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Results 1 - 6 of 6
EC Number
General Information
the enzyme affects multiple phenotypes in Streptococcus gordonii and is required for production of disulfide-bonded proteins like Anti-CR1 scFv
physiological function
a significant portion of protein HP_0377 is present in the oxidized form in an HP_0231 mutant
physiological function
gene deletion results in a severe growth defect at 37C. By electron microscopy, the MdbA mutant is indistinguishable from wild-type at 30C. At 37C, the mutant becomes chained, clumped and coccoid in appearance. The mutant also fails to assemble pilus structures and is greatly defective in toxin production
physiological 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; 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
physiological function
isoform DsbA1 is essential for the motility and autoagglutination phenotypes, and plays a critical role in the oxidative folding of alkaline phosphatase PhoX; loss of isoform DsbA2 has no impact on motility and autoagglutination phenotypes. DsbA2 is crucial for the activity of arylsulfotransferase AstA
physiological 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
Results 1 - 6 of 6