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Literature summary for 1.8.4.2 extracted from

  • Jalal, N.A.; Davey, L.; Halperin, S.A.; Lee, S.F.
    Identification of redox partners of the thiol-disulfide oxidoreductase SdbA in Streptococcus gordonii (2019), J. Bacteriol., 201, e00030-19 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.4.2

Cloned(Commentary)

Cloned (Comment) Organism
gene SGO_2006, DNA and amino acid sequence determination and analysis, quantitative real-time PCR, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain XL-1 Blue Streptococcus gordonii

Protein Variants

Protein Variants Comment Organism
C89A site-directed mutagenesis, the single-cysteine active site variant, SdbAC89A, forms a number of mixed disulfide complexes in the mutant Streptococcus gordonii
additional information gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. The phenotypes exhibited by the sdbB-ccdA2 mutant are reversed when functional copies of sdbB and ccdA2 are knocked back into the same location on the chromosome. Quantitative realtime PCR analysis of the sdbB-ccdA2 mutant shows that the genes immediately upstream (sgo_1174) and downstream (sgo_1170) of the mutated genes are transcribed, indicating that the mutation does not affect the expression of adjacent genes. The levels of sgo_1174 and sgo_1170 expression are similar between the parent, sdbBccdA2 mutant, and sdbB-ccdA2 knockin mutant Streptococcus gordonii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 glutathione + protein AtlS-disulfide Streptococcus gordonii
-
 glutathione-disulfide + protein AtlS-dithiol
-
 ?
2 glutathione + protein AtlS-disulfide Streptococcus gordonii Challis
-
 glutathione-disulfide + protein AtlS-dithiol
-
 ?
2 glutathione + protein AtlS-disulfide Streptococcus gordonii ATCC 35105
-
 glutathione-disulfide + protein AtlS-dithiol
-
 ?
2 glutathione + protein AtlS-disulfide Streptococcus gordonii DL1
-
 glutathione-disulfide + protein AtlS-dithiol
-
 ?
2 glutathione + protein AtlS-disulfide Streptococcus gordonii V288
-
 glutathione-disulfide + protein AtlS-dithiol
-
 ?
2 glutathione + protein AtlS-disulfide Streptococcus gordonii BCRC 15272
-
 glutathione-disulfide + protein AtlS-dithiol
-
 ?
2 glutathione + protein AtlS-disulfide Streptococcus gordonii CH1
-
 glutathione-disulfide + protein AtlS-dithiol
-
 ?
2 glutathione + protein-disulfide Streptococcus gordonii
-
 glutathione-disulfide + protein-dithiol
-
 ?
2 glutathione + protein-disulfide Streptococcus gordonii Challis
-
 glutathione-disulfide + protein-dithiol
-
 ?
2 glutathione + protein-disulfide Streptococcus gordonii ATCC 35105
-
 glutathione-disulfide + protein-dithiol
-
 ?
2 glutathione + protein-disulfide Streptococcus gordonii DL1
-
 glutathione-disulfide + protein-dithiol
-
 ?
2 glutathione + protein-disulfide Streptococcus gordonii V288
-
 glutathione-disulfide + protein-dithiol
-
 ?
2 glutathione + protein-disulfide Streptococcus gordonii BCRC 15272
-
 glutathione-disulfide + protein-dithiol
-
 ?
2 glutathione + protein-disulfide Streptococcus gordonii CH1
-
 glutathione-disulfide + protein-dithiol
-
 ?

