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

    Gene ID: 948649, updated on 3-Dec-2024

    Summary

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    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
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; 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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    Genomic context

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    Sequence:
    NC_000913.3 (4363345..4365042, complement)

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

    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. Protein folding in the bacterial periplasm. Missiakas D, et al. J Bacteriol, 1997 Apr. PMID 9098040, Free PMC Article
    2. 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
    3. 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
    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. 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

    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)

    General gene information

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    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 

    General protein information

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    Preferred Names
    thiol-disulfide exchange protein DsbD

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

    mRNA and Protein(s)

    1. NP_418559.1 thiol-disulfide exchange protein DsbD [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418559.1

      Status: PROVISIONAL

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

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