node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
glnE | hldE | b3053 | b3052 | 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 [...] | Heptose 7-phosphate kinase and heptose 1-phosphate adenyltransferase; Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7- phosphate at the C-1 position to selectively form D-glycero-beta-D- manno-heptose-1,7-bisphosphate; In the N-terminal section; belongs to the carbohydrate kinase PfkB family. | 0.670 |
glnE | ygiF | b3053 | b3054 | 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). | 0.873 |
glnE | ygiM | b3053 | b3055 | 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. | 0.586 |
hldE | glnE | b3052 | b3053 | Heptose 7-phosphate kinase and heptose 1-phosphate adenyltransferase; Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7- phosphate at the C-1 position to selectively form D-glycero-beta-D- manno-heptose-1,7-bisphosphate; In the N-terminal section; belongs to the carbohydrate kinase PfkB family. | 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 [...] | 0.670 |
hldE | ygiF | b3052 | b3054 | Heptose 7-phosphate kinase and heptose 1-phosphate adenyltransferase; Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7- phosphate at the C-1 position to selectively form D-glycero-beta-D- manno-heptose-1,7-bisphosphate; In the N-terminal section; belongs to the carbohydrate kinase PfkB family. | 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). | 0.613 |
hldE | ygiM | b3052 | b3055 | Heptose 7-phosphate kinase and heptose 1-phosphate adenyltransferase; Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7- phosphate at the C-1 position to selectively form D-glycero-beta-D- manno-heptose-1,7-bisphosphate; In the N-terminal section; belongs to the carbohydrate kinase PfkB family. | SH3 domain protein. | 0.406 |
phoE | ygiF | b0241 | b3054 | Outer membrane porin PhoE; Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes; Belongs to the Gram-negative porin family. | 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). | 0.485 |
proQ | sixA | b1831 | b2340 | RNA chaperone, putative ProP translation regulator; RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism. | Phosphohistidine phosphatase; Exhibits phosphohistidine phosphatase activity towards the HPt domain of the ArcB sensor involved in the multistep His-Asp phosphorelay. | 0.572 |
proQ | syd | b1831 | b2793 | RNA chaperone, putative ProP translation regulator; RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism. | SecY-interacting protein; Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function; Belongs to the Syd family. | 0.762 |
proQ | yfbV | b1831 | b2295 | RNA chaperone, putative ProP translation regulator; RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism. | UPF0208 family inner membrane protein. | 0.766 |
proQ | ygiF | b1831 | b3054 | RNA chaperone, putative ProP translation regulator; RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism. | 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). | 0.469 |
proQ | yihI | b1831 | b3866 | RNA chaperone, putative ProP translation regulator; RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism. | Activator of Der GTPase; A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function, negatively regulating cell growth, probably via ribosome assembly. Stimulates the GTPase activity of Der; a construct missing the first 45 residues is even more stimulatory. Does not stimulate 2 other GTPases (ObgE and Era). Overexpression inhibits cell growth; precursor 16S rRNA accumulates, the 23S rRNA is 6-7 bases longer than usual, and 50S ribosomal subunits are improperly assembled, leading to 45S subunits lacking proteins L9, L18 and L25. Overexpression of Der in the same cells sup [...] | 0.749 |
pspB | syd | b1305 | b2793 | Psp operon transcription co-activator; The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspB is involved in transcription regulation; Belongs to the PspB family. | SecY-interacting protein; Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function; Belongs to the Syd family. | 0.641 |
pspB | yfbV | b1305 | b2295 | Psp operon transcription co-activator; The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspB is involved in transcription regulation; Belongs to the PspB family. | UPF0208 family inner membrane protein. | 0.714 |
pspB | ygiF | b1305 | b3054 | Psp operon transcription co-activator; The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspB is involved in transcription regulation; Belongs to the PspB family. | 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). | 0.491 |
pspB | yihI | b1305 | b3866 | Psp operon transcription co-activator; The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspB is involved in transcription regulation; Belongs to the PspB family. | Activator of Der GTPase; A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function, negatively regulating cell growth, probably via ribosome assembly. Stimulates the GTPase activity of Der; a construct missing the first 45 residues is even more stimulatory. Does not stimulate 2 other GTPases (ObgE and Era). Overexpression inhibits cell growth; precursor 16S rRNA accumulates, the 23S rRNA is 6-7 bases longer than usual, and 50S ribosomal subunits are improperly assembled, leading to 45S subunits lacking proteins L9, L18 and L25. Overexpression of Der in the same cells sup [...] | 0.591 |
sixA | proQ | b2340 | b1831 | Phosphohistidine phosphatase; Exhibits phosphohistidine phosphatase activity towards the HPt domain of the ArcB sensor involved in the multistep His-Asp phosphorelay. | RNA chaperone, putative ProP translation regulator; RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism. | 0.572 |
sixA | syd | b2340 | b2793 | Phosphohistidine phosphatase; Exhibits phosphohistidine phosphatase activity towards the HPt domain of the ArcB sensor involved in the multistep His-Asp phosphorelay. | SecY-interacting protein; Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function; Belongs to the Syd family. | 0.762 |
sixA | ygiF | b2340 | b3054 | Phosphohistidine phosphatase; Exhibits phosphohistidine phosphatase activity towards the HPt domain of the ArcB sensor involved in the multistep His-Asp phosphorelay. | 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). | 0.692 |
syd | proQ | b2793 | b1831 | SecY-interacting protein; Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function; Belongs to the Syd family. | RNA chaperone, putative ProP translation regulator; RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism. | 0.762 |