Organism

Organism UniProt Comment Textmining
Streptococcus gordonii A8AZP5
-
-
Streptococcus gordonii ATCC 35105 A8AZP5
-
-
Streptococcus gordonii BCRC 15272 A8AZP5
-
-
Streptococcus gordonii CH1 A8AZP5
-
-
Streptococcus gordonii Challis A8AZP5
-
-
Streptococcus gordonii DL1 A8AZP5
-
-
Streptococcus gordonii V288 A8AZP5
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain XL-1 Blue by nickel affinity chromatography Streptococcus gordonii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 glutathione + protein AtlS-disulfide
-
 Streptococcus gordonii glutathione-disulfide + protein AtlS-dithiol
-
 ?
2 glutathione + protein AtlS-disulfide
-
 Streptococcus gordonii Challis glutathione-disulfide + protein AtlS-dithiol
-
 ?
2 glutathione + protein AtlS-disulfide
-
 Streptococcus gordonii ATCC 35105 glutathione-disulfide + protein AtlS-dithiol
-
 ?
2 glutathione + protein AtlS-disulfide
-
 Streptococcus gordonii DL1 glutathione-disulfide + protein AtlS-dithiol
-
 ?
2 glutathione + protein AtlS-disulfide
-
 Streptococcus gordonii V288 glutathione-disulfide + protein AtlS-dithiol
-
 ?
2 glutathione + protein AtlS-disulfide
-
 Streptococcus gordonii BCRC 15272 glutathione-disulfide + protein AtlS-dithiol
-
 ?
2 glutathione + protein AtlS-disulfide
-
 Streptococcus gordonii CH1 glutathione-disulfide + protein AtlS-dithiol
-
 ?
2 glutathione + protein-disulfide
-
 Streptococcus gordonii glutathione-disulfide + protein-dithiol
-
 ?
2 glutathione + protein-disulfide
-
 Streptococcus gordonii Challis glutathione-disulfide + protein-dithiol
-
 ?
2 glutathione + protein-disulfide
-
 Streptococcus gordonii ATCC 35105 glutathione-disulfide + protein-dithiol
-
 ?
2 glutathione + protein-disulfide
-
 Streptococcus gordonii DL1 glutathione-disulfide + protein-dithiol
-
 ?
2 glutathione + protein-disulfide
-
 Streptococcus gordonii V288 glutathione-disulfide + protein-dithiol
-
 ?
2 glutathione + protein-disulfide
-
 Streptococcus gordonii BCRC 15272 glutathione-disulfide + protein-dithiol
-
 ?
2 glutathione + protein-disulfide
-
 Streptococcus gordonii CH1 glutathione-disulfide + protein-dithiol
-
 ?
additional information oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed Streptococcus gordonii ?
-
-
additional information oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed Streptococcus gordonii Challis ?
-
-
additional information oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed Streptococcus gordonii ATCC 35105 ?
-
-
additional information oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed Streptococcus gordonii DL1 ?
-
-
additional information oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed Streptococcus gordonii V288 ?
-
-
additional information oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed Streptococcus gordonii BCRC 15272 ?
-
-
additional information oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed Streptococcus gordonii CH1 ?
-
-

Synonyms

Synonyms Comment Organism
SdbA
-
 Streptococcus gordonii
SGO_2006
-
 Streptococcus gordonii
Streptococcus disulfide bond protein A
-
 Streptococcus gordonii
TDOR
-
 Streptococcus gordonii
thiol-disulfide oxidoreductase
-
 Streptococcus gordonii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Streptococcus gordonii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Streptococcus gordonii

General Information

General Information Comment Organism
evolution homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA Streptococcus gordonii
malfunction gene sdbA mutants are defective in autolysis, extracellular DNA (eDNA) release, bacteriocin production, and genetic competence but form more biofilm. Inactivation of sdbA upregulates the CiaRH two-component regulatory system in Streptococcus gordonii, leading to the repression of the ComDE quorum sensing system, which results in the enhanced biofilm formation and the lack of bacteriocin production. The sdbB-ccdA2 mutant produces all of the phenotypes displayed by the sdbA mutant. The sdbB-sgo_1177 mutant is defective in eDNA release and bacteriocin production but not autolysis or genetic competence. The sdbB-ccdA1 mutant is defective in autolysis but not eDNA release, bacteriocin production, or genetic competence. The sgo_1177-ccdA2 mutant is partially defective in autolysis but not in other phenotypes. The ccdA1-ccdA2 mutant is defective only in bacteriocin production. AtlS, the natural substrate of SdbA, in the sdbB-ccdA2 mutant lacks activity and a disulfide bond. The lack of autolysis in the sdbB-ccdA2 mutant is due to a defect in the activity of AtlS. Enzyme mutant SdbAC89A variant forms mixed disulfide with SdbB in vivo Streptococcus gordonii
metabolism identification and characterization of the SdbA redox partners SdbB and CcdA2 (encoded by gene ccdA2) in Streptococcus gordonii. CcdA2 is annotated as cytochrome c biogenesis protein A. Thiol-disulfide oxidoreductase-associated lipoprotein SdbB, encoded by gene sgo_1177, constitutes the main pathway for SdbA reoxidation. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii Streptococcus gordonii
physiological function thiol-disulfide oxidoreductase, SdbA, in Streptococcus gordonii forms disulfide bonds in substrate proteins and plays a role in multiple phenotypes. SdbA has multiple redox partners, e.g. SdbB and CcdA2, forming a complex oxidative protein-folding pathway. This pathway is essential for autolysis, bacteriocin production, genetic competence, and extracellular DNA (eDNA) release in Streptococcus gordonii. These cellular processes are considered to be important for the success of Streptococcus gordonii as a dental plaque organism. Homologues of SdbA appear to be present in a range of Gram-positive bacteria that lack DsbA. SdbA is able to introduce a disulfide bond into its natural substrate, the major autolysin AtlS. This can be achieved with a single C-terminal cysteine in its CPDC active site, further suggesting SdbA is quite different from DsbA Streptococcus gordonii