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    umuD DNA polymerase V protein UmuD [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945746, updated on 3-Dec-2024

    Summary

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    Official Symbol
    umuD
    Official Full Name
    DNA polymerase V protein UmuD
    Primary source
    ECOCYC:EG11057
    Locus tag
    b1183
    See related
    ASAP:ABE-0003974
    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
    ECK1171
    Summary
    LexA regulon. [More information is available at EcoGene: EG11057]. Following induction of the SOS response, UmuD is proteolytically processed into UmuD' in a cleavage reaction that depends on activated RecA . [More information is available at EcoCyc: EG11057].
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    Genomic context

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    Sequence:
    NC_000913.3 (1230767..1231186)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative metal-chelating domain-containing protein YcgN Neighboring gene hemolysin E Neighboring gene DNA polymerase V catalytic protein Neighboring gene protein thiol:quinone oxidoreductase DsbB

    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. The dimeric SOS mutagenesis protein UmuD is active as a monomer. Ollivierre JN, et al. J Biol Chem, 2011 Feb 4. PMID 21118802, Free PMC Article
    2. Structure of the UmuD' protein and its regulation in response to DNA damage. Peat TS, et al. Nature, 1996 Apr 25. PMID 8614470
    3. Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products. Simon SM, et al. Proc Natl Acad Sci U S A, 2008 Jan 29. PMID 18216271, Free PMC Article
    4. Targeting of the UmuD, UmuD', and MucA' mutagenesis proteins to DNA by RecA protein. Frank EG, et al. Proc Natl Acad Sci U S A, 1993 Sep 1. PMID 8367479, Free PMC Article
    5. Subunit-specific degradation of the UmuD/D' heterodimer by the ClpXP protease: the role of trans recognition in UmuD' stability. Gonzalez M, et al. EMBO J, 2000 Oct 2. PMID 11013227, Free PMC Article

    See all (164) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Tracking Escherichia coli DNA polymerase V to the entire genome during the SOS response.
      Title: Tracking Escherichia coli DNA polymerase V to the entire genome during the SOS response.
    2. Single-molecule fluorescence microscopy reveals modulation of DNA polymerase IV-binding lifetimes by UmuD (K97A) and UmuD'.
      Title: Single-molecule fluorescence microscopy reveals modulation of DNA polymerase IV-binding lifetimes by UmuD (K97A) and UmuD'.
    3. A Comprehensive View of Translesion Synthesis in Escherichia coli.
      Title: A Comprehensive View of Translesion Synthesis in Escherichia coli.
    4. DNA binding and synthesis cannot occur until pol V interacts with a RecA nucleoprotein filament (RecA*) and ATP to form a mutasome complex, pol V Mut = UmuD'2C-RecA-ATP.
      Title: Conformational regulation of Escherichia coli DNA polymerase V by RecA and ATP.
    5. There are multiple levels of regulation imposed on pol V including transcriptional control, posttranslational modification, targeted proteolysis, activation of the catalytic activity of pol V through protein-protein interactions and the very recently described intracellular spatial regulation of pol V. (Review)
      Title: Insights into the complex levels of regulation imposed on Escherichia coli DNA polymerase V.
    6. The current study delves deeper into this process, initiating the task of mapping out the molecular details of the interaction between RecA and UmuD'2C
      Title: A RecA protein surface required for activation of DNA polymerase V.
    7. The results suggest that competition between UmuD and ssDNA for DNA polymerase III alpha binding is a new mechanism for polymerase exchange.
      Title: Polymerase manager protein UmuD directly regulates Escherichia coli DNA polymerase III α binding to ssDNA.
    8. Like the self-cleaving serine proteases LexA and UmuD in Escherichia coli, UmuDAb required RecA for cleavage.
      Title: The Acinetobacter regulatory UmuDAb protein cleaves in response to DNA damage with chimeric LexA/UmuD characteristics.
    9. Authors propose that the interaction between DNA polymerase III alpha and UmuD contributes to the transition between replicative and translesion synthesis polymerases by removing DNA polymerase III alpha from the beta clamp.
      Title: Selective disruption of the DNA polymerase III α-β complex by the umuD gene products.
    10. Electron paramagnetic resonance (EPR) spectroscopy study determined that the arms of UmuD2 display a large degree of motion, are largely unbound from the globular C-terminal domain, and that the free energy of dissociation is 2.1 kJ mol-1
      Title: Electron spin labeling reveals the highly dynamic N-terminal arms of the SOS mutagenesis protein UmuD.
    Submit: New GeneRIF Correction See all GeneRIFs (19)

    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-dependent activity, acting on DNA IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables DNA binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables DNA-directed DNA polymerase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables nucleic acid binding EXP
    Inferred from Experiment
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables serine-type peptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables single-stranded DNA binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in DNA damage response IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    involved_in DNA repair IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in DNA repair IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in SOS response IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in SOS response IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in regulation of DNA-templated transcription IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in translesion synthesis IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of DNA polymerase V complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytosol IC
    Inferred by Curator
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    DNA polymerase V protein UmuD
    NP_415701.1

    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
      1230767..1231186
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415701.1 DNA polymerase V protein UmuD [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415701.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S0FWZ5
      Conserved Domains (1) summary
      PRK10276
      Location:1 → 139
      PRK10276; translesion error-prone DNA polymerase V autoproteolytic subunit
    Nucleotide Protein
    Heading Accession and Version

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