Arginine-specific carbamoyl-phosphate synthetase (small subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.

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

Arginine-specific carbamoyl-phosphate synthetase (small subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.

Putative enzyme with DAC domain protein; One of 3 paralogous diadenylate cyclases (DAC) in this bacteria, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (Probable). Upon expression in E.coli leads to c-di- AMP synthesis. Probably the main producer of c-di-AMP for the cell; is probably implicated in control of peptidogylcan synthesis. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess.

Arginine-specific carbamoyl-phosphate synthetase (small subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.

Conserved hypothetical protein; Upon coexpression in E.coli stimulates the diadenylate cyclase activity of CdaA about 20-fold. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess.

Arginine-specific carbamoyl-phosphate synthetase (small subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.

Putative enzyme with DAC domain; One of 3 paralogous diadenylate cyclases (DAC) in this bacteria, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (Probable). Upon expression in E.coli leads to c-di- AMP synthesis. Overexpression of the hyperactive mutant (L44F) in the absence of c-di-AMP phosphodiesterase GdpP leads to growth defects in log phase (long curly cell filaments) that disappear upon sporulation; spore formation is normal, showing sporulation is insensitive to the excess c-di-AMP. In B.subtilis c-di-AMP is a second messenger that mediates growth, [...]

Diadenylate cyclase; Participates in a DNA-damage check-point that is active prior to asymmetric division when DNA is damaged. Forms globular foci that rapidly scan along the chromosomes during sporulation, searching for lesions. Its ability to scan through the chromosome rapidly is due to its non-specific DNA- binding. When a lesion is present, DisA pauses at the lesion site. This triggers a cellular response that culminates in a temporary block in sporulation initiation. It is required, at least partially, to inhibit the activity of the transcription factor spo0A, which controls, amo [...]

DNA repair protein; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.

Bifunctional glucosamine-1-phosphate N-acetyltransferase/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; belon [...]

Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate (By similarity). Glucosamine-1-phosphate is used for cell wall biosynthesis (Probable); Belongs to the phosphohexose mutase family.

Bifunctional glucosamine-1-phosphate N-acetyltransferase/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; belon [...]

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

Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate (By similarity). Glucosamine-1-phosphate is used for cell wall biosynthesis (Probable); Belongs to the phosphohexose mutase family.

Bifunctional glucosamine-1-phosphate N-acetyltransferase/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; belon [...]

Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate (By similarity). Glucosamine-1-phosphate is used for cell wall biosynthesis (Probable); Belongs to the phosphohexose mutase family.

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

Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate (By similarity). Glucosamine-1-phosphate is used for cell wall biosynthesis (Probable); Belongs to the phosphohexose mutase family.

Pyruvate kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; In the C-terminal section; belongs to the PEP-utilizing enzyme family.

Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate (By similarity). Glucosamine-1-phosphate is used for cell wall biosynthesis (Probable); Belongs to the phosphohexose mutase family.

Putative enzyme with DAC domain protein; One of 3 paralogous diadenylate cyclases (DAC) in this bacteria, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (Probable). Upon expression in E.coli leads to c-di- AMP synthesis. Probably the main producer of c-di-AMP for the cell; is probably implicated in control of peptidogylcan synthesis. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess.

Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate (By similarity). Glucosamine-1-phosphate is used for cell wall biosynthesis (Probable); Belongs to the phosphohexose mutase family.

Conserved hypothetical protein; Upon coexpression in E.coli stimulates the diadenylate cyclase activity of CdaA about 20-fold. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess.

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

Arginine-specific carbamoyl-phosphate synthetase (small subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.

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

Bifunctional glucosamine-1-phosphate N-acetyltransferase/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; belon [...]

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

Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate (By similarity). Glucosamine-1-phosphate is used for cell wall biosynthesis (Probable); Belongs to the phosphohexose mutase family.

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

Putative enzyme with DAC domain protein; One of 3 paralogous diadenylate cyclases (DAC) in this bacteria, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (Probable). Upon expression in E.coli leads to c-di- AMP synthesis. Probably the main producer of c-di-AMP for the cell; is probably implicated in control of peptidogylcan synthesis. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess.

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

Conserved hypothetical protein; Upon coexpression in E.coli stimulates the diadenylate cyclase activity of CdaA about 20-fold. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess.

Pyruvate kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; In the C-terminal section; belongs to the PEP-utilizing enzyme family.

Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate (By similarity). Glucosamine-1-phosphate is used for cell wall biosynthesis (Probable); Belongs to the phosphohexose mutase family.

DNA repair protein; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.

Diadenylate cyclase; Participates in a DNA-damage check-point that is active prior to asymmetric division when DNA is damaged. Forms globular foci that rapidly scan along the chromosomes during sporulation, searching for lesions. Its ability to scan through the chromosome rapidly is due to its non-specific DNA- binding. When a lesion is present, DisA pauses at the lesion site. This triggers a cellular response that culminates in a temporary block in sporulation initiation. It is required, at least partially, to inhibit the activity of the transcription factor spo0A, which controls, amo [...]

DNA repair protein; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.

Putative enzyme with DAC domain protein; One of 3 paralogous diadenylate cyclases (DAC) in this bacteria, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (Probable). Upon expression in E.coli leads to c-di- AMP synthesis. Probably the main producer of c-di-AMP for the cell; is probably implicated in control of peptidogylcan synthesis. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess.