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2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
GTP
cyclic di-3',5'-guanylate + diphosphate
GTP
diphosphate + cyclic di-3',5'-guanylate
GTP + GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
GTP + GTP
cyclic-di-3',5'-GMP + diphosphate + diphosphate
pH 7.8
reaction stop with 25 mM EDTA, pH 6, KD (cyclic-di-3,5-GMP): 0.3 microM or 0.4 microM (in presence of activator BeF3)
-
?
additional information
?
-
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The DgcP of Caulobacter crescentus binds dimeric c-di-GMP at an allosteric site I-site that is characterized by the RxxD motif. Binding of cyclic-di-GMP at the I-site accounts for a strong non-competitive product inhibition, which establishes a limit on the cellular c-di-GMP concentration
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The DgcP of Caulobacter crescentus binds dimeric c-di-GMP at an allosteric site I-site that is characterized by the RxxD motif. Binding of cyclic-di-GMP at the I-site accounts for a strong non-competitive product inhibition, which establishes a limit on the cellular c-di-GMP concentration
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Thermosynechococcus vestitus
-
conversion is enhanced under blue light irradiation, with 38fold difference between the blue and green light-induced activities
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
Vibrio cholerae serotype O1 A1552
-
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
the enzyme uses its GGDEF domain for catalysis. The GGDEF signature domain forms part of the active site A-site where GTP is bound (one molecule of GTP substrate per monomer)
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
2 GTP
2 diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
diguanylate cyclase activity constitutes the signaling output of the PleD response regulator
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
Marinobacter nauticus
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
SwDGC has both cyclase and phosphodiesterase activities. Peaks for c-di-GMP and pGpG (5'-phosphoguanylyl-(3',5')-guanosine) appear within several min of reaction
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
-
-
-
?
GTP
cyclic di-3',5'-guanylate + diphosphate
-
-
-
?
GTP
diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
GTP
diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
GTP
diphosphate + cyclic di-3',5'-guanylate
-
-
-
-
?
GTP
diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
GTP
diphosphate + cyclic di-3',5'-guanylate
-
-
-
-
?
GTP
diphosphate + cyclic di-3',5'-guanylate
-
-
-
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
pH 8, 60 min, 25°C, 10 mM MgCl2
reaction stop by 0.083 mM EDTA
-
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
analyses by pyrophosphatase-coupled spectrophotometric assay
-
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
2 mM Mg2+
analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
-
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
2 mM Mg2+, 25°C
analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
-
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
2 mM Mg2+, 25°C
analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
-
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
2 mM Mg2+, 25°C
analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
-
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
2 mM Mg2+, 25°C
analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
-
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
2 mM Mg2+, 25°C
analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
-
?
GTP + GTP
cyclic di-3',5'-guanylate + diphosphate + diphosphate
-
2 mM Mg2+, 25°C
analysis by coupled spectrophotometric assay measuring diphosphate synthesis or by reverse-phase HPLC
-
?
additional information
?
-
-
MifA and MifB proteins act posttranscriptionally on flagellation
-
-
?
additional information
?
-
-
analysis of the DGC specificity, overview
-
-
-
additional information
?
-
-
mode of GTPalphaS/Mg2+-binding suggests two-metal catalytic mechanism analogous to adenylate cyclases
-
-
?
additional information
?
-
mode of GTPalphaS/Mg2+-binding suggests two-metal catalytic mechanism analogous to adenylate cyclases
-
-
?
additional information
?
-
-
on-rates constants of substrate and product range between 100/sec and 300/sec
-
-
?
additional information
?
-
on-rates constants of substrate and product range between 100/sec and 300/sec
-
-
?
additional information
?
-
-
analysis of the DGC specificity, overview
-
-
-
additional information
?
-
-
no substrate: ATP, ADP, AMP, GDP, GMP,CTP, TTP, c-di-GMP, cAMP, and cGMP
-
-
?
additional information
?
-
-
no substrate: ATP, ADP, AMP, GDP, GMP,CTP, TTP, c-di-GMP, cAMP, and cGMP
-
-
?
additional information
?
-
-
analysis of the DGC specificity, overview
-
-
-
additional information
?
-
-
cyclic guanylate cyclase YvvD and Dos, a heme based oxygen sensor with cyclic diguanylate phosphodiesterase activity may be part of a fine-tuning mechanism for regulating the intracellular levels of cyclic diguanylate
-
-
?
additional information
?
-
-
the interaction between MANT (2'(3'))-O-(N-methylanthraniloyl)- or TNP (2',3'-O-(2,4,6-trinitrophenyl))-substituted nucleotides and the DGC YdeH by fluorimetric and mass-spectrometric means is investigated. A strong fluorescence resonance energy transfer between tryptophan and tyrosine residues of YdeH and the MANT group of MANT-NTPs (MANT-ATP,-CTP, -GTP, -ITP, -UTP, and -XTP) and an enhanced direct MANT fluorescence upon interaction with YdeH is observed
-
-
?
additional information
?
-
analysis of the DGC specificity, overview
-
-
-
additional information
?
-
analysis of the DGC specificity, overview
-
-
-
additional information
?
-
-
purified enzyme shows phosphodiesterase activity, but no diguanylate cyclase activity
-
-
?
additional information
?
-
-
pppGpG co-purified with reaction products, possible intermediate of diguanylate cyclisation
-
-
?
additional information
?
-
HsbD interacts with the anti-anti-sigma factor HsbA, this interaction is lost when the HsbA phosphorylation site, Ser56, is substituted. In contrast, a phosphorylated mimicry of HsbA, engineered by replacing Ser56 with an aspartate residue, interacts more strongly with HsbDs, suggesting that phosphorylation of HsbA possibly strengthens the stability of the HsbDs/HsbA complex with an alanine. HsbD binds to the phosphorylated form of the anti-anti-sigma factor HsbA
-
-
-
additional information
?
-
-
HsbD interacts with the anti-anti-sigma factor HsbA, this interaction is lost when the HsbA phosphorylation site, Ser56, is substituted. In contrast, a phosphorylated mimicry of HsbA, engineered by replacing Ser56 with an aspartate residue, interacts more strongly with HsbDs, suggesting that phosphorylation of HsbA possibly strengthens the stability of the HsbDs/HsbA complex with an alanine. HsbD binds to the phosphorylated form of the anti-anti-sigma factor HsbA
-
-
-
additional information
?
-
-
analysis of the DGC specificity, overview
-
-
-
additional information
?
-
HsbD interacts with the anti-anti-sigma factor HsbA, this interaction is lost when the HsbA phosphorylation site, Ser56, is substituted. In contrast, a phosphorylated mimicry of HsbA, engineered by replacing Ser56 with an aspartate residue, interacts more strongly with HsbDs, suggesting that phosphorylation of HsbA possibly strengthens the stability of the HsbDs/HsbA complex with an alanine. HsbD binds to the phosphorylated form of the anti-anti-sigma factor HsbA
-
-
-
additional information
?
-
diguanylate cyclase GcbC physically interacts with the effector protein LapD in order to promote biofilm formation
-
-
-
additional information
?
-
-
diguanylate cyclase GcbC physically interacts with the effector protein LapD in order to promote biofilm formation
-
-
-
additional information
?
-
diguanylate cyclase GcbC physically interacts with the effector protein LapD in order to promote biofilm formation
-
-
-
additional information
?
-
-
GcsA has no PDE activity
-
-
-
additional information
?
-
GcsA has no PDE activity
-
-
-
additional information
?
-
GcsA has no PDE activity
-
-
-
additional information
?
-
-
GcsA has no PDE activity
-
-
-
additional information
?
-
GcsA has no PDE activity
-
-
-
additional information
?
-
GcsA has no PDE activity
-
-
-
additional information
?
-
Thermosynechococcus vestitus
no substrate: ATP
-
-
?
additional information
?
-
-
analysis of the DGC specificity, overview
-
-
-
additional information
?
-
Vibrio cholerae serotype O1 A1552
-
analysis of the DGC specificity, overview
-
-
-
additional information
?
-
sequential random binding model of two identical substrates binding to two equivalent GGDEF domains that come together to form a symmetrical active site
-
-
?
additional information
?
-
-
sequential random binding model of two identical substrates binding to two equivalent GGDEF domains that come together to form a symmetrical active site
-
-
?
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2',3'-O-[2,4,6-trinitrocyclohexa-2,5-diene-1,1-diyl]-GTP
-
-
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
2'-(N-methylanthraniloyl)-GTP
-
-
2'-(N-methylanthraniloyl)-GTP-gamma-S
-
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-(gammaS)triphosphate
2'-O-[2-(methylamino)benzoyl]guanosine 5'-triphosphate
2-(5-amino-1,3,4-thiadiazol-2-yl)-N'-[(1E,2E)-3-(3-nitrophenyl)prop-2-en-1-ylidene]acetohydrazide
4% inhibition at 0.1 mM
2-hydroxy-5-[(E)-[4-[(pyridin-2-yl)sulfamoyl]phenyl]diazenyl]benzoic acid
3-(3,5-dioxo-2,3,4,5-tetrahydro-1,2,4-triazin-6-yl)-N'-[(E)-(4-nitrophenyl)methylidene]propanehydrazide
11.0% inhibition at 0.1 mM
3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
3-O-alpha-L-rhamnopyranosyl-(1-2)-beta-D-galactopyranosyl-(1-2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
3-O-alpha-L-rhamnopyronosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-gluconopyranosyl soyasapogenol B 22-o-alpha-D-glucopyranoside
potent non-competitive inhibitor in vitro, not membrane-permeable
-
4(R)-1-(benzylsulfonyl)-3-phenoxy-2-propanol
4(S)-1-(benzylsulfonyl)-3-phenoxy-2-propanol
4-(2,5-dimethylphenoxy)-N-(4-morpholin-4-ylphenyl)butanamide
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
Ca2+
-
8% inhibitin at 10 mM
Co2+
-
60% inhibitin at 10 mM
cyclic 3',5'-diguanylate
-
product inhibition is due to domain immobilization and sets an upper limit for the concentration of this second messenger in the cell
cyclic di-3',5'-(2'-fluoroguanylate)
cyclic di-3',5'-guanlylate
-
strong product inhibition
cyclic di-3',5'-guanylate
cyclic di-3',5'-inosinylic acid
cyclic di-GMP
binding at the inhibitory site mediates dimer formation and inactivation
cyclic diguanylate
noncompetitive, product inhibition
cyclic-di-3',5'-GMP
allosteric feedback, product inhibition, independent of activation status, binding induces change in conformation and protein-solvent interactions
cyclo-di-inosinylic acid
-
-
D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
isolated from Pisum sativum, specific and highly potent inhibition of enzyme
Fe2+
-
19% inhibitin at 10 mM
KCl
25 mM, slight decrease in activity
Mn2+
-
18% inhibitin at 10 mM
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
-
N'-[(E)-(2,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
17% inhibition at 0.1 mM; 6% inhibition at 0.1 mM
N'-[(E)-(2-hydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
13% inhibition at 0.1 mM
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
N-(((2-phenylethyl)amino)carbonothioyl)benzamide
N-(4-anilinophenyl)benzamide
N-(4-bromophenyl)-3-phenylpropanamide
N-(4-chlorophenyl)-3-phenylpropanamide
N-(4-methoxyphenyl)-3-phenylpropanamide
N-(4-phenoxyphenyl)-2-thiophenecarboxamide
NaCl
activity decreases with increasing concentrations of NaCl
Ni2+
-
6.5% inhibitin at 10 mM
Zn2+
-
45% inhibitin at 10 mM
[2- oxo-2-(2-oxopyrrolidin-1-yl)ethyl] 1,3-benzothiazole-6-carboxylate
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
-
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
-
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
-
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
-
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
-
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
-
2',3'-O-[4-(dihydroxyiminio)-2,6-dinitrocyclohexa-2,5-diene-1,1-diyl]guanosine 5'-triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-(gammaS)triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-(gammaS)triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-(gammaS)triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-(gammaS)triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-(gammaS)triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-(gammaS)triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-(gammaS)triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-triphosphate
-
2'-O-[2-(methylamino)benzoyl]guanosine 5'-triphosphate
-
2-hydroxy-5-[(E)-[4-[(pyridin-2-yl)sulfamoyl]phenyl]diazenyl]benzoic acid
-
2-hydroxy-5-[(E)-[4-[(pyridin-2-yl)sulfamoyl]phenyl]diazenyl]benzoic acid
-
2-hydroxy-5-[(E)-[4-[(pyridin-2-yl)sulfamoyl]phenyl]diazenyl]benzoic acid
-
2-hydroxy-5-[(E)-[4-[(pyridin-2-yl)sulfamoyl]phenyl]diazenyl]benzoic acid
-
2-hydroxy-5-[(E)-[4-[(pyridin-2-yl)sulfamoyl]phenyl]diazenyl]benzoic acid
-
2-hydroxy-5-[(E)-[4-[(pyridin-2-yl)sulfamoyl]phenyl]diazenyl]benzoic acid
-
2-hydroxy-5-[(E)-[4-[(pyridin-2-yl)sulfamoyl]phenyl]diazenyl]benzoic acid
-
3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
85% inhibition at 0.1 mM, competitive binding
3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
-
3-O-alpha-L-rhamnopyranosyl-(1-2)-beta-D-galactopyranosyl-(1-2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
-
3-O-alpha-L-rhamnopyranosyl-(1-2)-beta-D-galactopyranosyl-(1-2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
noncompetitive, inhibition is decreased by 50% in presence of 0.02 mM cyclic diguanylate, no inhibition in presence of detergents. Inhibitor affects binding of cyclic diguanylate to enzyme. In situ, inhibitor affects bacterial cellulose synthesis and enzyme activity
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
3-O-alpha-L-rhamnopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->2)-beta-D-glucuronopyranosyl soyasapogenol B 22-O-alpha-D-glucopyranoside
-
4(R)-1-(benzylsulfonyl)-3-phenoxy-2-propanol
-
-
4(R)-1-(benzylsulfonyl)-3-phenoxy-2-propanol
-
4(S)-1-(benzylsulfonyl)-3-phenoxy-2-propanol
-
-
4(S)-1-(benzylsulfonyl)-3-phenoxy-2-propanol
-
4-(2,5-dimethylphenoxy)-N-(4-morpholin-4-ylphenyl)butanamide
-
4-(2,5-dimethylphenoxy)-N-(4-morpholin-4-ylphenyl)butanamide
-
4-(2,5-dimethylphenoxy)-N-(4-morpholin-4-ylphenyl)butanamide
-
4-(2,5-dimethylphenoxy)-N-(4-morpholin-4-ylphenyl)butanamide
-
4-(2,5-dimethylphenoxy)-N-(4-morpholin-4-ylphenyl)butanamide
-
4-(2,5-dimethylphenoxy)-N-(4-morpholin-4-ylphenyl)butanamide
-
4-(2,5-dimethylphenoxy)-N-(4-morpholin-4-ylphenyl)butanamide
-
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
-
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
-
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
-
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
-
