Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.

Regulatory protein P-II for glutamine synthetase; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme; Belongs to the P(II) protein family.

Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.

Uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.

Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.

DNA-binding transcriptional regulator NtrC; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes. Activates transcription of many genes and operons whose products minimize the slowing of growth under nitrogen-limiting conditions, including genes coding for glutamine synthetase (glnA), transporters, amino acid permeases and catabolic enzymes.

Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.

Sensory histidine kinase in two-component regulatory system with GlnG; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen limitation, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosphatase that dephosphorylates and inactivates NtrC.

Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.

DNA gyrase, subunit B; DNA gyrase negatively supercoils closed circular double- stranded DNA in an ATP-dependent manner to maintain chromosomes in an underwound state. This makes better substrates for topoisomerase 4 (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli. Gyrase catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes. Relaxes negatively supercoiled DNA in an ATP-independent manner. E.coli gyrase has higher supercoiling activity than other characterized bacterial gyrases; at compa [...]

Regulatory protein P-II for glutamine synthetase; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme; Belongs to the P(II) protein family.

Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.

Regulatory protein P-II for glutamine synthetase; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme; Belongs to the P(II) protein family.

Uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.

Regulatory protein P-II for glutamine synthetase; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme; Belongs to the P(II) protein family.

DNA-binding transcriptional regulator NtrC; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes. Activates transcription of many genes and operons whose products minimize the slowing of growth under nitrogen-limiting conditions, including genes coding for glutamine synthetase (glnA), transporters, amino acid permeases and catabolic enzymes.

Regulatory protein P-II for glutamine synthetase; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme; Belongs to the P(II) protein family.

Sensory histidine kinase in two-component regulatory system with GlnG; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen limitation, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosphatase that dephosphorylates and inactivates NtrC.

Uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.

Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.

Uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.

Regulatory protein P-II for glutamine synthetase; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme; Belongs to the P(II) protein family.

Uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.

DNA-binding transcriptional regulator NtrC; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes. Activates transcription of many genes and operons whose products minimize the slowing of growth under nitrogen-limiting conditions, including genes coding for glutamine synthetase (glnA), transporters, amino acid permeases and catabolic enzymes.

Uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.

Sensory histidine kinase in two-component regulatory system with GlnG; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen limitation, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosphatase that dephosphorylates and inactivates NtrC.

DNA-binding transcriptional regulator NtrC; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes. Activates transcription of many genes and operons whose products minimize the slowing of growth under nitrogen-limiting conditions, including genes coding for glutamine synthetase (glnA), transporters, amino acid permeases and catabolic enzymes.

Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.

DNA-binding transcriptional regulator NtrC; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes. Activates transcription of many genes and operons whose products minimize the slowing of growth under nitrogen-limiting conditions, including genes coding for glutamine synthetase (glnA), transporters, amino acid permeases and catabolic enzymes.

Regulatory protein P-II for glutamine synthetase; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme; Belongs to the P(II) protein family.

DNA-binding transcriptional regulator NtrC; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes. Activates transcription of many genes and operons whose products minimize the slowing of growth under nitrogen-limiting conditions, including genes coding for glutamine synthetase (glnA), transporters, amino acid permeases and catabolic enzymes.

Uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.

DNA-binding transcriptional regulator NtrC; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes. Activates transcription of many genes and operons whose products minimize the slowing of growth under nitrogen-limiting conditions, including genes coding for glutamine synthetase (glnA), transporters, amino acid permeases and catabolic enzymes.

Sensory histidine kinase in two-component regulatory system with GlnG; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen limitation, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosphatase that dephosphorylates and inactivates NtrC.

Sensory histidine kinase in two-component regulatory system with GlnG; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen limitation, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosphatase that dephosphorylates and inactivates NtrC.

Glutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.

Sensory histidine kinase in two-component regulatory system with GlnG; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen limitation, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosphatase that dephosphorylates and inactivates NtrC.

Regulatory protein P-II for glutamine synthetase; P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR- I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme; Belongs to the P(II) protein family.

Sensory histidine kinase in two-component regulatory system with GlnG; Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen limitation, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosphatase that dephosphorylates and inactivates NtrC.

Uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.