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Results 1 - 10 of 33 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2metabolism the enzyme affects multiple phenotypes in Streptococcus gordonii and is required for production of disulfide-bonded proteins like Anti-CR1 scFv 725524
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2physiological function a significant portion of protein HP_0377 is present in the oxidized form in an HP_0231 mutant -, 742200
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2physiological function inactivation of SdbA results in enhanced biofilm formation. Biofilm formation is mediated by the interaction between the CiaRH and ComDE two-component signalling systems. CiaRH is upregulated in the SdbA mutant and is essential for the enhanced biofilm phenotype. The enhanced biofilm phenotype also corresponds to increased oral colonization in mice -, 742794
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2physiological function SdbA mutants lack bacteriocin activity due to strong repression of bacteriocin gene. The Com pathway is functional but not activated in the SdbA mutant. Repression of bacteriocin production is mediated by the CiaRH two-component system, which is strongly upregulated in the sdbA mutant. The CiaRH-induced protease DegP is also upregulated in the SdbA mutant -, 742794
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2physiological function reoxidation of MdbA involves bacterial vitamin K epoxide reductase-like protein that contains four cysteine residues, C93/C101 and C175/C178. Mutation C101A in this protein results in a high molecular weight complex of MdbA and bacterial vitamin K epoxide reductase-like protein 742796
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2physiological function gene deletion results in a severe growth defect at 37°C. By electron microscopy, the MdbA mutant is indistinguishable from wild-type at 30°C. At 37°C, the mutant becomes chained, clumped and coccoid in appearance. The mutant also fails to assemble pilus structures and is greatly defective in toxin production -, 743311
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2physiological function isoform DsbA1 is essential for the motility and autoagglutination phenotypes, and plays a critical role in the oxidative folding of alkaline phosphatase PhoX 743646
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2physiological function loss of isoform DsbA2 has no impact on motility and autoagglutination phenotypes. DsbA2 is crucial for the activity of arylsulfotransferase AstA 743646
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2metabolism 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 745224
Display the word mapDisplay the reaction diagram Show all sequences 1.8.4.2more 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 745224
Results 1 - 10 of 33 > >>