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

Gene ID: 945987, updated on 11-Jun-2025
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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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 Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

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

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 protein maturation IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in protein maturation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytoplasm IMP
Inferred from Mutant Phenotype
more info
 PubMed 
located_in membrane IEA
Inferred from Electronic Annotation
more info
  
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  
Preferred Names
redox enzyme maturation protein DmsD

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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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