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
-
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
-
4-chloro-3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide
-
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
-
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
-
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
-
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
-
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
-
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
-
9-(3-[4-[(2-amino-6-chloro-9H-purin-9-yl)methyl]-1H-1,2,3-triazol-1-yl]propyl)-6-chloro-9H-purin-2-amine
-
c-di-GMP
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
c-di-GMP
feedback inhibition of DGC enzyme GcbC, modelling. In the crystal structure, two molecules of c-di-GMP are found to be bound between the primary and secondary I-sites of this inactive dimer. Three more residues are found to coordinate the formation of the I-site pocket where residue R363 of each monomer of GcbC forms a polar contact with residues E360 and E429 of the other GcbC monomer within the dimer complex of this protein
cyclic di-3',5'-(2'-fluoroguanylate)
-
cyclic di-3',5'-(2'-fluoroguanylate)
-
cyclic di-3',5'-(2'-fluoroguanylate)
-
cyclic di-3',5'-(2'-fluoroguanylate)
-
cyclic di-3',5'-(2'-fluoroguanylate)
-
cyclic di-3',5'-(2'-fluoroguanylate)
-
cyclic di-3',5'-(2'-fluoroguanylate)
-
cyclic di-3',5'-guanylate
noncompetitive product inhibition at an allosteric binding site fully contained within the GGDEF domain. Core of the binding site is an RXXD motif formed by residues R359, D362, and R390
cyclic di-3',5'-guanylate
product inhibition, allosteric feedback regualtion is not affected by the activation state of enzyme
cyclic di-3',5'-guanylate
noncompetitive product inhibition, binding causes crosslinking of diguanylate cyclase (GGDEF) domains within the dimer, integrity of only one inhibitory site required for inhibition
cyclic di-3',5'-guanylate
-
product inhibition, allosteric, negative feedback, slow intrinsic off-rate of cyclic di-3,5-guanylate from RxxD inhibitory-site motif, inhibitory action depends on tetramer formation and subsequent conformational change in dimeric enzyme from global to elongated shape
cyclic di-3',5'-guanylate
-
product inhibition, allosteric, negative feedback, slow intrinsic off-rate of cyclic di-3,5-guanylate from RxxD inhibitory-site motif, inhibitory action depends on tetramer formation and subsequent conformational change in dimeric enzyme from global to elongated shape
cyclic di-3',5'-guanylate
-
product inhibition, allosteric, negative feedback, slow intrinsic off-rate of cyclic di-3,5-guanylate from RxxD inhibitory-site motif, inhibitory action depends on tetramer formation and subsequent conformational change in dimeric enzyme from global to elongated shape
cyclic di-3',5'-guanylate
-
product inhibition, allosteric, negative feedback, slow intrinsic off-rate of cyclic di-3,5-guanylate from RxxD inhibitory-site motif, inhibitory action depends on tetramer formation and subsequent conformational change in dimeric enzyme from global to elongated shape
cyclic di-3',5'-guanylate
-
product inhibition
cyclic di-3',5'-inosinylic acid
-
cyclic di-3',5'-inosinylic acid
-
cyclic di-3',5'-inosinylic acid
-
cyclic di-3',5'-inosinylic acid
-
cyclic di-3',5'-inosinylic acid
-
cyclic di-3',5'-inosinylic acid
-
cyclic di-3',5'-inosinylic acid
-
ebselen
-
eprosartan
-
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
LP3134; LP3134
-
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
LP3134
-
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
LP3134
-
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
LP3134; LP3134
-
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
LP3134
-
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
LP3134
-
N'-((1E)-(4-ethoxy-3-[(8-oxo-1,5,6,8-tetrahydro-2H-1,5-methanopyrido[1,2-a][1,5]diazocin-3(4H)-yl)methylphenyl)methylene)]-3,4,5-trihydroxybenzohydrazide
LP3134
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
83.4% inhibition at 0.1 mM, competitive binding
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
-
N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide
-
N-(((2-phenylethyl)amino)carbonothioyl)benzamide
-
-
N-(((2-phenylethyl)amino)carbonothioyl)benzamide
significantly reduces the total concentration of c-di-GMP in Vibrio cholerae
N-(4-anilinophenyl)benzamide
-
N-(4-anilinophenyl)benzamide
-
N-(4-anilinophenyl)benzamide
-
N-(4-anilinophenyl)benzamide
-
-
N-(4-anilinophenyl)benzamide
-
N-(4-anilinophenyl)benzamide
-
N-(4-anilinophenyl)benzamide
-
N-(4-anilinophenyl)benzamide
significantly reduces the total concentration of c-di-GMP in Vibrio cholerae
N-(4-anilinophenyl)benzamide
-
N-(4-bromophenyl)-3-phenylpropanamide
-
-
N-(4-bromophenyl)-3-phenylpropanamide
-
N-(4-chlorophenyl)-3-phenylpropanamide
-
-
N-(4-chlorophenyl)-3-phenylpropanamide
-
N-(4-methoxyphenyl)-3-phenylpropanamide
-
-
N-(4-methoxyphenyl)-3-phenylpropanamide
-
N-(4-phenoxyphenyl)-2-thiophenecarboxamide
-
-
N-(4-phenoxyphenyl)-2-thiophenecarboxamide
-
[2- oxo-2-(2-oxopyrrolidin-1-yl)ethyl] 1,3-benzothiazole-6-carboxylate
-
[2- oxo-2-(2-oxopyrrolidin-1-yl)ethyl] 1,3-benzothiazole-6-carboxylate
-
[2- oxo-2-(2-oxopyrrolidin-1-yl)ethyl] 1,3-benzothiazole-6-carboxylate
-
[2- oxo-2-(2-oxopyrrolidin-1-yl)ethyl] 1,3-benzothiazole-6-carboxylate
-
[2- oxo-2-(2-oxopyrrolidin-1-yl)ethyl] 1,3-benzothiazole-6-carboxylate
-
[2- oxo-2-(2-oxopyrrolidin-1-yl)ethyl] 1,3-benzothiazole-6-carboxylate
-
[2- oxo-2-(2-oxopyrrolidin-1-yl)ethyl] 1,3-benzothiazole-6-carboxylate
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases; screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases; screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
virtual screening of the ZINC database, in silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD. The compounds retrieved from the pharmacophore searches are docked into the active site of PleD, by means of Molegro Virtual Docker (MVD) software (CLCbio), using the three-dimensional structure of PleD (PDB ID 2V0N). Binding of N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide to PleD is stabilized by polar interactions with residues surrounding the GTP binding pocket, namely, N335, D344, and R366. N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide share a hydrazine moiety with the previously identified inhibitors LP3134 and LP4010, which has been predicted to interact with the amino group of N335
-
additional information
-
virtual screening of the ZINC database, in silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD. The compounds retrieved from the pharmacophore searches are docked into the active site of PleD, by means of Molegro Virtual Docker (MVD) software (CLCbio), using the three-dimensional structure of PleD (PDB ID 2V0N). Binding of N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide to PleD is stabilized by polar interactions with residues surrounding the GTP binding pocket, namely, N335, D344, and R366. N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide share a hydrazine moiety with the previously identified inhibitors LP3134 and LP4010, which has been predicted to interact with the amino group of N335
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
-
the reaction shows non-competitive product inhibition only at comparatively large c-di-GMP concentration
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2'(3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases; screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2'(3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases; screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2'(3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
enzyme PA0847 demonstrates no significant product inhibition, though the key residues of two I-sites for c-di-GMP binding are conserved in its GGDEF domain. ENzyme PA0847 contains the canonical product inhibition site (primary I site) of the RxxD motif, which is located upstream of the conserved GGDEF motif. It also has a secondary inhibition site which is conserved in GGDEF domains that can undergo feedback inhibition. These two sites may form a pocket for c-di-GMP binding
-
additional information
virtual screening of the ZINC database, in silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD. N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide are also tested on the YfiNHAMP-GGDEF and WspR DGCs from Pseudomonas aeruginosa, two DGCs which are in the on state and therefore do not require preactivation; virtual screening of the ZINC database, in silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD. N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide are also tested on the YfiNHAMP-GGDEF and WspR DGCs from Pseudomonas aeruginosa, two DGCs which are in the on state and therefore do not require preactivation
-
additional information
virtual screening of the ZINC database, in silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD. N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide are also tested on the YfiNHAMP-GGDEF and WspR DGCs from Pseudomonas aeruginosa, two DGCs which are in the on state and therefore do not require preactivation; virtual screening of the ZINC database, in silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD. N'-[(E)-(3,4-dihydroxyphenyl)methylidene]-4-methyl-3-nitrobenzene-1-sulfonohydrazide and 3-nitro-N'-[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1-sulfonohydrazide are also tested on the YfiNHAMP-GGDEF and WspR DGCs from Pseudomonas aeruginosa, two DGCs which are in the on state and therefore do not require preactivation
-
additional information
GcbC has a primary inhibitory site with the previously characterized RXXD motif. The RXXD motif is found at residues R410 to D413 of GcbC. Residue R409 also makes contact with a c-di-GMP molecule. In addition to the primary I-site, GcbC also contains a secondary I-site at position R366 that completes GcbC's regulatory c-di-GMP binding site. The autoinhibitory site (I-site) of a diguanylate cyclase is a necessary element for interaction and signaling with an effector protein
-
additional information
-
GcbC has a primary inhibitory site with the previously characterized RXXD motif. The RXXD motif is found at residues R410 to D413 of GcbC. Residue R409 also makes contact with a c-di-GMP molecule. In addition to the primary I-site, GcbC also contains a secondary I-site at position R366 that completes GcbC's regulatory c-di-GMP binding site. The autoinhibitory site (I-site) of a diguanylate cyclase is a necessary element for interaction and signaling with an effector protein
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2'(3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
screenings for chemicals capable of inhibiting the c-di-GMP synthesis activity of DGCs have been performed in order to inhibit bacterial biofilm formation. 2',3'-O-(2,4,6-trinitrophenyl) (TNP)- and 2' (3')-O-(N-methylanthraniloyl) (MANT)-substituted nucleotides are potent inhibitors of guanylyl and adenylyl cyclases
-
additional information
not inhibitory: cyclic di-GMP
-
additional information
-
not inhibitory: cyclic di-GMP
-
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evolution
close LIC13137 orthologues, with more than 23% identity, are exclusively found in pathogenic species of the Leptospira genus
evolution
proteins with a conserved C-terminal GGDEF domain act as DGCs, whereas proteins containing EAL or HD-GYP domains act as c-di-GMP-specific phosphodiesterases (PDEs). Vibrio cholerae genome typically encodes 31 proteins with a GGDEF domain
evolution
Pseudomonas putida strain KT2440 has dozens of DGC/PDE-encoding genes in its genome. GcsA homologues are also found in strains of several other Pseudomonas species, including Pseudomonas monteilii strain SB3078, Pseudomonas plecoglossicida strain NyZ12, and Pseudomonas cremoricolorata strain ND07, which share more than 79% amino acid sequence identity with one another, but no GcsA homologues are found in the model organisms Pseudomonas aeruginosa strains PAO1 and PA14, Pseudomonas fluorescens strain Pfl5, and Pseudomonas syringae pv. tomato strain DC3000
evolution
the GGDEF domain of HsbD has the conserved RxxDmotif (293-296 aa), which forms the allosteric inhibitory site (I-site) of diguanylate cyclases
evolution
-
the GGDEF domain of HsbD has the conserved RxxDmotif (293-296 aa), which forms the allosteric inhibitory site (I-site) of diguanylate cyclases
-
evolution
-
Pseudomonas putida strain KT2440 has dozens of DGC/PDE-encoding genes in its genome. GcsA homologues are also found in strains of several other Pseudomonas species, including Pseudomonas monteilii strain SB3078, Pseudomonas plecoglossicida strain NyZ12, and Pseudomonas cremoricolorata strain ND07, which share more than 79% amino acid sequence identity with one another, but no GcsA homologues are found in the model organisms Pseudomonas aeruginosa strains PAO1 and PA14, Pseudomonas fluorescens strain Pfl5, and Pseudomonas syringae pv. tomato strain DC3000
-
evolution
-
proteins with a conserved C-terminal GGDEF domain act as DGCs, whereas proteins containing EAL or HD-GYP domains act as c-di-GMP-specific phosphodiesterases (PDEs). Vibrio cholerae genome typically encodes 31 proteins with a GGDEF domain
-
evolution
-
Pseudomonas putida strain KT2440 has dozens of DGC/PDE-encoding genes in its genome. GcsA homologues are also found in strains of several other Pseudomonas species, including Pseudomonas monteilii strain SB3078, Pseudomonas plecoglossicida strain NyZ12, and Pseudomonas cremoricolorata strain ND07, which share more than 79% amino acid sequence identity with one another, but no GcsA homologues are found in the model organisms Pseudomonas aeruginosa strains PAO1 and PA14, Pseudomonas fluorescens strain Pfl5, and Pseudomonas syringae pv. tomato strain DC3000
-
evolution
-
Pseudomonas putida strain KT2440 has dozens of DGC/PDE-encoding genes in its genome. GcsA homologues are also found in strains of several other Pseudomonas species, including Pseudomonas monteilii strain SB3078, Pseudomonas plecoglossicida strain NyZ12, and Pseudomonas cremoricolorata strain ND07, which share more than 79% amino acid sequence identity with one another, but no GcsA homologues are found in the model organisms Pseudomonas aeruginosa strains PAO1 and PA14, Pseudomonas fluorescens strain Pfl5, and Pseudomonas syringae pv. tomato strain DC3000
-
evolution
-
proteins with a conserved C-terminal GGDEF domain act as DGCs, whereas proteins containing EAL or HD-GYP domains act as c-di-GMP-specific phosphodiesterases (PDEs). Vibrio cholerae genome typically encodes 31 proteins with a GGDEF domain
-
malfunction
a deletion mutant shows a marked reduction in biofilm formation
malfunction
-
Borrelia burgdorferi strains that lack Rrp1 or that constitutively produce elevated levels of Rrp1 are generated and analyzed for their ability to infect and transit between mice and Ixodes ticks. Rrp1, and by extension, c-di-GMP, are not required for murine infection, but are required for the successful establishment of a productive population of Borrelia burgdorferi in ticks
malfunction
