dsbB protein thiol:quinone oxidoreductase DsbB [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Gene symbol: dsbB
Gene description: protein thiol:quinone oxidoreductase DsbB
Primary source: ASAP:ABE-0003979
Locus tag: b1185
See related: ECOCYC:EG11393
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: dsbX; ECK1173; iarB; rosB; roxB; ycgA
Summary: The dsbB gene codes for a transmembrane protein that is responsible for reoxidizing the dsbA-encoded disulfide oxidoreductase. [More information is available at EcoCyc: EG11393].
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Genomic context

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Sequence:: NC_000913.3 (1232500..1233030, complement)

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?

Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA.
Title: Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA.
Data find that overexpressing PspE, a periplasmic rhodanese, partially restores substantial disulphide bond formation to a dsbA strain. This activity depends on DsbC, the bacterial disulphide bond isomerase, but not on DsbB.
Title: Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA.
study reports sequential 13C and 15N chemical shift assignments for the majority of the residues in the transmembrane helices
Title: Chemical shift assignment of the transmembrane helices of DsbB, a 20-kDa integral membrane enzyme, by 3D magic-angle spinning NMR spectroscopy.
DsbB is converted by its specific substrate, DsbA, to a superoxidizing enzyme, capable of oxidizing this extremely oxidizing oxidase.
Title: Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation.
the linker alpha-helix of the bacterial disulfide isomerase DsbC is important for the avoidance of misoxidation by DsbB
Title: Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB.
We found classes of mutants that specifically affect the apparent K(m) of DsbB for either DsbA or quinones, suggesting that quinone and DsbA may interact with different regions of the DsbB protein.
Title: Mutational analysis of the disulfide catalysts DsbA and DsbB.
These observations suggest that the cytosolic loop is important to coordinate the active-site residues of DsbB and ubiquinone to allow their proper reaction cycles.
Title: Role of the cytosolic loop of DsbB in catalytic turnover of the ubiquinone-DsbB complex.
Arg-48 of DsbB in the alpha-helical arrangement is essential for the quinone transition
Title: Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB.
characterization of quinone-free forms of DsbB prepared from mutant cells unable to synthesize ubiquinone and menaquinone
Title: Reactivities of quinone-free DsbB from Escherichia coli.

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General gene information

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Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables electron transfer activity	IEA Inferred from Electronic Annotation more info
enables oxidoreductase activity	IEA Inferred from Electronic Annotation more info
enables oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-disulfide reductase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein-disulfide reductase activity	IEA Inferred from Electronic Annotation more info
enables protein-disulfide reductase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables ubiquinone binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within response to heat	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	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	ISM Inferred from Sequence Model more info	PubMed