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    iraD anti-adaptor protein IraD [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948851, updated on 3-Dec-2024

    Summary

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    Official Symbol
    iraD
    Official Full Name
    anti-adaptor protein IraD
    Primary source
    ECOCYC:G7923
    Locus tag
    b4326
    See related
    ASAP:ABE-0014190
    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
    ECK4317; yjiD
    Summary
    IraD inhibits proteolysis of the stationary phase sigma factor S by interacting with RssB, which would normally target S for degradation by the ClpXP protease . [More information is available at EcoCyc: G7923].
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    Genomic context

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    Sequence:
    NC_000913.3 (4556993..4557385)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene DUF2686 domain-containing protein YjiC Neighboring gene protein YtiC Neighboring gene protein YtiD Neighboring gene iraD leader peptide Neighboring gene DNA-binding transcriptional dual regulator HypT Neighboring gene isoaspartyl dipeptidase Neighboring gene Gate family protein YjiG Neighboring gene uncharacterized protein YjiH

    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. A DNA damage response in Escherichia coli involving the alternative sigma factor, RpoS. Merrikh H, et al. Proc Natl Acad Sci U S A, 2009 Jan 13. PMID 19124769, Free PMC Article
    2. Translational Repression of the RpoS Antiadapter IraD by CsrA Is Mediated via Translational Coupling to a Short Upstream Open Reading Frame. Park H, et al. mBio, 2017 Aug 29. PMID 28851853, Free PMC Article
    3. Anti-adaptors use distinct modes of binding to inhibit the RssB-dependent turnover of RpoS (σ(S)) by ClpXP. Micevski D, et al. Front Mol Biosci, 2015. PMID 25988182, Free PMC Article
    4. Growth phase and (p)ppGpp control of IraD, a regulator of RpoS stability, in Escherichia coli. Merrikh H, et al. J Bacteriol, 2009 Dec. PMID 19820090, Free PMC Article
    5. Multi-dimensional gene target search for improving lycopene biosynthesis in Escherichia coli. Jin YS, et al. Metab Eng, 2007 Jul. PMID 17509919

    See all (14) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. crystal structure of RssB bound to an antiadaptor, the DNA damage-inducible IraD; demonstrate that (1) in the presence of IraD, RssB adopts predominantly a closed conformation; (2) IraD contacts both domains of RssB; (3) the interactions observed in the structure are crucial for blocking sigmaS degradation in vivo and in vitro
      Title: Structural basis for inhibition of a response regulator of σ(S) stability by a ClpXP antiadaptor.
    2. findings show that CsrA employs a novel regulatory mechanism to repress translation of iraD; CsrA binds to four sites in the iraD leader transcript but does not directly occlude ribosome binding to the iraD SD sequence; instead, CsrA represses translation of a short open reading frame encoded upstream of iraD, causing repression of iraD translation
      Title: Translational Repression of the RpoS Antiadapter IraD by CsrA Is Mediated via Translational Coupling to a Short Upstream Open Reading Frame.
    3. iraD transcription is induced by DNA damage by a mechanism independent of the SOS response; IraD promoteS accumulation of the alternative transcription sigma factor, RpoS
      Title: A DNA damage response in Escherichia coli involving the alternative sigma factor, RpoS.
    4. These results suggest that the induction of RpoS during transition to stationary phase and by (p)ppGpp occurs at least partially through IraD.
      Title: Growth phase and (p)ppGpp control of IraD, a regulator of RpoS stability, in Escherichia coli.
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    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables anti-sigma factor antagonist activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables anti-sigma factor antagonist 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 damage response IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within DNA damage response IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    involved_in cellular response to oxidative stress IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within negative regulation of protein catabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in positive regulation of DNA-templated transcription IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    anti-adaptor protein IraD

    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
      4556993..4557385
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418746.4 anti-adaptor protein IraD [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418746.4

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8E0KUI3
      Conserved Domains (1) summary
      PRK14128
      Location:54 → 122
      iraD; anti-adapter protein IraD
    Nucleotide Protein
    Heading Accession and Version

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    Other Literature Sources
    Molecular Biology Databases
    Research Materials