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

Summary

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Gene symbol: dsbA
Gene description: thiol:disulfide oxidoreductase DsbA
Primary source: ASAP:ABE-0012606
Locus tag: b3860
See related: ECOCYC:EG11297
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_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
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.
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.
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.
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].
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.
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.
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.
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.
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.

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General gene information

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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

EC 1.8.4.15

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

NC_000913.3 Reference assembly

Range

4043418..4044044

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

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, A0A826NX20

Conserved Domains (1) summary

PRK10954
Location:1 → 208

PRK10954; thiol:disulfide interchange protein DsbA