Putative Clp proteinase, ATP-binding subunit ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to th [...]

Heat shock protein DnaJ (HSP-40); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwe [...]

Putative Clp proteinase, ATP-binding subunit ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to th [...]

Putative excinuclease ABC (subunit A); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.

Class III stress response-related ATP-dependent Clp protease, ATP-binding subunit; Best Blastp Hit: gb|AAD01783.1| (AF023422) ClpC [Lactococcus lactis]; Belongs to the ClpA/ClpB family.

Heat shock protein DnaJ (HSP-40); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwe [...]

Class III stress response-related ATP-dependent Clp protease, ATP-binding subunit; Best Blastp Hit: gb|AAD01783.1| (AF023422) ClpC [Lactococcus lactis]; Belongs to the ClpA/ClpB family.

Putative excinuclease ABC (subunit A); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.

Putative tetrahydrodipicolinate succinylase; Catalyzes the transfer of an acetyl group from acetyl-CoA to tetrahydrodipicolinate.

Putative UDP-N-acetylglucosamine pyrophosphorylase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belongs to the transferase hexapeptide repeat family.

Heat shock protein DnaJ (HSP-40); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwe [...]

Putative Clp proteinase, ATP-binding subunit ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Belongs to th [...]

Heat shock protein DnaJ (HSP-40); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwe [...]

Class III stress response-related ATP-dependent Clp protease, ATP-binding subunit; Best Blastp Hit: gb|AAD01783.1| (AF023422) ClpC [Lactococcus lactis]; Belongs to the ClpA/ClpB family.

Heat shock protein DnaJ (HSP-40); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions betwe [...]

Putative excinuclease ABC (subunit A); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.

Glucosamine-fructose-6-phosphate aminotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.

Putative UDP-N-acetylglucosamine pyrophosphorylase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belongs to the transferase hexapeptide repeat family.

Glucosamine-fructose-6-phosphate aminotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.

Carbamoylphosphate synthetase, large subunit; Best Blastp Hit: emb|CAA03928.1| (AJ000109) carbamoylphosphate synthetase [Lactococcus lactis].

Putative UDP-N-acetylglucosamine pyrophosphorylase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belongs to the transferase hexapeptide repeat family.

Putative tetrahydrodipicolinate succinylase; Catalyzes the transfer of an acetyl group from acetyl-CoA to tetrahydrodipicolinate.

Putative UDP-N-acetylglucosamine pyrophosphorylase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belongs to the transferase hexapeptide repeat family.

Glucosamine-fructose-6-phosphate aminotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.

glucosyltransferase-I; Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris; Belongs to the glycosyl hydrolase 70 family.

glucosyltransferase-SI; Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris; Belongs to the glycosyl hydrolase 70 family.

glucosyltransferase-I; Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris; Belongs to the glycosyl hydrolase 70 family.

glucosyltransferase-S; Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris; Belongs to the glycosyl hydrolase 70 family.

glucosyltransferase-I; Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris; Belongs to the glycosyl hydrolase 70 family.

Cell surface antigen SpaP; Surface protein antigen implicated in dental caries; Belongs to the SpaP/Ssp5/SpaA family.

glucosyltransferase-SI; Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris; Belongs to the glycosyl hydrolase 70 family.

glucosyltransferase-I; Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris; Belongs to the glycosyl hydrolase 70 family.

glucosyltransferase-SI; Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris; Belongs to the glycosyl hydrolase 70 family.

glucosyltransferase-S; Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris; Belongs to the glycosyl hydrolase 70 family.

glucosyltransferase-SI; Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris; Belongs to the glycosyl hydrolase 70 family.

Cell surface antigen SpaP; Surface protein antigen implicated in dental caries; Belongs to the SpaP/Ssp5/SpaA family.

glucosyltransferase-S; Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris; Belongs to the glycosyl hydrolase 70 family.

glucosyltransferase-I; Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris; Belongs to the glycosyl hydrolase 70 family.

glucosyltransferase-S; Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris; Belongs to the glycosyl hydrolase 70 family.

glucosyltransferase-SI; Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris; Belongs to the glycosyl hydrolase 70 family.