Fused tRNA nucleotidyl transferase/2'3'-cyclic phosphodiesterase/2'nucleotidase and phosphatase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows highest phosphatase activity in the presence of Ni(2+) and hydrolyzes pyrophosphate, canonical 5'-nucleoside tri- and diphosphates, NADP, and 2'-AMP with the production of Pi. Displays a metal-independent [...]

SH3 domain protein.

Fused deadenylyltransferase/adenylyltransferase for glutamine synthetase; 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 inactivates GlnA by covalent transfer of an adenylyl group from ATP to 'Tyr-398' 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 signa [...]

Inorganic triphosphatase; Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside- linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi), which could be cytotoxic because of its high affinity for calcium ion, thereby interfering with calcium signaling. It also hydrolyzes slowly thiamine triphosphate (ThTP). YgiF is a specific PPPase, but it contributes only marginally to the total PPPase activity in E.coli, where the main enzyme responsible for hydrolysis of PPPi is inorganic pyrophosphatase (PPase).

Fused deadenylyltransferase/adenylyltransferase for glutamine synthetase; 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 inactivates GlnA by covalent transfer of an adenylyl group from ATP to 'Tyr-398' 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 signa [...]

SH3 domain protein.

DUF2884 family putative periplasmic protein.

Putative membrane-anchored secretion pathway M-type protein; Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane.

DUF2884 family putative periplasmic protein.

SH3 domain protein.

DUF2884 family putative periplasmic protein.

Putative transcriptional regulator.

Putative membrane-anchored secretion pathway M-type protein; Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane.

DUF2884 family putative periplasmic protein.

Putative membrane-anchored secretion pathway M-type protein; Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane.

SH3 domain protein.

Putative membrane-anchored secretion pathway M-type protein; Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane.

Putative transcriptional regulator.

Inorganic triphosphatase; Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside- linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi), which could be cytotoxic because of its high affinity for calcium ion, thereby interfering with calcium signaling. It also hydrolyzes slowly thiamine triphosphate (ThTP). YgiF is a specific PPPase, but it contributes only marginally to the total PPPase activity in E.coli, where the main enzyme responsible for hydrolysis of PPPi is inorganic pyrophosphatase (PPase).

Fused deadenylyltransferase/adenylyltransferase for glutamine synthetase; 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 inactivates GlnA by covalent transfer of an adenylyl group from ATP to 'Tyr-398' 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 signa [...]

Inorganic triphosphatase; Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside- linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi), which could be cytotoxic because of its high affinity for calcium ion, thereby interfering with calcium signaling. It also hydrolyzes slowly thiamine triphosphate (ThTP). YgiF is a specific PPPase, but it contributes only marginally to the total PPPase activity in E.coli, where the main enzyme responsible for hydrolysis of PPPi is inorganic pyrophosphatase (PPase).

SH3 domain protein.

SH3 domain protein.

Fused tRNA nucleotidyl transferase/2'3'-cyclic phosphodiesterase/2'nucleotidase and phosphatase; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows highest phosphatase activity in the presence of Ni(2+) and hydrolyzes pyrophosphate, canonical 5'-nucleoside tri- and diphosphates, NADP, and 2'-AMP with the production of Pi. Displays a metal-independent [...]

SH3 domain protein.

Fused deadenylyltransferase/adenylyltransferase for glutamine synthetase; 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 inactivates GlnA by covalent transfer of an adenylyl group from ATP to 'Tyr-398' 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 signa [...]

SH3 domain protein.

DUF2884 family putative periplasmic protein.

SH3 domain protein.

Putative membrane-anchored secretion pathway M-type protein; Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane.

SH3 domain protein.

Inorganic triphosphatase; Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside- linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi), which could be cytotoxic because of its high affinity for calcium ion, thereby interfering with calcium signaling. It also hydrolyzes slowly thiamine triphosphate (ThTP). YgiF is a specific PPPase, but it contributes only marginally to the total PPPase activity in E.coli, where the main enzyme responsible for hydrolysis of PPPi is inorganic pyrophosphatase (PPase).

Putative transcriptional regulator.

DUF2884 family putative periplasmic protein.

Putative transcriptional regulator.

Putative membrane-anchored secretion pathway M-type protein; Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane.

Putative transcriptional regulator.

DUF1107 family protein.

DUF1107 family protein.

Putative transcriptional regulator.