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    dmsD redox enzyme maturation protein DmsD [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945987, updated on 3-Dec-2024

    Summary

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    Official Symbol
    dmsD
    Official Full Name
    redox enzyme maturation protein DmsD
    Primary source
    ECOCYC:G6849
    Locus tag
    b1591
    See related
    ASAP:ABE-0005314
    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
    ECK1586; ynfI
    Summary
    dmsD is the fifth gene in the dmsABC-like operon ynfEFGH-dmsD. torD, dmsD and ycdY are paralogs.Overexpressed YdcY and DmsD interfere with apoTorA maturation by TorD, independent of the TorA signal peptide (Ilbert, 2004). [More information is available at EcoGene: EG13847]. DmsD binds to the twin-arginine leaders of certain proteins, including dimethylsulfoxide (DMSO) reductase and trimethylamine N-oxide (TMAO) reductase that are translocated to the cytoplasmic membrane for the periplasm by the Sec-independent system that is termed Mtt (membrane targeting and transport) or more frequently Tat (twin-arginine translocation) . [More information is available at EcoCyc: G6849].
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    Genomic context

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    Sequence:
    NC_000913.3 (1664506..1665120)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative oxidoreductase YnfG Neighboring gene putative menaquinol dehydrogenase Neighboring gene putative chloride:H(+) antiporter ClcB Neighboring gene dethiobiotin synthetase BidA Neighboring gene DNA-binding transcriptional repressor Mlc

    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. Influence of GTP on system specific chaperone - Twin arginine signal peptide interaction. Cherak SJ, et al. Biochem Biophys Res Commun, 2015 Oct 2. PMID 26299930
    2. Folding forms of Escherichia coli DmsD, a twin-arginine leader binding protein. Sarfo KJ, et al. Biochem Biophys Res Commun, 2004 Mar 5. PMID 14766221
    3. DmsD is required for the biogenesis of DMSO reductase in Escherichia coli but not for the interaction of the DmsA signal peptide with the Tat apparatus. Ray N, et al. FEBS Lett, 2003 Jan 16. PMID 12527378
    4. Structural analysis of a monomeric form of the twin-arginine leader peptide binding chaperone Escherichia coli DmsD. Stevens CM, et al. J Mol Biol, 2009 May 29. PMID 19361518, Free PMC Article
    5. Structure of the twin-arginine signal-binding protein DmsD from Escherichia coli. Ramasamy SK, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2009 Aug 1. PMID 19652330, Free PMC Article

    See all (27) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. utilized the in vitro protein-protein interaction technique of an affinity pull down assay, as well as protein thermal stability measurement via differential scanning fluorimetry to investigate the interaction of guanosine nucleotides with DmsD
      Title: Influence of GTP on system specific chaperone - Twin arginine signal peptide interaction.
    2. Data suggest that a portion of the hydrophobic region of the DmsA (dimethyl sulfoxide reductase, subunit A) leader peptide determines the specificity of binding and may produce helical properties upon binding to DmsD.
      Title: The hydrophobic region of the DmsA twin-arginine leader peptide determines specificity with chaperone DmsD.
    3. analysis of DmsD (specific for dimethylsulfoxide reductase, DmsA) and TorD (specific for trimethylamine N-oxide reductase, TorA).
      Title: The hydrophobic core of twin-arginine signal sequences orchestrates specific binding to Tat-pathway related chaperones.
    4. DmsD protein is required for reduction of selenate.
      Title: A genetic analysis of in vivo selenate reduction by Salmonella enterica serovar Typhimurium LT2 and Escherichia coli K12.
    5. Results illustrate the positions of important DmsD residues involved in binding the DmsA leader peptide and identify a "hot pocket" of residues important for leader binding on the structure of DmsD.
      Title: Identification of residues in DmsD for twin-arginine leader peptide binding, defined through random and bioinformatics-directed mutagenesis.
    6. N-terminus verified by Edman degradation on mature peptide
      Title: Identification of a twin-arginine leader-binding protein.
    Submit: New GeneRIF Correction

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables signal sequence binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in chaperone-mediated protein folding IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein maturation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytoplasm IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    redox enzyme maturation protein DmsD

    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
      1664506..1665120
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416108.2 redox enzyme maturation protein DmsD [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416108.2

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A2H4TZR9
      Conserved Domains (1) summary
      PRK11621
      Location:1 → 204
      PRK11621; Tat proofreading chaperone DmsD
    Nucleotide Protein
    Heading Accession and Version

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