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    uvrA UvrABC excision nuclease subunit A [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948559, updated on 3-Dec-2024

    Summary

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    Official Symbol
    uvrA
    Official Full Name
    UvrABC excision nuclease subunit A
    Primary source
    ECOCYC:EG11061
    Locus tag
    b4058
    See related
    ASAP:ABE-0013290
    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
    dar; dinE; ECK4050
    Summary
    UvrA is a subunit of the UvrABC nucleotide excision repair (NER) generalized DNA repair process. [More information is available at EcoCyc: EG11061].
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    Genomic context

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    Sequence:
    NC_000913.3 (4271049..4273871, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene PF01894 family protein YjbQ Neighboring gene PF04237 family protein YjbR Neighboring gene ssDNA-binding protein Neighboring gene uncharacterized protein YjcB

    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. Understanding the coupling between DNA damage detection and UvrA's ATPase using bulk and single molecule kinetics. Barnett JT, et al. FASEB J, 2019 Jan. PMID 30020831, Free PMC Article
    2. Isolation and characterization of functional domains of UvrA. Myles GM, et al. Biochemistry, 1991 Apr 23. PMID 1826851
    3. Evidence from extended X-ray absorption fine structure and site-specific mutagenesis for zinc fingers in UvrA protein of Escherichia coli. Navaratnam S, et al. J Biol Chem, 1989 Sep 25. PMID 2550431
    4. Superhelical stress restrained in plasmid DNA during repair synthesis initiated by the UvrA, B and C proteins in vitro. Backendorf C, et al. Nucleic Acids Res, 1989 Dec 25. PMID 2557590, Free PMC Article
    5. Sequences of Escherichia coli uvrA gene and protein reveal two potential ATP binding sites. Husain I, et al. J Biol Chem, 1986 Apr 15. PMID 3007478

    See all (105) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Real-time investigation of the roles of ATP hydrolysis by UvrA and UvrB during DNA damage recognition in nucleotide excision repair.
      Title: Real-time investigation of the roles of ATP hydrolysis by UvrA and UvrB during DNA damage recognition in nucleotide excision repair.
    2. UV-irradiated Escherichia coli cells with a recN mutation did not exhibit increased nucleoid condensation, but chromosome replication and cytokinesis occurred. In the uvrA and recJ strains, the condensation step was delayed compared to the wild-type strain, and chromosome replication and cytokinesis did not occur.
      Title: Influence of uvrA, recJ and recN gene mutations on nucleoid reorganization in UV-treated Escherichia coli cells.
    3. suggest that UvrA uses negative cooperativity between its ATPase sites that is gated by damage recognition
      Title: Understanding the coupling between DNA damage detection and UvrA's ATPase using bulk and single molecule kinetics.
    4. Recruitment of UvrBC complexes to UV-induced damage in the absence of UvrA increases bacterial survival.
      Title: Recruitment of UvrBC complexes to UV-induced damage in the absence of UvrA increases cell survival.
    5. The movement of beta-hairpin in the third zinc-binding module of UvrA (Zn3hp) is required for damage-specific binding, UvrB loading and ATPase activities of UvrA. The conformational change of Zn3hp is controlled by ATP hydrolysis at the distal nucleotide binding site. A bi-phasic damage inspection model of UvrA was proposed in which movement of the Zn3hp plays a key role in damage recognition.
      Title: Movement of the β-hairpin in the third zinc-binding module of UvrA is required for DNA damage recognition.
    6. study visualized how UvrA and UvrB interacted with DNA individually or together by single- molecule imaging of quantum-dot-labeled proteins
      Title: Collaborative dynamic DNA scanning by nucleotide excision repair proteins investigated by single- molecule imaging of quantum-dot-labeled proteins.
    7. UvrA is induced after UV irradiation. UvrA levels decrease principally as a result of ClpXP-dependent protein degradation.
      Title: Controlled degradation by ClpXP protease tunes the levels of the excision repair protein UvrA to the extent of DNA damage.
    8. N-terminus verified by Edman degradation on complete protein
      Title: Sequences of Escherichia coli uvrA gene and protein reveal two potential ATP binding sites.
    9. In solution, two UvrB subunits bind to UvrA, most likely as part of a UvrA2B2 complex. The UvrA-induced dimerization of the C-terminal domain 4 regions of UvrB serves to shield these domains from premature UvrC binding.
      Title: Dynamics of the UvrABC nucleotide excision repair proteins analyzed by fluorescence resonance energy transfer.
    10. we examined the interaction of UvrABC with a DNA substrate containing a single G[8,5-Me]T cross-link and compared it with T[6,4]T (the 6-4 pyrimidine-pyrimidone photoproduct) and the C8 guanine adduct of N-acetyl-2-aminofluorene (AAF)
      Title: Recognition and incision of gamma-radiation-induced cross-linked guanine-thymine tandem lesion G[8,5-Me]T by UvrABC nuclease.
    Submit: New GeneRIF Correction See all GeneRIFs (11)

    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 IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP hydrolysis activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables DNA binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables DNA binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables catalytic activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables excinuclease ABC activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables nuclease activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables zinc ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in DNA repair IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within DNA repair IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in SOS response IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in nucleotide-excision repair IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in nucleotide-excision repair NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    involved_in nucleotide-excision repair, DNA damage recognition IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in nucleotide-excision repair, preincision complex assembly NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    acts_upstream_of_or_within response to radiation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of DNA repair complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of excinuclease repair complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of excinuclease repair complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of excinuclease repair complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    UvrABC excision nuclease subunit A

    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
      4271049..4273871 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418482.1 UvrABC excision nuclease subunit A [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418482.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376ME40, A0A8S7EBZ6
      Conserved Domains (1) summary
      PRK00349
      Location:1 → 940
      uvrA; excinuclease ABC subunit UvrA
    Nucleotide Protein
    Heading Accession and Version

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