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Literature summary for 1.17.4.4 extracted from

  • Luong, T.T.; Reardon-Robinson, M.E.; Siegel, S.D.; Ton-That, H.
    Reoxidation of the thiol-disulfide oxidoreductase MdbA by a bacterial vitamin K epoxide reductase in the biofilm-forming actinobacterium actinomyces oris (2017), J. Bacteriol., 199, e00817-16 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.17.4.4

Cloned(Commentary)

Cloned (Comment) Organism
expression in Actinomyces oris VKOR deletion (DELTAVKOR) mutant Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
C101A formation of of a high-molecular-weight complex that is positive for thiol-disulfide oxidoreductase MdbA and vitamin K epoxide reductase Actinomyces oris

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane topological view of the the membrane spanning enzyme with these four exoplasmic cysteine residues Actinomyces oris 16020
-

Organism

Organism UniProt Comment Textmining
Actinomyces oris
-
-
-
Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
purification of a high-molecular-weight complex that is positive for thiol-disulfide oxidoreductase MdbA and vitamin K epoxide reductase VKOR in the C101A mutant Actinomyces oris

Synonyms

Synonyms Comment Organism
VKOR
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
metabolism posttranslocational protein folding in the Gram-positive biofilm-forming actinobacterium Actinomyces oris is mediated by a membrane-bound thiol-disulfide oxidoreductase named MdbA, which catalyzes oxidative folding of nascent polypeptides transported by the Sec translocon. Reoxidation of MdbA involves a bacterial vitamin K epoxide reductase (VKOR)-like protein Actinomyces oris