deletion mutant shows a biofilm formation defect, a 4fold better swarming motility and a significant reduction of c-di-GMP levels. No correlation between leveles of c-di-GMP and the observed phenotypic output with regard to swarming motilities and extracellular polysaccharide (EPS) is observed
malfunction
deletion mutant shows a biofilm formation defect, a better swarming motility and a significant reduction of c-di-GMP levels. No correlation between leveles of c-di-GMP and the observed phenotypic output with regard to swarming motilities and extracellular polysaccharide (EPS) is observed
malfunction
double mutant containing a deleted sadC and PA1107 gene show a more severe biofilm defect compared to single mutant
malfunction
-
heterologous expression of cdgB in Escherichia coli results in increased production of extracellular matrix in colonies and enhanced surface attachment of cells in standing liquid cultures. In Streptomyces coelicolor, both overexpression and deletion of cdgB inhibits aerial-mycelium formation, and overexpression also inhibits production of the antibiotic actinorhodin, implicating c-di-GMP in the regulation of developmental processes in Streptomyces
malfunction
over-expression of PA1107 leads to enhanced c-di-GMP levels
malfunction
-
overexpression of YddV stimulates production of poly-N-acetylglucosamine (PNAG), an extracellular polysaccharaide able to promote biofilm formation, by triggering expression of pgaABCD, the PNAG biosynthetic operon
malfunction
BpeGReg266 (residues 1-266) and BpeGReg296 (residues 1-296), which only contain the globin and middle domains, can inhibit bacterial motility. The distal residues of the globin domain affect diguanylate cyclase activity, Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
malfunction
-
deletion of hns or rsmB in the gcpAD418A site-directed mutant restored its Pel production and pelD expression, demonstrating that H-NS and RsmB contribute to the GcpA-dependent regulation of Pel in Dickeya dadantii
malfunction
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
malfunction
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
malfunction
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
malfunction
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
malfunction
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
malfunction
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
malfunction
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
malfunction
inactivation of PA3177 renders Pseudomonas aeruginosa strain PAO1 biofilms susceptible to tobramycin and hydrogen peroxide. Inactivation of PA3177 also eliminates the recalcitrance of biofilms to killing by tobramycin, with multicopy expression of PA3177 but not PA3177_GGAAF harboring substitutions in the active site, restoring tolerance to wild-type levels. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation. Inactivation of PA3177 correlates with reduced c-di-GMP levels in biofilm but not planktonic cells. Inactivation of PA3177 has no effect on attachment and the formation of mature biofilms characterized by a three-dimensional biofilm architecture
malfunction
mutation in the GGDEF motif (from GGDEF to GGAAF) abolishes the c-di-GMP synthesis ability of GcsA
malfunction
mutation of gene slr1143 results in an aberrant phototactic behaviour in red light. DELTAslr1143 and Slr1143 overexpression mutant lines in different light qualities suggesting that motility of Synechocystis cells can be affected by the cellular levels of c-di-GMP, but this appears to not be the exclusive reason for differences in motility
malfunction
mutation of residues at the I-site of a DGC disrupts the interaction with its target receptor. By creating various substitutions to a DGC's I-site, it is shown that signaling between a DGC (GcbC) and its target protein (LapD) is a combined function of the I-site-dependent protein-protein interaction and the level of c-di-GMP production. Disruption of the I-site of GcbC leads to deregulation of c-di-GMP production, an increase in the c-di-GMP level and a concomitant increase in c-di-GMP-regulated processes
malfunction
mutations at the central positions of the GGEEF sequence are detrimental to the functional activity of the enzyme. This DGC lacks the site for allosteric inhibition found in the other DGCs of Vibrio cholerae, suggesting a different mode of inhibitory control in this DGC
malfunction
nutrient starvation or the accumulation of byproducts in the medium may result in polar localization of DgcZ in stationary phase. Restoring nutrient-sufficient conditions results in decreased levels and dispersed localization of DgcZ
malfunction
-
overexpression of cdgH results in a high amount of c-di-GMP accumulation in the cell
malfunction
overexpression of SadC in Pseudomonas aeruginosa strain PAO1 totally inhibits swimming motility and significantly enhances the production of exopolysaccharide Psl. SadC lacking transmembrane domains (SadC300-487) cannot localize on cytoplasmic membrane and form cluster, loses the ability to inhibit the swimming and twitching motility, and shows the attenuated activity to promote Psl production despite that SadC300-487 is able to catalyze the synthesize of c-di-GMP in vitro and in vivo. Truncated enzyme version SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but version SadC323-487 cannot, structure-function analysis, overview
malfunction
-
the CdgD deletion mutant shows significant alteration in the biofilm formation compared to wild-type. Deletion of cdgD causes an increase in motility
malfunction
the CdgD deletion mutant shows significant alteration in the biofilm formation compared to wild-type. Deletion of cdgD causes an increase in motility
malfunction
the inactive heme-free H93A mutant is primarily octameric, suggesting that catalytically active dimer formation requires heme binding
malfunction
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
overexpression of SadC in Pseudomonas aeruginosa strain PAO1 totally inhibits swimming motility and significantly enhances the production of exopolysaccharide Psl. SadC lacking transmembrane domains (SadC300-487) cannot localize on cytoplasmic membrane and form cluster, loses the ability to inhibit the swimming and twitching motility, and shows the attenuated activity to promote Psl production despite that SadC300-487 is able to catalyze the synthesize of c-di-GMP in vitro and in vivo. Truncated enzyme version SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but version SadC323-487 cannot, structure-function analysis, overview
-
malfunction
-
inactivation of PA3177 renders Pseudomonas aeruginosa strain PAO1 biofilms susceptible to tobramycin and hydrogen peroxide. Inactivation of PA3177 also eliminates the recalcitrance of biofilms to killing by tobramycin, with multicopy expression of PA3177 but not PA3177_GGAAF harboring substitutions in the active site, restoring tolerance to wild-type levels. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation. Inactivation of PA3177 correlates with reduced c-di-GMP levels in biofilm but not planktonic cells. Inactivation of PA3177 has no effect on attachment and the formation of mature biofilms characterized by a three-dimensional biofilm architecture
-
malfunction
-
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
-
malfunction
-
BpeGReg266 (residues 1-266) and BpeGReg296 (residues 1-296), which only contain the globin and middle domains, can inhibit bacterial motility. The distal residues of the globin domain affect diguanylate cyclase activity, Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
overexpression of SadC in Pseudomonas aeruginosa strain PAO1 totally inhibits swimming motility and significantly enhances the production of exopolysaccharide Psl. SadC lacking transmembrane domains (SadC300-487) cannot localize on cytoplasmic membrane and form cluster, loses the ability to inhibit the swimming and twitching motility, and shows the attenuated activity to promote Psl production despite that SadC300-487 is able to catalyze the synthesize of c-di-GMP in vitro and in vivo. Truncated enzyme version SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but version SadC323-487 cannot, structure-function analysis, overview
-
malfunction
-
inactivation of PA3177 renders Pseudomonas aeruginosa strain PAO1 biofilms susceptible to tobramycin and hydrogen peroxide. Inactivation of PA3177 also eliminates the recalcitrance of biofilms to killing by tobramycin, with multicopy expression of PA3177 but not PA3177_GGAAF harboring substitutions in the active site, restoring tolerance to wild-type levels. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation. Inactivation of PA3177 correlates with reduced c-di-GMP levels in biofilm but not planktonic cells. Inactivation of PA3177 has no effect on attachment and the formation of mature biofilms characterized by a three-dimensional biofilm architecture
-
malfunction
-
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
mutation in the GGDEF motif (from GGDEF to GGAAF) abolishes the c-di-GMP synthesis ability of GcsA
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
overexpression of SadC in Pseudomonas aeruginosa strain PAO1 totally inhibits swimming motility and significantly enhances the production of exopolysaccharide Psl. SadC lacking transmembrane domains (SadC300-487) cannot localize on cytoplasmic membrane and form cluster, loses the ability to inhibit the swimming and twitching motility, and shows the attenuated activity to promote Psl production despite that SadC300-487 is able to catalyze the synthesize of c-di-GMP in vitro and in vivo. Truncated enzyme version SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but version SadC323-487 cannot, structure-function analysis, overview
-
malfunction
-
inactivation of PA3177 renders Pseudomonas aeruginosa strain PAO1 biofilms susceptible to tobramycin and hydrogen peroxide. Inactivation of PA3177 also eliminates the recalcitrance of biofilms to killing by tobramycin, with multicopy expression of PA3177 but not PA3177_GGAAF harboring substitutions in the active site, restoring tolerance to wild-type levels. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation. Inactivation of PA3177 correlates with reduced c-di-GMP levels in biofilm but not planktonic cells. Inactivation of PA3177 has no effect on attachment and the formation of mature biofilms characterized by a three-dimensional biofilm architecture
-
malfunction
-
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
overexpression of SadC in Pseudomonas aeruginosa strain PAO1 totally inhibits swimming motility and significantly enhances the production of exopolysaccharide Psl. SadC lacking transmembrane domains (SadC300-487) cannot localize on cytoplasmic membrane and form cluster, loses the ability to inhibit the swimming and twitching motility, and shows the attenuated activity to promote Psl production despite that SadC300-487 is able to catalyze the synthesize of c-di-GMP in vitro and in vivo. Truncated enzyme version SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but version SadC323-487 cannot, structure-function analysis, overview
-
malfunction
-
inactivation of PA3177 renders Pseudomonas aeruginosa strain PAO1 biofilms susceptible to tobramycin and hydrogen peroxide. Inactivation of PA3177 also eliminates the recalcitrance of biofilms to killing by tobramycin, with multicopy expression of PA3177 but not PA3177_GGAAF harboring substitutions in the active site, restoring tolerance to wild-type levels. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation. Inactivation of PA3177 correlates with reduced c-di-GMP levels in biofilm but not planktonic cells. Inactivation of PA3177 has no effect on attachment and the formation of mature biofilms characterized by a three-dimensional biofilm architecture
-
malfunction
-
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
overexpression of SadC in Pseudomonas aeruginosa strain PAO1 totally inhibits swimming motility and significantly enhances the production of exopolysaccharide Psl. SadC lacking transmembrane domains (SadC300-487) cannot localize on cytoplasmic membrane and form cluster, loses the ability to inhibit the swimming and twitching motility, and shows the attenuated activity to promote Psl production despite that SadC300-487 is able to catalyze the synthesize of c-di-GMP in vitro and in vivo. Truncated enzyme version SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but version SadC323-487 cannot, structure-function analysis, overview
-
malfunction
-
inactivation of PA3177 renders Pseudomonas aeruginosa strain PAO1 biofilms susceptible to tobramycin and hydrogen peroxide. Inactivation of PA3177 also eliminates the recalcitrance of biofilms to killing by tobramycin, with multicopy expression of PA3177 but not PA3177_GGAAF harboring substitutions in the active site, restoring tolerance to wild-type levels. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation. Inactivation of PA3177 correlates with reduced c-di-GMP levels in biofilm but not planktonic cells. Inactivation of PA3177 has no effect on attachment and the formation of mature biofilms characterized by a three-dimensional biofilm architecture
-
malfunction
-
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
overexpression of SadC in Pseudomonas aeruginosa strain PAO1 totally inhibits swimming motility and significantly enhances the production of exopolysaccharide Psl. SadC lacking transmembrane domains (SadC300-487) cannot localize on cytoplasmic membrane and form cluster, loses the ability to inhibit the swimming and twitching motility, and shows the attenuated activity to promote Psl production despite that SadC300-487 is able to catalyze the synthesize of c-di-GMP in vitro and in vivo. Truncated enzyme version SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but version SadC323-487 cannot, structure-function analysis, overview
-
malfunction
-
inactivation of PA3177 renders Pseudomonas aeruginosa strain PAO1 biofilms susceptible to tobramycin and hydrogen peroxide. Inactivation of PA3177 also eliminates the recalcitrance of biofilms to killing by tobramycin, with multicopy expression of PA3177 but not PA3177_GGAAF harboring substitutions in the active site, restoring tolerance to wild-type levels. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation. Inactivation of PA3177 correlates with reduced c-di-GMP levels in biofilm but not planktonic cells. Inactivation of PA3177 has no effect on attachment and the formation of mature biofilms characterized by a three-dimensional biofilm architecture
-
malfunction
-
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
-
malfunction
-
the CdgD deletion mutant shows significant alteration in the biofilm formation compared to wild-type. Deletion of cdgD causes an increase in motility
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
BpeGReg266 (residues 1-266) and BpeGReg296 (residues 1-296), which only contain the globin and middle domains, can inhibit bacterial motility. The distal residues of the globin domain affect diguanylate cyclase activity, Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
-
malfunction
-
