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    dnaC DNA replication protein DnaC [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948864, updated on 17-Dec-2024

    Summary

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    Official Symbol
    dnaC
    Official Full Name
    DNA replication protein DnaC
    Primary source
    ECOCYC:EG10237
    Locus tag
    b4361
    See related
    ASAP:ABE-0014304
    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
    dnaD; ECK4351
    Summary
    DnaC is an accessory protein that loads the DnaB replicative helicase onto duplex DNA to initiate replication and onto single-stranded DNA to assist in primer formation by primase . [More information is available at EcoCyc: EG10237].
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    Genomic context

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    Sequence:
    NC_000913.3 (4600238..4600975, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene phosphoglycerol transferase I Neighboring gene DUF2501 domain-containing protein YjjA Neighboring gene primosomal protein DnaT Neighboring gene putative succinate exporter YjjB Neighboring gene putative succinate exporter YjjP

    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. Global conformation of the Escherichia coli replication factor DnaC protein in absence and presence of nucleotide cofactors. Galletto R, et al. Biochemistry, 2004 Aug 31. PMID 15323558
    2. Kinetics of allosteric conformational transition of a macromolecule prior to ligand binding: analysis of stopped-flow kinetic experiments. Galletto R, et al. Cell Biochem Biophys, 2005. PMID 15858229
    3. Characterization of dnaC2 and dnaC28 mutants by flow cytometry. Withers HL, et al. J Bacteriol, 1998 Apr. PMID 9537356, Free PMC Article
    4. The nucleotide-binding site of the Escherichia coli DnaC protein: molecular topography of DnaC protein-nucleotide cofactor complexes. Galletto R, et al. Cell Biochem Biophys, 2005. PMID 16244362
    5. The dnaC protein of Escherichia coli. Purification, physical properties and interaction with dnaB protein. Lanka E, et al. Nucleic Acids Res, 1983 Feb 25. PMID 6298736, Free PMC Article

    See all (88) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The molecular coupling between substrate recognition and ATP turnover in a AAA+ hexameric helicase loader.
      Title: The molecular coupling between substrate recognition and ATP turnover in a AAA+ hexameric helicase loader.
    2. Data show how DnaC opens the DnaB ring and represses the helicase prior to DNA binding and how DnaC ATPase activity is reciprocally regulated by DnaB and DNA.
      Title: Physical Basis for the Loading of a Bacterial Replicative Helicase onto DNA.
    3. we propose that DnaC controls the ability of DnaB to interact with primase by modifying the conformation of the N-terminal domain of DnaB
      Title: DnaC, the indispensable companion of DnaB helicase, controls the accessibility of DnaB helicase by primase.
    4. Thus, imbalances in levels of the replicative helicase and helicase loader can inhibit replication both via inhibition of DnaB6-DnaC6 complex formation with excess DnaB, as shown here, and promotion of formation of DnaB6-DnaC6 complexes with excess DnaC.
      Title: Overexpression of the Replicative Helicase in Escherichia coli Inhibits Replication Initiation and Replication Fork Reloading.
    5. Data demonstrate that DnaC opens DnaB by a mechanism akin to that of polymerase clamp loaders and indicate that bacterial replicative helicases, like their eukaryotic counterparts, possess autoregulatory elements that influence how hexameric motor domains are loaded onto and unwind DNA.
      Title: The bacterial DnaC helicase loader is a DnaB ring breaker.
    6. N-terminus verified by Edman degradation on complete protein
      Title: Structure of Escherichia coli dnaC. Identification of a cysteine residue possibly involved in association with dnaB protein.
    7. The complementation of EcDnaC function by HpDnaB in vivo, suggesting that HpDnaB can bypass EcDnaC activity in vivo.
      Title: Helicobacter pylori DnaB helicase can bypass Escherichia coli DnaC function in vivo.
    8. A new dnaC mutation (dnaC824) is reported here that efficiently suppresses priB rep mutant phenotypes.
      Title: A novel dnaC mutation that suppresses priB rep mutant phenotypes in Escherichia coli K-12.
    9. These results suggest that in the presence of ATP in vivo, the DnaB6 x DnaC6 complex should be more efficient in binding DNA as well as in loading DnaB onto the ssDNA than DnaB helicase itself.
      Title: Quantitative analysis of binding of single-stranded DNA by Escherichia coli DnaB helicase and the DnaB x DnaC complex.
    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 ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP hydrolysis activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables DNA binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in DNA replication IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in DNA replication IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in DNA replication initiation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in DNA replication, synthesis of primer IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in DNA replication, synthesis of primer NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    acts_upstream_of_or_within DNA strand elongation involved in DNA replication IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in DNA unwinding involved in DNA replication NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    involved_in replication fork processing NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of DnaB-DnaC complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    part_of DnaB-DnaC-DnaT-PriA-PriB complex NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    part_of DnaB-DnaC-DnaT-PriA-PriC complex NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    part_of DnaB-DnaC-Rep-PriC complex NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    part_of primosome complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of primosome complex NAS
    Non-traceable Author Statement
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    DNA replication protein DnaC

    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
      4600238..4600975 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418781.1 DNA replication protein DnaC [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418781.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5B9AAT9, A0A8T5ZDI4
      Conserved Domains (1) summary
      PRK07952
      Location:1 → 244
      PRK07952; DNA replication protein DnaC; Validated
    Nucleotide Protein
    Heading Accession and Version

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