EC Number   |
General Information |
Reference |
|---|
   1.8.4.2 | physiological function |
the organism encodes a large number of exported proteins containing paired cysteine residues. Proteins possessing 2 or more cysteine residues made up 58.4% of the Corynabacterium matruchotii proteome (1530 of 2619 proteins). In the Gram-positive actinobacteria, oxidative protein folding via disulfide bond formation appears to be the major pathway for posttranslocational folding of these unfolded proteins. The oxidoreductase MdbA identified from Corynebacterium matruchotii, MdbACm, catalyzes disulfide bond formation within the actinobacterial pilin FimA |
-, 765004 |
| 1.8.4.2 | physiological function |
the thiol-disulfide oxidoreductase DsbA carries out oxidative folding of extra-cytoplasmic proteins by catalyzing the formation of intramolecular disulfide bonds. It has an important role in various cellular functions, including cell division. DsbA activity is required for full respiratory capability of Rhodobacter capsulatus, and in particular, for proper biogenesis of its cbb3-type cytochrome c oxidase (cbb3-Cox). Enzyme DsbA facilitates oxidative folding of extra-cytoplasmic proteins by catalyzing the formation of intramolecular disulfide bonds between two reactive Cys residues of its substrates, which include the c-type apocyts with their conserved CxxCH heme-binding sites. Reduced DsbA is re-oxidized by its recycling partner DsbB, which then transfers the reducing equivalents to the Q pool, and eventually to the electron transport chain |
-, 764747 |
| 1.8.4.2 | 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 |
-, 765006 |
