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    dsbA thiol:disulfide oxidoreductase DsbA [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948353, updated on 3-Dec-2024

    Summary

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    Official Symbol
    dsbA
    Official Full Name
    thiol:disulfide oxidoreductase DsbA
    Primary source
    ECOCYC:EG11297
    Locus tag
    b3860
    See related
    ASAP:ABE-0012606
    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
    dsf; ECK3852; iarA; ppfA
    Summary
    DsbA has a role in cytochrome C synthesis. [More information is available at EcoGene: EG11297].
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    Genomic context

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    Sequence:
    NC_000913.3 (4043418..4044044)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene DUF1040 domain-containing protein YihD Neighboring gene stress response kinase A Neighboring gene DUF945 domain-containing protein YihF Neighboring gene 1-acylglycerol-3-phosphate O-acyltransferase YihG

    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. Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization. Guddat LW, et al. Structure, 1998 Jun 15. PMID 9655827
    2. [Structural basis for disulfide bond generation in the cell]. Inaba K, et al. Tanpakushitsu Kakusan Koso, 2007 Jul. PMID 17642268
    3. [Study on disulfide bond formation protein A in Escherichia coli]. Luo M, et al. Sheng Wu Gong Cheng Xue Bao, 2007 Jan. PMID 17366881
    4. Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant. Ondo-Mbele E, et al. J Mol Biol, 2005 Apr 1. PMID 15755450
    5. Structure of circularly permuted DsbA(Q100T99): preserved global fold and local structural adjustments. Manjasetty BA, et al. Acta Crystallogr D Biol Crystallogr, 2004 Feb. PMID 14747707

    See all (125) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. analysis of mutants that map to two areas in the structure of DsbB, one located between the two first transmembrane segments where the quinone ring binds and the other located in the second periplasmic loop of DsbB, which interacts with DsbA
      Title: Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions.
    2. DsbA and DsbL introduce the disulfide bond into unfolded bacterial aryl sulfotransferase (ASST) at similar rates.
      Title: Structural and mechanistic insights into the PAPS-independent sulfotransfer catalyzed by bacterial aryl sulfotransferase and the role of the DsbL/Dsbl system in its folding.
    3. A high-resolution structural model of integral membrane protein DsbB in E. coli is responsible for oxidizing the periplasmic protein DsbA, which forms disulfide bonds in substrate proteins.
      Title: Structure of the disulfide bond generating membrane protein DsbB in the lipid bilayer.
    4. Data found that the periplasmic disulfide isomerase DsbC cooperates with SurA and the thiol oxidase DsbA in the folding of the essential beta-barrel protein LptD.
      Title: The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD.
    5. Studies indicate that DsbA could effectively assist proteins folding, both in vivo coexpressed with the target protein, and in vitro replenished as foldases.
      Title: [Study on disulfide bond formation protein A in Escherichia coli].
    6. Study identified cotranslational and posttranslational folding intermediates of a periplasmic protein in which the protein and DsbA, a periplasmic disulfide bond-forming enzyme, are covalently linked by a disulfide bond.
      Title: Detecting folding intermediates of a protein as it passes through the bacterial translocation channel.
    7. Results describbe the catalytic mechanism of DsbL, and provide evidence for proton shuffling during catalysis.
      Title: Evidence for proton shuffling in a thioredoxin-like protein during catalysis.
    8. 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.
    9. N-terminus verified by Edman degradation on mature peptide
      Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
    10. Results describe the crystal structure of the DsbA mutant C33A at 2.0 angstroms resolution.
      Title: Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant.
    Submit: New GeneRIF Correction See all GeneRIFs (14)

    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 oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein disulfide isomerase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    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
    acts_upstream_of_or_within cellular response to antibiotic IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in outer membrane-bounded periplasmic space IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in periplasmic space IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    thiol:disulfide oxidoreductase DsbA
    NP_418297.1

    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
      4043418..4044044
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418297.1 thiol:disulfide oxidoreductase DsbA [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418297.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A478KNB2, A0A5B9AR11
      Conserved Domains (1) summary
      PRK10954
      Location:1 → 208
      PRK10954; thiol:disulfide interchange protein DsbA
    Nucleotide Protein
    Heading Accession and Version

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