Bacteriophage SPbeta thiol-disulfide oxidoreductase; Unknown; dispensable for production of the lantibiotic sublancin 168 and for competence for DNA uptake; Belongs to the thioredoxin family.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. Not normally required for production of the secreted lantibiotic sublancin 168, although it can partially substitute for BdbB when the latter is absent. It may also be required for the stability of other secreted proteins. Not required for sporulation; Belongs to the DsbB family. BdbC subfamily.

Bacteriophage SPbeta thiol-disulfide oxidoreductase; Unknown; dispensable for production of the lantibiotic sublancin 168 and for competence for DNA uptake; Belongs to the thioredoxin family.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. May be required for the stability of secreted proteins with disulfide bonds. Not required for sporulation.

Bacteriophage SPbeta thiol-disulfide oxidoreductase; Unknown; dispensable for production of the lantibiotic sublancin 168 and for competence for DNA uptake; Belongs to the thioredoxin family.

Thiol-disulfide isomerase; Thiol-disulfide oxidoreductase with a reductive function, involved in spore cortex synthesis. It could be involved either in breaking disulfide bonds in cortex components or in proteins that are important for cortex synthesis, or in thiol/disulfide bond interchange. Belongs to the thioredoxin family.

Bacteriophage SPbeta thiol-disulfide oxidoreductase; Unknown; dispensable for production of the lantibiotic sublancin 168 and for competence for DNA uptake; Belongs to the thioredoxin family.

Putative membrane-bound proteins with a thioredoxin-like domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the thioredoxin family.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. Not normally required for production of the secreted lantibiotic sublancin 168, although it can partially substitute for BdbB when the latter is absent. It may also be required for the stability of other secreted proteins. Not required for sporulation; Belongs to the DsbB family. BdbC subfamily.

Bacteriophage SPbeta thiol-disulfide oxidoreductase; Unknown; dispensable for production of the lantibiotic sublancin 168 and for competence for DNA uptake; Belongs to the thioredoxin family.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. Not normally required for production of the secreted lantibiotic sublancin 168, although it can partially substitute for BdbB when the latter is absent. It may also be required for the stability of other secreted proteins. Not required for sporulation; Belongs to the DsbB family. BdbC subfamily.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. May be required for the stability of secreted proteins with disulfide bonds. Not required for sporulation.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. Not normally required for production of the secreted lantibiotic sublancin 168, although it can partially substitute for BdbB when the latter is absent. It may also be required for the stability of other secreted proteins. Not required for sporulation; Belongs to the DsbB family. BdbC subfamily.

Cytochrome c-type biogenesis protein CcdA; Required for cytochrome c synthesis and stage V of sporulation. Might transfer reducing equivalents across the cytoplasmic membrane, promoting efficient disulfide bond isomerization of proteins localized on the outer surface of the membrane or in the spore coat.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. Not normally required for production of the secreted lantibiotic sublancin 168, although it can partially substitute for BdbB when the latter is absent. It may also be required for the stability of other secreted proteins. Not required for sporulation; Belongs to the DsbB family. BdbC subfamily.

Membrane associated ATPase for DNA competence; Required for uptake of DNA by competent cells.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. Not normally required for production of the secreted lantibiotic sublancin 168, although it can partially substitute for BdbB when the latter is absent. It may also be required for the stability of other secreted proteins. Not required for sporulation; Belongs to the DsbB family. BdbC subfamily.

Pilin-like component of the DNA transport membrane platform; Required for transformation and DNA binding. Belongs to the ComGC family.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. Not normally required for production of the secreted lantibiotic sublancin 168, although it can partially substitute for BdbB when the latter is absent. It may also be required for the stability of other secreted proteins. Not required for sporulation; Belongs to the DsbB family. BdbC subfamily.

heme-A synthase; Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group. Also involved in the sporulation.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. Not normally required for production of the secreted lantibiotic sublancin 168, although it can partially substitute for BdbB when the latter is absent. It may also be required for the stability of other secreted proteins. Not required for sporulation; Belongs to the DsbB family. BdbC subfamily.

Alkaline phosphatase A; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the alkaline phosphatase family.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. Not normally required for production of the secreted lantibiotic sublancin 168, although it can partially substitute for BdbB when the latter is absent. It may also be required for the stability of other secreted proteins. Not required for sporulation; Belongs to the DsbB family. BdbC subfamily.

Extracytoplasmic thioredoxin involved in cytochrome c maturation (lipoprotein); Thiol-disulfide oxidoreductase which is required in disulfide reduction during c-type cytochrome synthesis. May accept reducing equivalents from CcdA, leading to breakage of disulfide bonds in apocytochrome c; following this reduction heme can be covalently attached. Does not play a role in sporulation. Belongs to the thioredoxin family. ResA subfamily.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. Not normally required for production of the secreted lantibiotic sublancin 168, although it can partially substitute for BdbB when the latter is absent. It may also be required for the stability of other secreted proteins. Not required for sporulation; Belongs to the DsbB family. BdbC subfamily.

Thiol-disulfide isomerase; Thiol-disulfide oxidoreductase with a reductive function, involved in spore cortex synthesis. It could be involved either in breaking disulfide bonds in cortex components or in proteins that are important for cortex synthesis, or in thiol/disulfide bond interchange. Belongs to the thioredoxin family.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. Not normally required for production of the secreted lantibiotic sublancin 168, although it can partially substitute for BdbB when the latter is absent. It may also be required for the stability of other secreted proteins. Not required for sporulation; Belongs to the DsbB family. BdbC subfamily.

Putative membrane-bound proteins with a thioredoxin-like domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the thioredoxin family.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. May be required for the stability of secreted proteins with disulfide bonds. Not required for sporulation.

Bacteriophage SPbeta thiol-disulfide oxidoreductase; Unknown; dispensable for production of the lantibiotic sublancin 168 and for competence for DNA uptake; Belongs to the thioredoxin family.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. May be required for the stability of secreted proteins with disulfide bonds. Not required for sporulation.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. Not normally required for production of the secreted lantibiotic sublancin 168, although it can partially substitute for BdbB when the latter is absent. It may also be required for the stability of other secreted proteins. Not required for sporulation; Belongs to the DsbB family. BdbC subfamily.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. May be required for the stability of secreted proteins with disulfide bonds. Not required for sporulation.

Cytochrome c-type biogenesis protein CcdA; Required for cytochrome c synthesis and stage V of sporulation. Might transfer reducing equivalents across the cytoplasmic membrane, promoting efficient disulfide bond isomerization of proteins localized on the outer surface of the membrane or in the spore coat.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. May be required for the stability of secreted proteins with disulfide bonds. Not required for sporulation.

Membrane associated ATPase for DNA competence; Required for uptake of DNA by competent cells.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. May be required for the stability of secreted proteins with disulfide bonds. Not required for sporulation.

Pilin-like component of the DNA transport membrane platform; Required for transformation and DNA binding. Belongs to the ComGC family.

Thiol-disulfide oxidoreductase; Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. May be required for the stability of secreted proteins with disulfide bonds. Not required for sporulation.

Alkaline phosphatase A; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the alkaline phosphatase family.