BpeGReg266 (residues 1-266) and BpeGReg296 (residues 1-296), which only contain the globin and middle domains, can inhibit bacterial motility. The distal residues of the globin domain affect diguanylate cyclase activity, Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
-
malfunction
-
mutation of residues at the I-site of a DGC disrupts the interaction with its target receptor. By creating various substitutions to a DGC's I-site, it is shown that signaling between a DGC (GcbC) and its target protein (LapD) is a combined function of the I-site-dependent protein-protein interaction and the level of c-di-GMP production. Disruption of the I-site of GcbC leads to deregulation of c-di-GMP production, an increase in the c-di-GMP level and a concomitant increase in c-di-GMP-regulated processes
-
malfunction
-
mutations at the central positions of the GGEEF sequence are detrimental to the functional activity of the enzyme. This DGC lacks the site for allosteric inhibition found in the other DGCs of Vibrio cholerae, suggesting a different mode of inhibitory control in this DGC
-
malfunction
-
mutation in the GGDEF motif (from GGDEF to GGAAF) abolishes the c-di-GMP synthesis ability of GcsA
-
malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
overexpression of SadC in Pseudomonas aeruginosa strain PAO1 totally inhibits swimming motility and significantly enhances the production of exopolysaccharide Psl. SadC lacking transmembrane domains (SadC300-487) cannot localize on cytoplasmic membrane and form cluster, loses the ability to inhibit the swimming and twitching motility, and shows the attenuated activity to promote Psl production despite that SadC300-487 is able to catalyze the synthesize of c-di-GMP in vitro and in vivo. Truncated enzyme version SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but version SadC323-487 cannot, structure-function analysis, overview
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malfunction
-
inactivation of PA3177 renders Pseudomonas aeruginosa strain PAO1 biofilms susceptible to tobramycin and hydrogen peroxide. Inactivation of PA3177 also eliminates the recalcitrance of biofilms to killing by tobramycin, with multicopy expression of PA3177 but not PA3177_GGAAF harboring substitutions in the active site, restoring tolerance to wild-type levels. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation. Inactivation of PA3177 correlates with reduced c-di-GMP levels in biofilm but not planktonic cells. Inactivation of PA3177 has no effect on attachment and the formation of mature biofilms characterized by a three-dimensional biofilm architecture
-
malfunction
-
weak product feedback inhibition is found in PA0847 GGDEF domain suggesting that allosteric regulation from the sensory domain could play a dominant role in the control of intracellular c-di-GMP synthesis
-
malfunction
-
mutations at the central positions of the GGEEF sequence are detrimental to the functional activity of the enzyme. This DGC lacks the site for allosteric inhibition found in the other DGCs of Vibrio cholerae, suggesting a different mode of inhibitory control in this DGC
-
malfunction
-
mutation in the GGDEF motif (from GGDEF to GGAAF) abolishes the c-di-GMP synthesis ability of GcsA
-
malfunction
-
mutations at the central positions of the GGEEF sequence are detrimental to the functional activity of the enzyme. This DGC lacks the site for allosteric inhibition found in the other DGCs of Vibrio cholerae, suggesting a different mode of inhibitory control in this DGC
-
malfunction
-
the CdgD deletion mutant shows significant alteration in the biofilm formation compared to wild-type. Deletion of cdgD causes an increase in motility
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malfunction
-
enzyme inhibition by inhibitors causes inhibition of biofilm formation of the organism
-
malfunction
-
deletion of hns or rsmB in the gcpAD418A site-directed mutant restored its Pel production and pelD expression, demonstrating that H-NS and RsmB contribute to the GcpA-dependent regulation of Pel in Dickeya dadantii
-
metabolism
-
AdrA acts independently of the Gac system, which is also consistent with the activity of AdrA in the SadB branch of the signaling pathway, hypothetical regulatory model for flagellar synthesis in Pseudomonas fluorescens strain F113, overview
metabolism
BrlR is a c-di-GMP responsive transcriptional regulator. Inactivation of PA3177 coincides with BrlR abundance being reduced in biofilms and unable to bind to PmexE, inactivation of PA3177 coincides with reduced BrlR protein abundance
metabolism
-
cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
metabolism
-
cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
metabolism
-
cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
metabolism
-
cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
metabolism
-
cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
metabolism
cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
metabolism
cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
metabolism
DGC SadC is more effective than DGC WspR in promoting Psl synthesis in Pseudomonas aeruginosa strain PAO1
metabolism
DgcZ shows interaction with FrdB, a subunit of the fumarate reductase complex (FRD) involved in anaerobic respiration and in control of flagellum assembly, determined by coimmunoprecipitation analysis and bacterial-two-hybrid assay. The FRD complex is required for the increase in DgcZ-mediated biofilm formation upon induction of oxidative stress by addition of paraquat
metabolism
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propose of a pathway consisting of GcpA-H-NS-RsmB-RsmA-pelD, that controls Pel production in Dickeya dadantii, overview. Of the two PDEs involved in the regulation of Pels, only EGcpB regulates pelD expression through the same pathway as GcpA. GcpA regulates Pel through the Rsm system, H-NS is involved in the GcpA-Rsm pathway. H-NS and Rsm play different roles in the GcpAdependent regulation of swimming motility and T3SS, H-NS is not involved in the regulation of T3SS in either the Dickeya dadantii wild-type or gcpAD418A strain
metabolism
the HptB pathway controls biofilm formation, swarming motility by involving both HsbD and the anti-anti-sigma factor HsbA. The rewiring of c-di-GMP signaling into the HptB cascade relies on the original interaction between HsbD and HsbA and on the control of HsbD dynamic localization at the cell poles. The hptB gene cluster merges with flagellar and chemotaxis genes to evolve into a distinct Pseudomonas aeruginosa-specific flagellar locus. HsbD is a diguanylate cyclase which activity intersects with the HptB regulatory pathway. DGC enzymes SadC and HsbD differentially impact HptB-dependent phenotypes
metabolism
-
DGC SadC is more effective than DGC WspR in promoting Psl synthesis in Pseudomonas aeruginosa strain PAO1
-
metabolism
-
the HptB pathway controls biofilm formation, swarming motility by involving both HsbD and the anti-anti-sigma factor HsbA. The rewiring of c-di-GMP signaling into the HptB cascade relies on the original interaction between HsbD and HsbA and on the control of HsbD dynamic localization at the cell poles. The hptB gene cluster merges with flagellar and chemotaxis genes to evolve into a distinct Pseudomonas aeruginosa-specific flagellar locus. HsbD is a diguanylate cyclase which activity intersects with the HptB regulatory pathway. DGC enzymes SadC and HsbD differentially impact HptB-dependent phenotypes
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metabolism
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BrlR is a c-di-GMP responsive transcriptional regulator. Inactivation of PA3177 coincides with BrlR abundance being reduced in biofilms and unable to bind to PmexE, inactivation of PA3177 coincides with reduced BrlR protein abundance
-
metabolism
-
AdrA acts independently of the Gac system, which is also consistent with the activity of AdrA in the SadB branch of the signaling pathway, hypothetical regulatory model for flagellar synthesis in Pseudomonas fluorescens strain F113, overview
-
metabolism
-
DGC SadC is more effective than DGC WspR in promoting Psl synthesis in Pseudomonas aeruginosa strain PAO1
-
metabolism
-
BrlR is a c-di-GMP responsive transcriptional regulator. Inactivation of PA3177 coincides with BrlR abundance being reduced in biofilms and unable to bind to PmexE, inactivation of PA3177 coincides with reduced BrlR protein abundance
-
metabolism
-
DGC SadC is more effective than DGC WspR in promoting Psl synthesis in Pseudomonas aeruginosa strain PAO1
-
metabolism
-
BrlR is a c-di-GMP responsive transcriptional regulator. Inactivation of PA3177 coincides with BrlR abundance being reduced in biofilms and unable to bind to PmexE, inactivation of PA3177 coincides with reduced BrlR protein abundance
-
metabolism
-
DGC SadC is more effective than DGC WspR in promoting Psl synthesis in Pseudomonas aeruginosa strain PAO1
-
metabolism
-
BrlR is a c-di-GMP responsive transcriptional regulator. Inactivation of PA3177 coincides with BrlR abundance being reduced in biofilms and unable to bind to PmexE, inactivation of PA3177 coincides with reduced BrlR protein abundance
-
metabolism
-
DGC SadC is more effective than DGC WspR in promoting Psl synthesis in Pseudomonas aeruginosa strain PAO1
-
metabolism
-
BrlR is a c-di-GMP responsive transcriptional regulator. Inactivation of PA3177 coincides with BrlR abundance being reduced in biofilms and unable to bind to PmexE, inactivation of PA3177 coincides with reduced BrlR protein abundance
-
metabolism
-
DGC SadC is more effective than DGC WspR in promoting Psl synthesis in Pseudomonas aeruginosa strain PAO1
-
metabolism
-
BrlR is a c-di-GMP responsive transcriptional regulator. Inactivation of PA3177 coincides with BrlR abundance being reduced in biofilms and unable to bind to PmexE, inactivation of PA3177 coincides with reduced BrlR protein abundance
-
metabolism
-
DGC SadC is more effective than DGC WspR in promoting Psl synthesis in Pseudomonas aeruginosa strain PAO1
-
metabolism
-
BrlR is a c-di-GMP responsive transcriptional regulator. Inactivation of PA3177 coincides with BrlR abundance being reduced in biofilms and unable to bind to PmexE, inactivation of PA3177 coincides with reduced BrlR protein abundance
-
metabolism
Vibrio cholerae serotype O1 A1552
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cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. Effectors, e.g. LapD, can sense the c-di-GMP signal from a specific DGC. Relationship between DGC-effector contact and catalysis. Dynamics of a signaling complex, distinguishing interaction versus signaling, and relationship between local and global signaling, overview. Modeling
-
metabolism
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propose of a pathway consisting of GcpA-H-NS-RsmB-RsmA-pelD, that controls Pel production in Dickeya dadantii, overview. Of the two PDEs involved in the regulation of Pels, only EGcpB regulates pelD expression through the same pathway as GcpA. GcpA regulates Pel through the Rsm system, H-NS is involved in the GcpA-Rsm pathway. H-NS and Rsm play different roles in the GcpAdependent regulation of swimming motility and T3SS, H-NS is not involved in the regulation of T3SS in either the Dickeya dadantii wild-type or gcpAD418A strain
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physiological function
-
in Gram-negative bacteria production of of cyclic di-3',5'-guanylate, c-di-GMP, is the main trigger for production of extracellular polysaccharides and for biofilm formation
physiological function
-
SwDGC is capable of affecting extracellular polysaccharide matrix production, presumably by altering intracellular c-di-GMP levels
physiological function
a deletion mutation in the pgn_1932 gene has a significant effect on the intracellular cyclic-di-GMP level in Porphyromonas gingivalis. Expression of the fimA and rgpA genes, encoding the major protein subunit of fimbriae and an arginine-specific proteinase, respectively, is downregulated in the pgn_1932 mutant. Correspondingly, FimA protein production and the fimbrial display on the mutant are significantly reduced. Mutations in the pgn_1932 gene also have a significant impact on the adhesive and invasive capabilities of P.orphyromonas gingivalis, which are required for its pathogenicity
physiological function
Dcsbis tightly coordinates cell motility without markedly affecting biofilm formation and is a diguanylate cyclase with a catalytic activity much higher than those of many other diguanylate cyclases
physiological function
DgcA negatively affects virulence, extracellular polymeric substances production, bacterial autoaggregation and motility, but positively triggers biofilm formation via modulating the intracellular cyclic di-GMP levels. Deletion of dgcA substantially increases Xoo virulence against two different rice cultivars. 349 differentially expressed genes are controlled by DgcA
physiological function
DgcP negatively regulates motility and positively controls biofilm formation. Overexpression of the DgcP gene leads to increased exopolysaccharide production and upregulation of the type VI secretion system, in turn, it represses the type III secretion system, a hallmark of chronic infections and persistence for P.seudomonasaeruginosa. Deletion of the DgcP gene reduces the virulence in a mouse acute lung injury model
physiological function
diguanylate cyclase YfiN acts as a bifunctional protein that produces cyclic 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 Escherichia coli. YfiN localizes to the Z ring by interacting with early division proteins and stalls cell division by preventing the initiation of septal peptidoglycan synthesis
physiological function
-
DosD is a direct oxygen-sensing diguanylate cyclase playing a regulatory role in biofilm formation by Shewanella putrefaciens CN32 under aerobic conditions. The activity of DosD culminates to synthesis of cyclic diguanylate in the presence of oxygen. DosD regulates the transcription of the bpfA operon which encodes seven proteins including a large repetitive adhesin BpfA and its cognate type I secretion system (TISS). Regulation of DosD in aerobic biofilms is heavily dependent on an adhesin BpfA and the TISS
physiological function
-
ectopic expression of VCA0965 in ibrio. cholerae causes a 3fold reduction in flagellar-based motility. An RXXD allosteric inhibition mutant of VCA0965 strongly inhibits motility and stimulates biofilm formation. This activity is lost when the active site of VCA0965 is mutated to AGDAF, suggesting that VCA0965 synthesizes cyclic-di-GMP. Ectopic expression of VCA0965 and VCA0965 containing a mutation in its RXXD motif significantly increases the intracellular cyclic-di-GMP levels in Vibrio cholerae and Escherichia coli. Purified VCA0965 is able to synthesize cyclic-di-GMP in vitro
physiological function
-
enzyme synthesizes cyclic-di-GMP to regulate surface attachment via modulation of motility, without affecting subsequent biofilm formation. GcbA regulates flagellum-driven motility by suppressing flagellar reversal rates in a manner independent of viscosity, surface hardness, and polysaccharide production
physiological function
-
