Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

Diguanylate cyclase, zinc-sensing; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. May act as a zinc sensor that controls, via c-di-GMP, post-translational events. Overexpression leads to a strong repression of swimming; swimming returnes to normal when residues 206-207 are both mutated to Ala. Overexpression also leads to a reduction in flagellar abundance and a 20-fold increase in c-di-GMP levels in vivo. Required for aminoglycoside-mediated induction of biofilm formation, it also plays a lesser role in biofilm production in response to ot [...]

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

Diguanylate cyclase, cold- and stationary phase-induced oxygen-dependent biofilm regulator; Globin-coupled heme-based oxygen sensor protein displaying diguanylate cyclase (DGC) activity in response to oxygen availability. Thus, catalyzes the synthesis of cyclic diguanylate (c-di-GMP) via the condensation of 2 GTP molecules. Is involved in the modulation of intracellular c-di-GMP levels, in association with DosP which catalyzes the degradation of c-di-GMP (PDE activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. DosC regulates biofilm [...]

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

Oxygen sensor, c-di-GMP phosphodiesterase, heme-regulated; Heme-based oxygen sensor protein displaying phosphodiesterase (PDE) activity toward c-di-GMP in response to oxygen availability. Involved in the modulation of intracellular c-di-GMP levels, in association with DosC which catalyzes the biosynthesis of c-di-GMP (diguanylate cyclase activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Has very poor PDE activity on cAMP but is not active with cGMP, bis(p-nitrophenyl) phosphate or p-nitrophenyl phosphate. Via its PDE activity on [...]

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

cyclic-di-GMP phosphodiesterase; Part of a signaling cascade that regulates curli biosynthesis. The cascade is composed of two cyclic-di-GMP (c-di-GMP) control modules, in which c-di-GMP controlled by the DgcE/PdeH pair (module I) regulates the activity of the DgcM/PdeR pair (module II), which in turn regulates activity of the transcription factor MlrA and expression of the master biofilm regulator csgD. PdeR acts as a trigger enzyme that connects modules I and II. It inhibits DgcM and MlrA by direct interaction. Inhibition is relieved when PdeR binds and degrades c-di-GMP generated by [...]

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

Diguanylate cyclase, cellulose regualtor; A probable diguanylate cyclase. The last member of a cascade of expressed proteins, its expression requires DgcM. DgcC production induces biosynthesis of cellulose in some E.coli isolates, but not in K12 strains. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria.

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

Diguanylate cyclase, membrane-anchored; Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Overexpression leads to a strong repression of swimming; swimming returns to normal when residues 359-360 are both mutated to Ala. Overexpression also leads to a 20-fold increase in c-di-GMP levels in vivo. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria.

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

Diguanylate cyclase, csgD regulator; Part of a signaling cascade that regulates curli biosynthesis. The cascade is composed of two cyclic-di-GMP (c-di-GMP) control modules, in which c-di-GMP controlled by the DgcE/PdeH pair (module I) regulates the activity of the DgcM/PdeR pair (module II), which in turn regulates activity of the transcription factor MlrA and expression of the master biofilm regulator csgD. DgcM stimulates activity of MlrA by direct interaction, leading to the transcription of csgD. It also catalyzes the synthesis of c-di-GMP via the condensation of 2 GTP molecules, w [...]

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

Putative membrane-anchored diguanylate cyclase; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules.

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

Putative diguanylate cyclase; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules.

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

Diguanylate cyclase; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria.

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

Putative membrane-anchored diguanylate cyclase; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules (By similarity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Involved in the regulation of cellulose production.

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

Putative diguanylate cyclase; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules (By similarity). Involved in the control of the switch from cell motility to adhesion via regulation of cellular levels of c-di-GMP (Probable). Part of a signaling cascade that regulates curli biosynthesis. The cascade is composed of two c-di- GMP control modules, in which c-di-GMP controlled by the DgcE/PdeH pair (module I) regulates the activity of the DgcM/PdeR pair (module II), which in turn regulates activity of the transcription factor MlrA and expression of t [...]

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

Putative diguanylate cyclase; Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG.

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

cyclic-di-GMP phosphodiesterase, anaerobic; Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG. Truncated proteins consisting of the GGDEF/EAL domains (residues 319-747) or of the EAL domain alone (481-747) have c-di-GMP phosphodiesterase activity. They do not have diguanylate cyclase activity. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria.

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

Putative membrane-anchored diguanylate cyclase; Bifunctional protein that catalyzes the synthesis of cyclic- di-GMP (c-di-GMP) in response to reductive stress and then dynamically relocates to the division site to arrest cell division in response to envelope stress. In the presence of high intracellular c-di-GMP levels, and in response to envelope stress, interacts with cell division proteins and halts cell division, without disassembling the Z ring, but by blocking its further progress toward cytokinesis. Part of a network that regulates cell motility by altering levels of c- di-GMP.

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

cyclic-di-GMP phosphodiesterase; Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG.

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

Putative membrane-anchored diguanylate cyclase; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules.

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

Putative membrane-bound diguanylate cyclase; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules.

Diguanylate cyclase, zinc-sensing; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. May act as a zinc sensor that controls, via c-di-GMP, post-translational events. Overexpression leads to a strong repression of swimming; swimming returnes to normal when residues 206-207 are both mutated to Ala. Overexpression also leads to a reduction in flagellar abundance and a 20-fold increase in c-di-GMP levels in vivo. Required for aminoglycoside-mediated induction of biofilm formation, it also plays a lesser role in biofilm production in response to ot [...]

Targeting factor for csrBC sRNA degradation; Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression.

Diguanylate cyclase, zinc-sensing; Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. May act as a zinc sensor that controls, via c-di-GMP, post-translational events. Overexpression leads to a strong repression of swimming; swimming returnes to normal when residues 206-207 are both mutated to Ala. Overexpression also leads to a reduction in flagellar abundance and a 20-fold increase in c-di-GMP levels in vivo. Required for aminoglycoside-mediated induction of biofilm formation, it also plays a lesser role in biofilm production in response to ot [...]

Oxygen sensor, c-di-GMP phosphodiesterase, heme-regulated; Heme-based oxygen sensor protein displaying phosphodiesterase (PDE) activity toward c-di-GMP in response to oxygen availability. Involved in the modulation of intracellular c-di-GMP levels, in association with DosC which catalyzes the biosynthesis of c-di-GMP (diguanylate cyclase activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Has very poor PDE activity on cAMP but is not active with cGMP, bis(p-nitrophenyl) phosphate or p-nitrophenyl phosphate. Via its PDE activity on [...]