U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

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

    Gene ID: 946344, updated on 3-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    dsbB
    Official Full Name
    protein thiol:quinone oxidoreductase DsbB
    Primary source
    ECOCYC:EG11393
    Locus tag
    b1185
    See related
    ASAP:ABE-0003979
    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].
    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 (1232500..1233030, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene DNA polymerase V protein UmuD Neighboring gene DNA polymerase V catalytic protein Neighboring gene Na(+):H(+) antiporter NhaB Neighboring gene DNA-binding transcriptional dual regulator FadR

    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. Thermodynamics of unfolding of an integral membrane protein in mixed micelles. Sehgal P, et al. Protein Sci, 2006 Apr. PMID 16600971, Free PMC Article
    2. DsbB catalyzes disulfide bond formation de novo. Regeimbal J, et al. J Biol Chem, 2002 Sep 6. PMID 12072444
    3. Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B. Xie T, et al. J Biol Chem, 2002 Jan 18. PMID 11698406
    4. Identification of a segment of DsbB essential for its respiration-coupled oxidation. Kobayashi T, et al. Mol Microbiol, 2001 Jan. PMID 11123697
    5. Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli. Kadokura H, et al. Proc Natl Acad Sci U S A, 2000 Sep 26. PMID 11005861, Free PMC Article

    See all (73) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA.
      Title: Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA.
    2. 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.
    3. 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.
    4. 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.
    5. 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.
    6. 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.
    7. 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.
    8. 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.
    9. 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.
    Submit: New GeneRIF Correction

    General gene information

    Go to the top of the page Help

    Homology

    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 

    General protein information

    Go to the top of the page Help
    Preferred Names
    protein thiol:quinone oxidoreductase DsbB
    NP_415703.3

    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
      1232500..1233030 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415703.3 protein thiol:quinone oxidoreductase DsbB [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415703.3

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376MAW8
      Conserved Domains (1) summary
      PRK01749
      Location:1 → 175
      PRK01749; disulfide bond formation protein DsbB
    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.