enzymic activity is dependent on the integrity of its GGDEF domain. Deletion of the dgcP gene shows that DgcP negatively regulates motility and positively controls biofilm formation, the deletion mutant mutant is hypovirulent in olive plants. Overexpression of the gene leads to an enhanced CR-binding phenotype that was accompanied by the formation of wrinkly colonies
physiological function
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isoform Chp8 is a functional diguanylate cyclase expressed in response to plant signals and codependent enhancer-binding proteins HrpRS. Chp8 decreases the expression of the major pathogen-associated molecular pattern flagellin and increases extracellular polysaccharides and impacts the salicylic acid/jasmonic acid hormonal immune response and disease progression
physiological function
ML1419c expression in Pseudomonas aeruginosa alters colony morphology, motility and biofilm formation in a manner consistent with increased cyclic di-GMP production. ML1419c expression increases cyclic di-GMP production in cultures in comparison to the vector control. The observed phenotypes and increased levels of cyclic di-GMP can be abrogated by mutation of the active site in ML1419c
physiological function
-
overexpression of either diguanylate cyclase genes, celR (atu1297) and atu1060 results in increased cellulose production, while deletion of celR, but not atu1060, results in decreased cellulose biosynthesis
physiological function
-
overexpression of either diguanylate cyclase genes, celR (atu1297) and atu1060 results in increased cellulose production, while deletion of celR, but not atu1060, results in decreased cellulose biosynthesis. celR overexpression also affects biofilm formation, formation of a polar adhesion structure, plant surface attachment, and virulence, suggesting that the gene plays a role in regulating these processes
physiological function
protein has in vivo and in vitro diguanylate cyclase activity that leads to the production of cyclic di-GMP. Protein XAC0610 plays a role in the regulation of Xanthomonas citri motility and resistance to H2O2. XAC0610 is not subject to allosteric product inhibition. Instead, steady-state kinetics reveal a positive cooperative effect of the GTP substrate with a dissociation constant for the binding of the first GTP molecule (K1) approximately 5 times greater than the dissociation constant for the binding of the second GTP molecule (K2). The N-terminal GAF and PAS domains are required for high levels of XAC0610 diguanylate cyclase activity
physiological function
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Pseudomonas fluorescens GcbA is functional in P.seudomonas aeruginosa and is capable of restoring phenotypes associated with inactivation of gcbA in P.seudomonas aeruginosa to wild-type levels. Motility and attachment of a gcbA mutant strain can be restored to wild-type levels via overexpression of the small regulatory RNA RsmZ. While both contribute to the regulation of initial surface attachment and flagellum-driven motility, GcbA and the phosphodiesterase DipA act within different signaling networks to regulate these processes
physiological function
the cdgA gene encoding diguanylate cyclase A is involved in biofilm formation and exopolysaccharide production in Azospirillum brasilense. Bacteria harboring a cdgA mutation exhibit biofilms with considerably reduced thickness compared with those of the wild-type strain. Extracellular DNA and exopolysaccharide are components of the biofilm matrix in Azospirillum
physiological function
Thermosynechococcus vestitus
the protein reversibly photoconverts between blue- and green-absorbing forms, and has diguanylate cyclase activity, which is enhanced 38fold by blue light compared with green light. The protein's relatively low affinity for Mg2+, which is essential for diguanylate cyclase activity, suggests thatMg2might also regulate cyclic-di-GMP signaling. Blue light irradiation under low temperature is responsible for Thermosynechococcus vulcanus cell aggregation, which is abolished when gene Tlr0924 is disrupted
physiological function
3',5'-cyclic diguanylate monophosphate (c-di-GMP) is a ubiquitous secondary messenger that plays a key role in response regulation and lifestyle conventions of pathogenic bacteria, including Vibrio cholerae. Increases in c-di-GMP levels induce increased expression of various factors necessary for the establishment and maintenance of biofilm communities, whereas decreased levels usually lead to enhanced expression of virulence and motility factors related to biofilm degradation. C-di-GMP is synthesized from guanosine triphosphate by diguanylate cyclase (DGC) enzymes
physiological function
cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa. SadC is reported to contribute to sensing of Psl and correspondingly increase of cellular c-di-GMP level. Involvement of Psl signalling in the SadC-mediated c-di-GMP synthesis
physiological function
diguanylate cyclase (DGC) synthesizes the ubiquitous bacterial second messenger c-di-GMP. GcsA has no PDE activity. GcsA modulates the cellular c-di-GMP level at early exponential phase. Crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. GcsA plays a role in early biofilm formation of Pseudomonas putida and regulates the swimming motility in an FlgZ-dependent manner
physiological function
-
diguanylate cyclases (DGCs) are responsible for the synthesis of second messenger cyclic di-guanosine monophosphate (c-di-GMP), which are involved in various physiological activities of bacterial species. DGC catalyzes the reaction of cyclic di-guanosine monophosphate (c-di-GMP) synthesis using guanosine triphosphate (GTP) as substrate. c-di-GMP is one of the potent regulator molecules, which is involved in many bacterial cellular functions, such as virulence, motility, bioluminescence, cellulose biosynthesis, adhesion, secretion, community behavior, biofilm formation, and cell differentiation
physiological function
-
diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme CdgD has a GGDEF domain along with a sensory PAS domain. It is a diguanylate cyclase
physiological function
diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme CdgD has a GGDEF domain along with a sensory PAS domain. It is a diguanylate cyclase. The enzyme does not have the conserved GGDEF motif, but has a degenerate AGDEF site. Significantly, expression of VCA0965 in Vibrio cholerae causes a 3fold reduction in flagellar-based motility. But enzyme VCA0965, despite its degenerate active site, synthesizes c-di-GMP
physiological function
-
diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme CdgH has a GGDEF domain along with a sensory PAS domain. It is a diguanylate cyclase. CdgH positively regulats the rugosity of the cel
physiological function
diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme VC0395_0300 is a diguanylate cyclase with a GGEEF domain, it synthesizes c-di-GMP actively and has an essential role to play in the biofilm formation of Vibrio cholerae
physiological function
enzyme Lcd1 is a potential node for the integration of cAMP and c-di-GMP signaling in Leptospira interrogans
physiological function
Escherichia coli diguanylate cyclase DgcZ interlinks surface sensing and adhesion via multiple regulatory routes. A FRD complex is required for the increase in DgcZ-mediated biofilm formation upon induction of oxidative stress by addition of paraquat. Possible integrative role of DgcZ in regulation of surface attachment. Both DgcZ-stimulated PGA biosynthesis and interaction of DgcZ with the FRD complex contribute to impeding bacterial escape from the surface. DgcZ is the main DGC involved in PGA production in Escherichia coli. Abundance and activity of DgcZ are regulated at several levels. Gene dgcZ transcription is activated by the transcriptional regulator CpxR. Beyond transcriptional and translational regulation of protein concentration, DgcZ activity is regulated by Zn2+. DgcZ localization and c-di-GMP concentrations change between transition and stationary phase
physiological function
GcsA inhibits swimming motility in an FlgZ-dependent manner. The GGDEF domain of GcsA contains all the conserved signature amino acid residues that form the enzyme's active site, as well as other residues required for the diguanylate cyclase activity of the GGDEF domain. GcsA modulates the cellular cyclic di-GMP level at early exponential phase
physiological function
globin-coupled oxygen sensor with diguanylate cyclase activity from Escherichia coli, regulates cyclic-di-GMP synthesis based on oxygen availability. Cyclic-di-guanosine-5'-monophosphate (c-di-GMP) is an important bacterial second messenger that regulates many key physiological functions including cell motility, differentiation, development, virulence, biofilm formation, cell-cell communication, and environmental persistence
physiological function
many bacteria contain large cyclic diguanylate (c-di-GMP) signaling networks made of diguanylate cyclases (DGCs) and phosphodiesterases that can direct cellular activities sensitive to c-di-GMP levels. While DGCs synthesize c-di-GMP, many DGCs also contain an autoinhibitory site (I-site) that binds c-di-GMP to halt excess production of this small molecule, thus controlling the amount of c-di-GMP available to bind to target proteins in the cell. Signaling between a DGC (GcbC) and its target protein (LapD) is a combined function of the I-site-dependent protein-protein interaction and the level of c-di-GMP production. The dual role of the I-site in modulating DGC activity as well as participating in protein-protein interactions suggests caution in interpreting the function of the I-site as only a means to negatively regulate a cyclase. These results implicate the I-site as an important positive and negative regulatory element of DGCs that may contribute to signaling specificity. Signaling specificity in Pseudomonas fluorescens is achieved by physical interaction is the regulation of biofilm formation by the inner membrane proteins GcbC and LapD. GcbC is a DGC that signals to the effector LapD. When bound to c-di-GMP, LapD changes conformation to sequester a periplasmic protease called LapG, thus allowing the large adhesin LapA to accumulate on the cell surface and thereby promoting biofilm formation
physiological function
PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) levels of biofilm but not planktonic cells. PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular c-di-GMP levels of biofilm but not planktonic cells. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation
physiological function
-
the diguanylate cyclase AdrA regulates flagellar biosynthesis in Pseudomonas fluorescens F113 through SadB. AdrA is a diguanylate cyclase implicated in c-di-GMP-mediated cellulose production and biofilm formation. AdrA is involved in swimming and biofilm formation, since inactivation of the adrA gene results in increased swimming motility and a reduction in the initial stages of attachment to surfaces. The enzyme is implicated in flagellar gene expression, genetic interaction between adrA and sadB indicates that AdrA participates in the regulation of flagella biogenesis
physiological function
-
the diguanylate cyclase GcpA inhibits the production of pectate lyases (Pel) via the H-NS protein and RsmB regulatory RNA in Dickeya dadantii. GcpA is the dominant DGC to negatively regulate Pel production by the specific repression of pelD gene expression. The DGC activity of GcpA is essential for its regulation of Pel production. Quantitative reverse transcription-polymerase chain reaction (qRT-PCR) assays reveal that the expression levels of histone-like, nucleoid-structuring protein encoding gene hns and posttranscriptional regulator encoding genes rsmA and rsmB are significantly affected by GcpA. H-NS and RsmB are responsible for the GcpA-dependent regulation of motility and type III secretion system (T3SS) gene expression, respectively. Gene gcpA might be essential for the viability of Dickeya dadantii, a functional A-site is required for GGDEF domain activity. GcpA negatively regulates the virulence, swimming motility, and T3SS gene expression of Dickeya dadantii
physiological function
the enzyme synthesizes the central signaling molecule, cyclic diguanylate (c-di-GMP), which is found to regulate various bacterial phenotypes, especially those involved in pathogen infection and drug resistance. Enzyme PA0847 is an active diguanylate cyclase (DGC). Roles of PA0847 in the regulation of bacterial motility and biofilm formation. Enzyme PA0847 is involved in response to a variety of environmental nutrients and factors, suggesting it might serve as a broad-range environmental sensor on the membrane of Pseudomonas aeruginosa. Gene of PA0847 affects biofilm formation and motility phenotypes in Pseudomonas aeruginosa
physiological function
the intracellular concentration of c-di-GMP determines both bacterial physiology and pathogenesis. HsbD is a diguanylate cyclase which activity intersects with the HptB regulatory pathway. The enzyme synthesizes c-di-GMP to locally implement the HptB regulatory pathway for the control of swarming, twitching, swimming motilities and biofilmformation. The HptB pathway controls biofilm formation and motility by involving both HsbD and the anti-anti-sigma factor HsbA. HsbD modulates type IV pili assembly and twitching motility and impacts swarming motility, overview. The rewiring of c-di-GMP signaling into the HptB cascade relies on the original interaction between HsbD and HsbA and on the control of HsbD dynamic localization at the cell poles
physiological function
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
physiological function
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
physiological function
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
physiological function
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
physiological function
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
physiological function
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
physiological function
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
physiological function
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
physiological function
the second messenger cyclic dimeric guanosine monophosphate (c-di-GMP) is ubiquitous in bacteria. It is synthesized from two molecules of GTP by diguanylate cyclases (DGCs), which possess the c-di-GMP synthesis GGDEF domain. In the unicellular cyanobacterium Synechocystis sp. PCC 6803 (Synechocystis) c-di-GMP influences the decision between motility and sessility. The photoreceptor Cph2 from the cyanobacterium Synechocystis sp. PCC 6803 comprises three domains related to c-di-GMP metabolism: two GGDEF and one EAL domain. It has been shown that the C-terminal GGDEF domain acts as blue-light triggered c-di-GMP producer thereby inhibiting motility of the cells in blue light. Binding of Cph2 and Slr1143 is likely mediated through interaction of Cph2 with the GGDEF domain of Slr1143, the interaction is not stoichiometric. Analysis of protein-protein interaction of Slr1143 with Cph2, overview
physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
