N-acetylmuramoyl-L-alanine amidase, putative; Cell-wall hydrolase involved in septum cleavage during cell division; Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.

2-amino-4-hydroxy-6- hydroxymethyldihydropteridine-pyrophosphokinase (folK); Similar to GB:D26562 SP:P26281 GB:L06495 PID:146013 PID:473801 percent identity: 56.33; identified by sequence similarity; putative.

N-acetylmuramoyl-L-alanine amidase, putative; Cell-wall hydrolase involved in septum cleavage during cell division; Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.

Glutamate-ammonia-ligase adenylyltransferase (glnE); Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal [...]

N-acetylmuramoyl-L-alanine amidase, putative; Cell-wall hydrolase involved in septum cleavage during cell division; Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.

tRNA delta(2)-isopentenylpyrophosphate transferase (trpX); Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); Belongs to the IPP transferase family.

N-acetylmuramoyl-L-alanine amidase, putative; Cell-wall hydrolase involved in septum cleavage during cell division; Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.

DNA mismatch repair protein (mutL); This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex (By similarity).

N-acetylmuramoyl-L-alanine amidase, putative; Cell-wall hydrolase involved in septum cleavage during cell division; Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.

poly(A) polymerase (pcnB); Adds poly(A) tail to the 3' end of many RNAs, which usually targets these RNAs for decay. Plays a significant role in the global control of gene expression, through influencing the rate of transcript degradation, and in the general RNA quality control. Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.

N-acetylmuramoyl-L-alanine amidase, putative; Cell-wall hydrolase involved in septum cleavage during cell division; Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.

Conserved hypothetical protein; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaB. TsaE seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD (By similarity). Displays ATPase activity in vitro.

2-amino-4-hydroxy-6- hydroxymethyldihydropteridine-pyrophosphokinase (folK); Similar to GB:D26562 SP:P26281 GB:L06495 PID:146013 PID:473801 percent identity: 56.33; identified by sequence similarity; putative.

N-acetylmuramoyl-L-alanine amidase, putative; Cell-wall hydrolase involved in septum cleavage during cell division; Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.

2-amino-4-hydroxy-6- hydroxymethyldihydropteridine-pyrophosphokinase (folK); Similar to GB:D26562 SP:P26281 GB:L06495 PID:146013 PID:473801 percent identity: 56.33; identified by sequence similarity; putative.

Glutamate-ammonia-ligase adenylyltransferase (glnE); Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal [...]

2-amino-4-hydroxy-6- hydroxymethyldihydropteridine-pyrophosphokinase (folK); Similar to GB:D26562 SP:P26281 GB:L06495 PID:146013 PID:473801 percent identity: 56.33; identified by sequence similarity; putative.

tRNA delta(2)-isopentenylpyrophosphate transferase (trpX); Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); Belongs to the IPP transferase family.

2-amino-4-hydroxy-6- hydroxymethyldihydropteridine-pyrophosphokinase (folK); Similar to GB:D26562 SP:P26281 GB:L06495 PID:146013 PID:473801 percent identity: 56.33; identified by sequence similarity; putative.

DNA mismatch repair protein (mutL); This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex (By similarity).

2-amino-4-hydroxy-6- hydroxymethyldihydropteridine-pyrophosphokinase (folK); Similar to GB:D26562 SP:P26281 GB:L06495 PID:146013 PID:473801 percent identity: 56.33; identified by sequence similarity; putative.

poly(A) polymerase (pcnB); Adds poly(A) tail to the 3' end of many RNAs, which usually targets these RNAs for decay. Plays a significant role in the global control of gene expression, through influencing the rate of transcript degradation, and in the general RNA quality control. Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.

2-amino-4-hydroxy-6- hydroxymethyldihydropteridine-pyrophosphokinase (folK); Similar to GB:D26562 SP:P26281 GB:L06495 PID:146013 PID:473801 percent identity: 56.33; identified by sequence similarity; putative.

Conserved hypothetical protein; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaB. TsaE seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD (By similarity). Displays ATPase activity in vitro.

Glutamine synthetase (glnA); Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family.

Nitrogen regulatory protein P-II (glnB); 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 (By similarity).

Glutamine synthetase (glnA); Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family.

Uridylyl transferase (glnD); Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), 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 (glnA); Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family.

Glutamate-ammonia-ligase adenylyltransferase (glnE); Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal [...]

Nitrogen regulatory protein P-II (glnB); 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 (By similarity).

Glutamine synthetase (glnA); Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family.

Nitrogen regulatory protein P-II (glnB); 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 (By similarity).

Uridylyl transferase (glnD); Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), 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.

Nitrogen regulatory protein P-II (glnB); 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 (By similarity).

Glutamate-ammonia-ligase adenylyltransferase (glnE); Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal [...]

Uridylyl transferase (glnD); Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), 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 (glnA); Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family.

Uridylyl transferase (glnD); Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), 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.

Nitrogen regulatory protein P-II (glnB); 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 (By similarity).