesis in Escherichia coli demonstrates preferential translocation of formate over other mixed-acid fermentation products.
    8. Analysis of the oligomeric state by blue-native polyacrylamide gel electrophoresis revealed FocA to have an unexpected pentameric quaternary structure.
      Title: Unexpected oligomeric structure of the FocA formate channel of Escherichia coli : a paradigm for the formate-nitrite transporter family of integral membrane proteins.
    9. Deletion of the E. coli focA gene (together with deletions of other ferementation disruption genes) increased production of succinate
      Title: Eliminating side products and increasing succinate yields in engineered strains of Escherichia coli C.
    Submit: New GeneRIF Correction

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables formate transmembrane transporter activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables formate transmembrane transporter activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables formate transmembrane transporter activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables identical protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in formate transport IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in formate transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in formate transport IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in mixed acid fermentation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in response to acidic pH TAS
    Traceable Author Statement
    more info
    		 PubMed 
    involved_in transmembrane transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in plasma membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in plasma membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in plasma membrane ISM
    Inferred from Sequence Model
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    formate channel FocA

    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
      953609..954466 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415424.1 formate channel FocA [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415424.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A090J485
      Conserved Domains (1) summary
      PRK10805
      Location:1 → 285
      PRK10805; formate transporter; Provisional
    Nucleotide Protein
    Heading Accession and Version

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