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physiological function
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cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa. SadC is reported to contribute to sensing of Psl and correspondingly increase of cellular c-di-GMP level. Involvement of Psl signalling in the SadC-mediated c-di-GMP synthesis
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
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the intracellular concentration of c-di-GMP determines both bacterial physiology and pathogenesis. HsbD is a diguanylate cyclase which activity intersects with the HptB regulatory pathway. The enzyme synthesizes c-di-GMP to locally implement the HptB regulatory pathway for the control of swarming, twitching, swimming motilities and biofilmformation. The HptB pathway controls biofilm formation and motility by involving both HsbD and the anti-anti-sigma factor HsbA. HsbD modulates type IV pili assembly and twitching motility and impacts swarming motility, overview. The rewiring of c-di-GMP signaling into the HptB cascade relies on the original interaction between HsbD and HsbA and on the control of HsbD dynamic localization at the cell poles
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physiological function
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PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) levels of biofilm but not planktonic cells. PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular c-di-GMP levels of biofilm but not planktonic cells. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation
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physiological function
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the enzyme synthesizes the central signaling molecule, cyclic diguanylate (c-di-GMP), which is found to regulate various bacterial phenotypes, especially those involved in pathogen infection and drug resistance. Enzyme PA0847 is an active diguanylate cyclase (DGC). Roles of PA0847 in the regulation of bacterial motility and biofilm formation. Enzyme PA0847 is involved in response to a variety of environmental nutrients and factors, suggesting it might serve as a broad-range environmental sensor on the membrane of Pseudomonas aeruginosa. Gene of PA0847 affects biofilm formation and motility phenotypes in Pseudomonas aeruginosa
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physiological function
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ML1419c expression in Pseudomonas aeruginosa alters colony morphology, motility and biofilm formation in a manner consistent with increased cyclic di-GMP production. ML1419c expression increases cyclic di-GMP production in cultures in comparison to the vector control. The observed phenotypes and increased levels of cyclic di-GMP can be abrogated by mutation of the active site in ML1419c
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physiological function
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enzymic activity is dependent on the integrity of its GGDEF domain. Deletion of the dgcP gene shows that DgcP negatively regulates motility and positively controls biofilm formation, the deletion mutant mutant is hypovirulent in olive plants. Overexpression of the gene leads to an enhanced CR-binding phenotype that was accompanied by the formation of wrinkly colonies
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physiological function
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the diguanylate cyclase AdrA regulates flagellar biosynthesis in Pseudomonas fluorescens F113 through SadB. AdrA is a diguanylate cyclase implicated in c-di-GMP-mediated cellulose production and biofilm formation. AdrA is involved in swimming and biofilm formation, since inactivation of the adrA gene results in increased swimming motility and a reduction in the initial stages of attachment to surfaces. The enzyme is implicated in flagellar gene expression, genetic interaction between adrA and sadB indicates that AdrA participates in the regulation of flagella biogenesis
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
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DosD is a direct oxygen-sensing diguanylate cyclase playing a regulatory role in biofilm formation by Shewanella putrefaciens CN32 under aerobic conditions. The activity of DosD culminates to synthesis of cyclic diguanylate in the presence of oxygen. DosD regulates the transcription of the bpfA operon which encodes seven proteins including a large repetitive adhesin BpfA and its cognate type I secretion system (TISS). Regulation of DosD in aerobic biofilms is heavily dependent on an adhesin BpfA and the TISS
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
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physiological function
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cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa. SadC is reported to contribute to sensing of Psl and correspondingly increase of cellular c-di-GMP level. Involvement of Psl signalling in the SadC-mediated c-di-GMP synthesis
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
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PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) levels of biofilm but not planktonic cells. PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular c-di-GMP levels of biofilm but not planktonic cells. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation
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physiological function
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the enzyme synthesizes the central signaling molecule, cyclic diguanylate (c-di-GMP), which is found to regulate various bacterial phenotypes, especially those involved in pathogen infection and drug resistance. Enzyme PA0847 is an active diguanylate cyclase (DGC). Roles of PA0847 in the regulation of bacterial motility and biofilm formation. Enzyme PA0847 is involved in response to a variety of environmental nutrients and factors, suggesting it might serve as a broad-range environmental sensor on the membrane of Pseudomonas aeruginosa. Gene of PA0847 affects biofilm formation and motility phenotypes in Pseudomonas aeruginosa
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physiological function
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isoform Chp8 is a functional diguanylate cyclase expressed in response to plant signals and codependent enhancer-binding proteins HrpRS. Chp8 decreases the expression of the major pathogen-associated molecular pattern flagellin and increases extracellular polysaccharides and impacts the salicylic acid/jasmonic acid hormonal immune response and disease progression
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physiological function
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DgcA negatively affects virulence, extracellular polymeric substances production, bacterial autoaggregation and motility, but positively triggers biofilm formation via modulating the intracellular cyclic di-GMP levels. Deletion of dgcA substantially increases Xoo virulence against two different rice cultivars. 349 differentially expressed genes are controlled by DgcA
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
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physiological function
Vibrio cholerae serotype O1 C6706str2
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ectopic expression of VCA0965 in ibrio. cholerae causes a 3fold reduction in flagellar-based motility. An RXXD allosteric inhibition mutant of VCA0965 strongly inhibits motility and stimulates biofilm formation. This activity is lost when the active site of VCA0965 is mutated to AGDAF, suggesting that VCA0965 synthesizes cyclic-di-GMP. Ectopic expression of VCA0965 and VCA0965 containing a mutation in its RXXD motif significantly increases the intracellular cyclic-di-GMP levels in Vibrio cholerae and Escherichia coli. Purified VCA0965 is able to synthesize cyclic-di-GMP in vitro
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physiological function
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GcsA inhibits swimming motility in an FlgZ-dependent manner. The GGDEF domain of GcsA contains all the conserved signature amino acid residues that form the enzyme's active site, as well as other residues required for the diguanylate cyclase activity of the GGDEF domain. GcsA modulates the cellular cyclic di-GMP level at early exponential phase
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physiological function
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diguanylate cyclase (DGC) synthesizes the ubiquitous bacterial second messenger c-di-GMP. GcsA has no PDE activity. GcsA modulates the cellular c-di-GMP level at early exponential phase. Crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. GcsA plays a role in early biofilm formation of Pseudomonas putida and regulates the swimming motility in an FlgZ-dependent manner
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physiological function
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the cdgA gene encoding diguanylate cyclase A is involved in biofilm formation and exopolysaccharide production in Azospirillum brasilense. Bacteria harboring a cdgA mutation exhibit biofilms with considerably reduced thickness compared with those of the wild-type strain. Extracellular DNA and exopolysaccharide are components of the biofilm matrix in Azospirillum
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
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physiological function
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cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa. SadC is reported to contribute to sensing of Psl and correspondingly increase of cellular c-di-GMP level. Involvement of Psl signalling in the SadC-mediated c-di-GMP synthesis
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
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PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) levels of biofilm but not planktonic cells. PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular c-di-GMP levels of biofilm but not planktonic cells. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation
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physiological function
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the enzyme synthesizes the central signaling molecule, cyclic diguanylate (c-di-GMP), which is found to regulate various bacterial phenotypes, especially those involved in pathogen infection and drug resistance. Enzyme PA0847 is an active diguanylate cyclase (DGC). Roles of PA0847 in the regulation of bacterial motility and biofilm formation. Enzyme PA0847 is involved in response to a variety of environmental nutrients and factors, suggesting it might serve as a broad-range environmental sensor on the membrane of Pseudomonas aeruginosa. Gene of PA0847 affects biofilm formation and motility phenotypes in Pseudomonas aeruginosa
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physiological function
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diguanylate cyclases (DGCs) are responsible for the synthesis of second messenger cyclic di-guanosine monophosphate (c-di-GMP), which are involved in various physiological activities of bacterial species. DGC catalyzes the reaction of cyclic di-guanosine monophosphate (c-di-GMP) synthesis using guanosine triphosphate (GTP) as substrate. c-di-GMP is one of the potent regulator molecules, which is involved in many bacterial cellular functions, such as virulence, motility, bioluminescence, cellulose biosynthesis, adhesion, secretion, community behavior, biofilm formation, and cell differentiation
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physiological function
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a deletion mutation in the pgn_1932 gene has a significant effect on the intracellular cyclic-di-GMP level in Porphyromonas gingivalis. Expression of the fimA and rgpA genes, encoding the major protein subunit of fimbriae and an arginine-specific proteinase, respectively, is downregulated in the pgn_1932 mutant. Correspondingly, FimA protein production and the fimbrial display on the mutant are significantly reduced. Mutations in the pgn_1932 gene also have a significant impact on the adhesive and invasive capabilities of P.orphyromonas gingivalis, which are required for its pathogenicity
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
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physiological function
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cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa. SadC is reported to contribute to sensing of Psl and correspondingly increase of cellular c-di-GMP level. Involvement of Psl signalling in the SadC-mediated c-di-GMP synthesis
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
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PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) levels of biofilm but not planktonic cells. PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular c-di-GMP levels of biofilm but not planktonic cells. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation
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physiological function
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Dcsbis tightly coordinates cell motility without markedly affecting biofilm formation and is a diguanylate cyclase with a catalytic activity much higher than those of many other diguanylate cyclases
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physiological function
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the enzyme synthesizes the central signaling molecule, cyclic diguanylate (c-di-GMP), which is found to regulate various bacterial phenotypes, especially those involved in pathogen infection and drug resistance. Enzyme PA0847 is an active diguanylate cyclase (DGC). Roles of PA0847 in the regulation of bacterial motility and biofilm formation. Enzyme PA0847 is involved in response to a variety of environmental nutrients and factors, suggesting it might serve as a broad-range environmental sensor on the membrane of Pseudomonas aeruginosa. Gene of PA0847 affects biofilm formation and motility phenotypes in Pseudomonas aeruginosa
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
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physiological function
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cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa. SadC is reported to contribute to sensing of Psl and correspondingly increase of cellular c-di-GMP level. Involvement of Psl signalling in the SadC-mediated c-di-GMP synthesis
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
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PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) levels of biofilm but not planktonic cells. PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular c-di-GMP levels of biofilm but not planktonic cells. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation
