U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

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

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

Summary

Go to the top of the page Help
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].
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
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

Go to the top of the page Help
Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

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

Go to the top of the page Help

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

Go to the top of the page Help
Preferred Names
thiol:disulfide oxidoreductase DsbA
NP_418297.1

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.