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Literature summary 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

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.8.4.2 C101A site-directed mutagenesis, the mutation of the cysteine at position 101 to alanine results in a high-molecular-weight complex that is positive for MdbA and VKOR by immunoblotting and is absent in other alanine substitution mutants and the C93A/C101A double mutation and after treatment with the reducing agent 2-mercaptoethanol Actinomyces oris
1.17.4.4 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

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

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.2 Actinomyces oris A0A0M3KL32
-
-
1.17.4.4 Actinomyces oris
-
-
-
1.17.4.4 Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.4.4 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

EC Number Synonyms Comment Organism
1.8.4.2 MdbA
-
 Actinomyces oris
1.8.4.2 membrane-bound thiol-disulfide oxidoreductase
-
 Actinomyces oris
1.8.4.2 thiol-disulfide oxidoreductase
-
 Actinomyces oris
1.17.4.4 VKOR
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
1.8.4.2 metabolism posttranslocational protein folding in the Gram-positive biofilm-forming actinobacterium Actinomyces oris is mediated by membrane-bound thiol-disulfide oxidoreductase, 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 that contains four cysteine residues, C93/C101 and C175/C178, with the latter forming a canonical CXXC thioredoxin-like motif. Topological view of the Actinomyces oris membrane-spanning protein VKOR with these four exoplasmic cysteine residues that participate in MdbA reoxidation. Like deletion of the VKOR gene, alanine replacement of individual cysteine residues abrogates polymicrobial interactions and biofilm formation, concomitant with the failure to form adhesive pili on the bacterial surface. Mutational analysis of VKOR function, overview. The C93 residue of VKOR is postulated to form a mixed disulfide bond with MdbA Actinomyces oris
1.8.4.2 additional information VKOR-mediated reactivation of MdbA appears to be conserved in the Actinobacteria. Formation of the MdbA-VKOR mixed disulfide complex requires C93. The signal of this MdbA-VKOR complex is greatly diminished when the sample is treated with 2-mercaptoethanol. The complex is not found when both C93 and C101 are mutated to alanine. The results suggest that when C101 is mutated, VKOR forms a complex with MdbA via the VKOR C93 residue Actinomyces oris
1.8.4.2 physiological function posttranslocational protein folding in the Gram-positive biofilm-forming actinobacterium Actinomyces oris is mediated by membrane-bound thiol-disulfide oxidoreductase, MdbA, which catalyzes oxidative folding of nascent polypeptides transported by the Sec translocon Actinomyces oris
1.17.4.4 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