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physiological function
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the enzyme synthesizes the central signaling molecule, cyclic diguanylate (c-di-GMP), which is found to regulate various bacterial phenotypes, especially those involved in pathogen infection and drug resistance. Enzyme PA0847 is an active diguanylate cyclase (DGC). Roles of PA0847 in the regulation of bacterial motility and biofilm formation. Enzyme PA0847 is involved in response to a variety of environmental nutrients and factors, suggesting it might serve as a broad-range environmental sensor on the membrane of Pseudomonas aeruginosa. Gene of PA0847 affects biofilm formation and motility phenotypes in Pseudomonas aeruginosa
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
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physiological function
-
cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa. SadC is reported to contribute to sensing of Psl and correspondingly increase of cellular c-di-GMP level. Involvement of Psl signalling in the SadC-mediated c-di-GMP synthesis
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
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PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) levels of biofilm but not planktonic cells. PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular c-di-GMP levels of biofilm but not planktonic cells. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation
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physiological function
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the enzyme synthesizes the central signaling molecule, cyclic diguanylate (c-di-GMP), which is found to regulate various bacterial phenotypes, especially those involved in pathogen infection and drug resistance. Enzyme PA0847 is an active diguanylate cyclase (DGC). Roles of PA0847 in the regulation of bacterial motility and biofilm formation. Enzyme PA0847 is involved in response to a variety of environmental nutrients and factors, suggesting it might serve as a broad-range environmental sensor on the membrane of Pseudomonas aeruginosa. Gene of PA0847 affects biofilm formation and motility phenotypes in Pseudomonas aeruginosa
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physiological function
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diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme CdgD has a GGDEF domain along with a sensory PAS domain. It is a diguanylate cyclase. The enzyme does not have the conserved GGDEF motif, but has a degenerate AGDEF site. Significantly, expression of VCA0965 in Vibrio cholerae causes a 3fold reduction in flagellar-based motility. But enzyme VCA0965, despite its degenerate active site, synthesizes c-di-GMP
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physiological function
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the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
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3',5'-cyclic diguanylate monophosphate (c-di-GMP) is a ubiquitous secondary messenger that plays a key role in response regulation and lifestyle conventions of pathogenic bacteria, including Vibrio cholerae. Increases in c-di-GMP levels induce increased expression of various factors necessary for the establishment and maintenance of biofilm communities, whereas decreased levels usually lead to enhanced expression of virulence and motility factors related to biofilm degradation. C-di-GMP is synthesized from guanosine triphosphate by diguanylate cyclase (DGC) enzymes
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physiological function
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DgcP negatively regulates motility and positively controls biofilm formation. Overexpression of the DgcP gene leads to increased exopolysaccharide production and upregulation of the type VI secretion system, in turn, it represses the type III secretion system, a hallmark of chronic infections and persistence for P.seudomonasaeruginosa. Deletion of the DgcP gene reduces the virulence in a mouse acute lung injury model
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physiological function
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many bacteria contain large cyclic diguanylate (c-di-GMP) signaling networks made of diguanylate cyclases (DGCs) and phosphodiesterases that can direct cellular activities sensitive to c-di-GMP levels. While DGCs synthesize c-di-GMP, many DGCs also contain an autoinhibitory site (I-site) that binds c-di-GMP to halt excess production of this small molecule, thus controlling the amount of c-di-GMP available to bind to target proteins in the cell. Signaling between a DGC (GcbC) and its target protein (LapD) is a combined function of the I-site-dependent protein-protein interaction and the level of c-di-GMP production. The dual role of the I-site in modulating DGC activity as well as participating in protein-protein interactions suggests caution in interpreting the function of the I-site as only a means to negatively regulate a cyclase. These results implicate the I-site as an important positive and negative regulatory element of DGCs that may contribute to signaling specificity. Signaling specificity in Pseudomonas fluorescens is achieved by physical interaction is the regulation of biofilm formation by the inner membrane proteins GcbC and LapD. GcbC is a DGC that signals to the effector LapD. When bound to c-di-GMP, LapD changes conformation to sequester a periplasmic protease called LapG, thus allowing the large adhesin LapA to accumulate on the cell surface and thereby promoting biofilm formation
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physiological function
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diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme VC0395_0300 is a diguanylate cyclase with a GGEEF domain, it synthesizes c-di-GMP actively and has an essential role to play in the biofilm formation of Vibrio cholerae
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physiological function
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diguanylate cyclase (DGC) synthesizes the ubiquitous bacterial second messenger c-di-GMP. GcsA has no PDE activity. GcsA modulates the cellular c-di-GMP level at early exponential phase. Crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. GcsA plays a role in early biofilm formation of Pseudomonas putida and regulates the swimming motility in an FlgZ-dependent manner
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physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain. The enzyme is important for the organism's biofilm formation ability, which plays a pivotal role in the virulence
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physiological function
-
cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa. SadC is reported to contribute to sensing of Psl and correspondingly increase of cellular c-di-GMP level. Involvement of Psl signalling in the SadC-mediated c-di-GMP synthesis
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physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
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physiological function
-
PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) levels of biofilm but not planktonic cells. PA3177 is confirmed to be an active diguanylate cyclase, with overexpression affecting swimming and swarming motility, and inactivation affecting cellular c-di-GMP levels of biofilm but not planktonic cells. While PA3177 contributes to biofilm drug tolerance, inactivation of PA3177 has no effect on attachment and biofilm formation
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physiological function
-
the enzyme synthesizes the central signaling molecule, cyclic diguanylate (c-di-GMP), which is found to regulate various bacterial phenotypes, especially those involved in pathogen infection and drug resistance. Enzyme PA0847 is an active diguanylate cyclase (DGC). Roles of PA0847 in the regulation of bacterial motility and biofilm formation. Enzyme PA0847 is involved in response to a variety of environmental nutrients and factors, suggesting it might serve as a broad-range environmental sensor on the membrane of Pseudomonas aeruginosa. Gene of PA0847 affects biofilm formation and motility phenotypes in Pseudomonas aeruginosa
-
physiological function
-
diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme VC0395_0300 is a diguanylate cyclase with a GGEEF domain, it synthesizes c-di-GMP actively and has an essential role to play in the biofilm formation of Vibrio cholerae
-
physiological function
-
diguanylate cyclase (DGC) synthesizes the ubiquitous bacterial second messenger c-di-GMP. GcsA has no PDE activity. GcsA modulates the cellular c-di-GMP level at early exponential phase. Crosstalk between c-di-GMP and cAMP in the regulation of the expression of GcsA in Pseudomonas putida. GcsA plays a role in early biofilm formation of Pseudomonas putida and regulates the swimming motility in an FlgZ-dependent manner
-
physiological function
-
diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme VC0395_0300 is a diguanylate cyclase with a GGEEF domain, it synthesizes c-di-GMP actively and has an essential role to play in the biofilm formation of Vibrio cholerae
-
physiological function
-
diguanylate cyclases in Vibrio cholerae are essential regulators of lifestyle switching, importance of DGCs and their product, cyclic-di-GMP, in the virulence and lifecycle of the bacteria. Biofilm formation in Vibrio cholerae empowers the bacteria to lead a dual lifestyle and enhances its infectivity. While the formation and dispersal of the biofilm involves multiple components, both proteinaceous and non-proteinaceous, the key to the regulatory control lies with the ubiquitous secondary signaling molecule, cyclic-di-GMP (c-di-GMP). Enzyme CdgD has a GGDEF domain along with a sensory PAS domain. It is a diguanylate cyclase. The enzyme does not have the conserved GGDEF motif, but has a degenerate AGDEF site. Significantly, expression of VCA0965 in Vibrio cholerae causes a 3fold reduction in flagellar-based motility. But enzyme VCA0965, despite its degenerate active site, synthesizes c-di-GMP
-
physiological function
-
the primary signaling molecule promoting bacterial biofilm formation is the universal second messenger cyclic di-GMP. This dinucleotide predominantly controls the gene expression of motility, adhesins, and capsule production to coordinate biofilm formation. Cyclic di-GMP is synthesized by diguanylate cyclases (DGCs) that have a GGDEF domain and is degraded by phosphodiesterases (PDEs) containing either an EAL or an HD-GYP domain
-
physiological function
-
3',5'-cyclic diguanylate monophosphate (c-di-GMP) is a ubiquitous secondary messenger that plays a key role in response regulation and lifestyle conventions of pathogenic bacteria, including Vibrio cholerae. Increases in c-di-GMP levels induce increased expression of various factors necessary for the establishment and maintenance of biofilm communities, whereas decreased levels usually lead to enhanced expression of virulence and motility factors related to biofilm degradation. C-di-GMP is synthesized from guanosine triphosphate by diguanylate cyclase (DGC) enzymes
-
physiological function
-
the diguanylate cyclase GcpA inhibits the production of pectate lyases (Pel) via the H-NS protein and RsmB regulatory RNA in Dickeya dadantii. GcpA is the dominant DGC to negatively regulate Pel production by the specific repression of pelD gene expression. The DGC activity of GcpA is essential for its regulation of Pel production. Quantitative reverse transcription-polymerase chain reaction (qRT-PCR) assays reveal that the expression levels of histone-like, nucleoid-structuring protein encoding gene hns and posttranscriptional regulator encoding genes rsmA and rsmB are significantly affected by GcpA. H-NS and RsmB are responsible for the GcpA-dependent regulation of motility and type III secretion system (T3SS) gene expression, respectively. Gene gcpA might be essential for the viability of Dickeya dadantii, a functional A-site is required for GGDEF domain activity. GcpA negatively regulates the virulence, swimming motility, and T3SS gene expression of Dickeya dadantii
-
additional information
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
additional information
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
additional information
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
additional information
-
DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
additional information
-
DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
additional information
-
DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
additional information
-
DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
additional information
-
DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
additional information
DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
additional information
DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
additional information
enzyme Lcd1 has an N-terminal cGMP-specific phosphodiesterase domain, an adenylyl cyclase domain, a FhlA (GAF) domain, and a C-terminal GGDEF domain. The GAF domain regulates the DGC activity of Lcd1. The GAF domain binds specifically cAMP and has animportant role in the regulation of the DGC activity of the GGDEF domain. Lcd1 DGC activity is negligible in the absence of cAMP and is significantly enhanced in its presence. Structure comparison, overview
additional information
in blue light, wild-type cells are sessile while DELTAcph2 cells move towards the light source. The product of the gene cph2 is a photosensory protein, Cph2, which consists of six domains with the architecture GAF-GAF-GGDEF-EAL-CBCR-GGDEF (GAF, cGMP phosphodiesterase/adenylyl cylase/FhlA, CBCR, cyanobacteriochrome, GGDEF, degenerate motif). The domains 1 (GAF) and 5 (CBCR) covalently bind phycocyanobilin (PCB) as a chromophore, allowing the absorbance of light in the visible spectrum
additional information
-
structure model of GST-DGC by the threading method, overview
additional information
the autoinhibitory I-site of a diguanylate cyclase is a necessary element for interaction and signaling with an effector protein
additional information
-
the autoinhibitory I-site of a diguanylate cyclase is a necessary element for interaction and signaling with an effector protein
additional information
the diguanylate cyclase activity of PA0847 depends on the neighboring PAS domain. A local structural change imposed by an adjacent tyrosine residue is identified, which indicates the structural and functional diversities of the GGDEF family proteins. Signaling mechanism of the unique c-di-GMP metabolizing protein PA0847, overview. Three-dimensional homology model of PA0847 GGDEF domain (residues 576-736) using DGC DgcZ (PDB ID 4H54) as a structure template. Seven critical residues, D609, K614, N617, D626, D652, E653, and K722, are involved in GTP binding
additional information
