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dsbD thiol-disulfide exchange protein DsbD [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948649, updated on 30-Jul-2025
Official Symbol
dsbD
Official Full Name
thiol-disulfide exchange protein DsbD
Primary source
ECOCYC:EG12178
Locus tag
b4136
See related
ASAP:ABE-0013539
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
cutA2; cycZ; dipZ; ECK4130; htrI
Summary
DsbD is required for the formation of disulfide bonds in some periplasmic proteins and for the assembly of C-type cytochromes in the periplasm. [More information is available at EcoGene: EG12178]. The crystal structure of DsbD has been determined to a resolution of 2.85 . [More information is available at EcoCyc: EG12178].
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Sequence:
NC_000913.3 (4363345..4365042, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene tRNA-Phe Neighboring gene DNA-binding transcriptional regulator DicD Neighboring gene copper binding protein CutA Neighboring gene C4-dicarboxylate transporter DcuA Neighboring gene ncRNA Neighboring gene aspartate ammonia-lyase

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Local frustration determines loop opening during the catalytic cycle of an oxidoreductase. Stelzl LS, et al. Elife, 2020 Jun 22. PMID 32568066, Free PMC Article
  2. Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function. Gordon EH, et al. Mol Microbiol, 2000 Mar. PMID 10760137
  3. Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD. Katzen F, et al. EMBO J, 2002 Aug 1. PMID 12145197, Free PMC Article
  4. Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity(1). Kim JH, et al. FEBS Lett, 2003 May 22. PMID 12753926
  5. Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD. Katzen F, et al. Proc Natl Acad Sci U S A, 2003 Sep 2. PMID 12925743, Free PMC Article

See all (69) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Local frustration determines loop opening during the catalytic cycle of an oxidoreductase.
    Title: Local frustration determines loop opening during the catalytic cycle of an oxidoreductase.
  2. Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA.
    Title: Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA.
  3. The authors show that the F plasmid-encoded TrbB relies on DsbD from Escherichia coli for maintenance of its C-X-X-C redox active site motif.
    Title: TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance.
  4. analysis of the structure and function of DsbD
    Title: Two snapshots of electron transport across the membrane: insights into the structure and function of DsbD.
  5. The data indicate that DsbC can assist DsbA in a DsbD-independent manner to oxidatively fold envelope proteins.
    Title: The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.
  6. N-terminus verified by Edman degradation on mature peptide
    Title: Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function.
  7. Properties of the mutants to the positions of the amino acids in the structure of DsbD and discuss mechanisms that would interfere with the electron transfer process.
    Title: Mutations of the membrane-bound disulfide reductase DsbD that block electron transfer steps from cytoplasm to periplasm in Escherichia coli.
  8. Cys109 and Cys461 form a transient interdomain disulfide bond between nDsbD and cDsbD in the reaction cycle of DsbD
    Title: Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD.
  9. kinetic analysis of DsbD-dependent cytochrome c maturation
    Title: Structural basis and kinetics of DsbD-dependent cytochrome c maturation.
  10. N-terminal (nDsbD) and a C-terminal (cDsbD) are likely to be correlated to the role of cDsbD as a covalently linked electron shuttle between the membrane domain and the N-terminal periplasmic domain of DsbD
    Title: High-resolution structures of Escherichia coli cDsbD in different redox states: A combined crystallographic, biochemical and computational study.
Submit: New GeneRIF Correction See all GeneRIFs (13)

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables disulfide oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
enables electron transfer activity IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein-disulfide reductase [NAD(P)H] activity IEA
Inferred from Electronic Annotation
more info
  
enables protein-disulfide reductase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables protein-disulfide reductase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein-disulfide reductase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Process Evidence Code Pubs
involved_in cell redox homeostasis IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within cell redox homeostasis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in cytochrome complex assembly IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within response to copper ion IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in membrane IEA
Inferred from Electronic Annotation
more info
  
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  
located_in plasma membrane ISM
Inferred from Sequence Model
more info
 PubMed 
Preferred Names
thiol-disulfide exchange protein DsbD
NP_418559.1

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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
    4363345..4365042 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_418559.1 thiol-disulfide exchange protein DsbD

    See identical proteins and their annotated locations for NP_418559.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A376X6T6, A0A376YHT1
    Conserved Domains (1) summary
    PRK00293
    Location:2 → 565
    dipZ; thiol:disulfide interchange protein precursor; Provisional
Nucleotide Protein
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