the enzyme's diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ala68, and Met69 are required to maintain full diguanylate cyclase activity. The highly conserved amino acids His223 and Lys224 in the middle domain of EcGReg are essential to diguanylate cyclase activity. Sixteen important residues (Leu300, Arg306, Asp333, Phe337, Lys338, Asn341, Asp342, Asp350, Leu353, Asp368, Arg372, Gly374, Gly375, Asp376, Glu377, and Phe378) are identified in the active site and inhibitory site of the diguanylate cyclase domain of EcGReg
additional information
-
the enzyme's diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ala68, and Met69 are required to maintain full diguanylate cyclase activity. The highly conserved amino acids His223 and Lys224 in the middle domain of EcGReg are essential to diguanylate cyclase activity. Sixteen important residues (Leu300, Arg306, Asp333, Phe337, Lys338, Asn341, Asp342, Asp350, Leu353, Asp368, Arg372, Gly374, Gly375, Asp376, Glu377, and Phe378) are identified in the active site and inhibitory site of the diguanylate cyclase domain of EcGReg
additional information
the enzyme's diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ser68, and Met69 are required to maintain full diguanylatecyclase activity. The highly conserved amino acids His225 and Lys226 in the middle domain of BpeGReg are essential to diguanylate cyclase activity. Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
additional information
-
the enzyme's diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ser68, and Met69 are required to maintain full diguanylatecyclase activity. The highly conserved amino acids His225 and Lys226 in the middle domain of BpeGReg are essential to diguanylate cyclase activity. Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
additional information
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
additional information
the periplasmic portion of CdgH forms a homodimer in solution which undergoes conformational changes upon L-arginine binding. Homodimerization leads to alignment of the two GGDEF domains, resulting in 2fold symmetry that enables the enzyme to catalyze c-diGMP synthesis. Both tandem PBPb domains of CdgH contain a typical interlobe ligand-binding structural architecture. PBPb-I and -II domains have different amino acid binding specificity. The PBPb-I domain is primarily an L-arginine/L-lysine/L-ornithine-binding domain, whereas the PBPb-II domain exhibits a preference for L-glutamine and L-histidine, binding site structures, overview. Comparison of the CdgH PBPb-I domain with other amino acid-binding proteins
additional information
-
the structure of CdgH is solved and displays the presence of two N-terminal tandem periplasmic substrate-binding (PBPb) domains for signal recognition
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the diguanylate cyclase activity of PA0847 depends on the neighboring PAS domain. A local structural change imposed by an adjacent tyrosine residue is identified, which indicates the structural and functional diversities of the GGDEF family proteins. Signaling mechanism of the unique c-di-GMP metabolizing protein PA0847, overview. Three-dimensional homology model of PA0847 GGDEF domain (residues 576-736) using DGC DgcZ (PDB ID 4H54) as a structure template. Seven critical residues, D609, K614, N617, D626, D652, E653, and K722, are involved in GTP binding
-
additional information
-
the enzyme's diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ser68, and Met69 are required to maintain full diguanylatecyclase activity. The highly conserved amino acids His225 and Lys226 in the middle domain of BpeGReg are essential to diguanylate cyclase activity. Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the diguanylate cyclase activity of PA0847 depends on the neighboring PAS domain. A local structural change imposed by an adjacent tyrosine residue is identified, which indicates the structural and functional diversities of the GGDEF family proteins. Signaling mechanism of the unique c-di-GMP metabolizing protein PA0847, overview. Three-dimensional homology model of PA0847 GGDEF domain (residues 576-736) using DGC DgcZ (PDB ID 4H54) as a structure template. Seven critical residues, D609, K614, N617, D626, D652, E653, and K722, are involved in GTP binding
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the diguanylate cyclase activity of PA0847 depends on the neighboring PAS domain. A local structural change imposed by an adjacent tyrosine residue is identified, which indicates the structural and functional diversities of the GGDEF family proteins. Signaling mechanism of the unique c-di-GMP metabolizing protein PA0847, overview. Three-dimensional homology model of PA0847 GGDEF domain (residues 576-736) using DGC DgcZ (PDB ID 4H54) as a structure template. Seven critical residues, D609, K614, N617, D626, D652, E653, and K722, are involved in GTP binding
-
additional information
-
structure model of GST-DGC by the threading method, overview
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the diguanylate cyclase activity of PA0847 depends on the neighboring PAS domain. A local structural change imposed by an adjacent tyrosine residue is identified, which indicates the structural and functional diversities of the GGDEF family proteins. Signaling mechanism of the unique c-di-GMP metabolizing protein PA0847, overview. Three-dimensional homology model of PA0847 GGDEF domain (residues 576-736) using DGC DgcZ (PDB ID 4H54) as a structure template. Seven critical residues, D609, K614, N617, D626, D652, E653, and K722, are involved in GTP binding
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the diguanylate cyclase activity of PA0847 depends on the neighboring PAS domain. A local structural change imposed by an adjacent tyrosine residue is identified, which indicates the structural and functional diversities of the GGDEF family proteins. Signaling mechanism of the unique c-di-GMP metabolizing protein PA0847, overview. Three-dimensional homology model of PA0847 GGDEF domain (residues 576-736) using DGC DgcZ (PDB ID 4H54) as a structure template. Seven critical residues, D609, K614, N617, D626, D652, E653, and K722, are involved in GTP binding
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the diguanylate cyclase activity of PA0847 depends on the neighboring PAS domain. A local structural change imposed by an adjacent tyrosine residue is identified, which indicates the structural and functional diversities of the GGDEF family proteins. Signaling mechanism of the unique c-di-GMP metabolizing protein PA0847, overview. Three-dimensional homology model of PA0847 GGDEF domain (residues 576-736) using DGC DgcZ (PDB ID 4H54) as a structure template. Seven critical residues, D609, K614, N617, D626, D652, E653, and K722, are involved in GTP binding
-
additional information
-
the periplasmic portion of CdgH forms a homodimer in solution which undergoes conformational changes upon L-arginine binding. Homodimerization leads to alignment of the two GGDEF domains, resulting in 2fold symmetry that enables the enzyme to catalyze c-diGMP synthesis. Both tandem PBPb domains of CdgH contain a typical interlobe ligand-binding structural architecture. PBPb-I and -II domains have different amino acid binding specificity. The PBPb-I domain is primarily an L-arginine/L-lysine/L-ornithine-binding domain, whereas the PBPb-II domain exhibits a preference for L-glutamine and L-histidine, binding site structures, overview. Comparison of the CdgH PBPb-I domain with other amino acid-binding proteins
-
additional information
-
the enzyme's diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ser68, and Met69 are required to maintain full diguanylatecyclase activity. The highly conserved amino acids His225 and Lys226 in the middle domain of BpeGReg are essential to diguanylate cyclase activity. Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
-
additional information
-
the enzyme's diguanylate cyclase activity requires an intact globin domain. In the distal heme pocket of the globin domain, residues Phe42, Tyr43, Ser68, and Met69 are required to maintain full diguanylatecyclase activity. The highly conserved amino acids His225 and Lys226 in the middle domain of BpeGReg are essential to diguanylate cyclase activity. Bpe-GReg may interact with other c-di-GMP-metabolizing proteins to form mixed signaling teams
-
additional information
-
the autoinhibitory I-site of a diguanylate cyclase is a necessary element for interaction and signaling with an effector protein
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The GGDEF domain of SadC has a typical GGDEF structure
-
additional information
-
binding mode of the substrate analogue GTP-alpha-S (guanosine-alpha-thio-triphosphate) bound to PleD
-
additional information
-
the diguanylate cyclase activity of PA0847 depends on the neighboring PAS domain. A local structural change imposed by an adjacent tyrosine residue is identified, which indicates the structural and functional diversities of the GGDEF family proteins. Signaling mechanism of the unique c-di-GMP metabolizing protein PA0847, overview. Three-dimensional homology model of PA0847 GGDEF domain (residues 576-736) using DGC DgcZ (PDB ID 4H54) as a structure template. Seven critical residues, D609, K614, N617, D626, D652, E653, and K722, are involved in GTP binding
-
additional information
Vibrio cholerae serotype O1 A1552
-
DGCs operate as dimers, using their GGDEF domains to produce c-di-GMP. In addition to GGDEF, active cyclases have also been found that make use of GGEEF, AGDEF, and GGDEM motifs
-
additional information
-
the periplasmic portion of CdgH forms a homodimer in solution which undergoes conformational changes upon L-arginine binding. Homodimerization leads to alignment of the two GGDEF domains, resulting in 2fold symmetry that enables the enzyme to catalyze c-diGMP synthesis. Both tandem PBPb domains of CdgH contain a typical interlobe ligand-binding structural architecture. PBPb-I and -II domains have different amino acid binding specificity. The PBPb-I domain is primarily an L-arginine/L-lysine/L-ornithine-binding domain, whereas the PBPb-II domain exhibits a preference for L-glutamine and L-histidine, binding site structures, overview. Comparison of the CdgH PBPb-I domain with other amino acid-binding proteins
-
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multimer
x * 94500, calculated
?
x * 62000, calculated
?
-
x * 62000, calculated
-
?
-
x * 78000, calculated
?
-
x * 76000, calculated
-
?
-
x * 76000, calculated
?
-
x * 76000, calculated
-
dimer
at high protein concentrations and/or presence of divalent metal ions (Mg2+, Mn2+), tightened upon BeF3-modification, exothermic dimerisation, KD: 100 microM, gel filtration chromatography and crystallography
dimer
enzymatically active state, concentration dependent, crosslinking (using disuccinimidyl suberate, DSS)
dimer
MBP-tagged YddV is primarily dimeric in solution
dimer
2 * 37600, apoform Lcd1GAF domain, SDS-PAGE, 2 * 37700, Lcd1GAF domain in complex with cAMP, SDS-PAGE
dimer
-
compact structure, globular shape, active state, phosphodiesterase-treated (hydrolysis of bound cyclic di-3,5-guanylate) and nucleotide-free wild-type, nucleotide-free mutants GGAAF, R242A and R198A and cyclic di-3,5-guanylate-bound mutant L170D, coupled gel-filtration/multiangle light scattering
dimer
-
elongated shape, product-inhibited state, purified wild-type (cyclic di-3,5-guanylate-bound), coupled gel-filtration/multiangle light scattering
dimer
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain. Structural model of PA0847 GGDEF dimer, overview
dimer
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain. Structural model of PA0847 GGDEF dimer, overview
-
dimer
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain. Structural model of PA0847 GGDEF dimer, overview
-
dimer
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain. Structural model of PA0847 GGDEF dimer, overview
-
dimer
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain. Structural model of PA0847 GGDEF dimer, overview
-
dimer
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain. Structural model of PA0847 GGDEF dimer, overview
-
dimer
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain. Structural model of PA0847 GGDEF dimer, overview
-
dimer
-
domain analysis of PA0847 shows a unique molecular architecture with an N-terminal periplasmic sensory domain and a C-terminal intracellular GGDEF domain. Structural model of PA0847 GGDEF dimer, overview
-
dimer
-
compact structure, globular shape, active state, phosphodiesterase-treated (hydrolysis of bound cyclic di-3,5-guanylate) and nucleotide-free wild-type, coupled gel-filtration/multiangle light scattering
dimer
-
elongated shape, product-inhibited state, purified wild-type (cyclic di-3,5-guanylate-bound), coupled gel-filtration/multiangle light scattering
dimer
-
compact structure, globular shape, active state, phosphodiesterase-treated (hydrolysis of bound cyclic di-3,5-guanylate) and nucleotide-free wild-type, coupled gel-filtration/multiangle light scattering
-
dimer
-
elongated shape, product-inhibited state, purified wild-type (cyclic di-3,5-guanylate-bound), coupled gel-filtration/multiangle light scattering
-
dimer
-
compact structure, globular shape, active state, phosphodiesterase-treated (hydrolysis of bound cyclic di-3,5-guanylate) and nucleotide-free wild-type, coupled gel-filtration/multiangle light scattering
dimer
-
elongated shape, product-inhibited state, purified wild-type (cyclic di-3,5-guanylate-bound), coupled gel-filtration/multiangle light scattering
dimer
-
compact structure, globular shape, active state, phosphodiesterase-treated (hydrolysis of bound cyclic di-3,5-guanylate) and nucleotide-free wild-type, coupled gel-filtration/multiangle light scattering
-
dimer
-
elongated shape, product-inhibited state, purified wild-type (cyclic di-3,5-guanylate-bound), coupled gel-filtration/multiangle light scattering
-
dimer
-
compact structure, globular shape, active state, phosphodiesterase-treated (hydrolysis of bound cyclic di-3,5-guanylate) and nucleotide-free wild-type, coupled gel-filtration/multiangle light scattering
dimer
-
elongated shape, product-inhibited state, purified wild-type (cyclic di-3,5-guanylate-bound), coupled gel-filtration/multiangle light scattering
dimer
-
compact structure, globular shape, active state, phosphodiesterase-treated (hydrolysis of bound cyclic di-3,5-guanylate) and nucleotide-free wild-type, coupled gel-filtration/multiangle light scattering
-
dimer
-
elongated shape, product-inhibited state, purified wild-type (cyclic di-3,5-guanylate-bound), coupled gel-filtration/multiangle light scattering
-
homotetramer
4 * 42000
octamer
-
8 * 71900, recombinant GST-tagged enzyme, SDS- and native PAGE, and LC-MS/MS, 8 * 73000, about, sequence calculation
octamer
-
8 * 71900, recombinant GST-tagged enzyme, SDS- and native PAGE, and LC-MS/MS, 8 * 73000, about, sequence calculation
-
tetramer
-
transient intermediate state between active, compact dimer and product-inhibited, elongated dimer, induced by high enzyme concentration, nucleotide-depleted wild-type sample, nucleotide-free mutants GGAAF, R242A and R198A and cyclic di-3,5-guanylate-bound mutant L170D, crystallography, coupled gel-filtration/multiangle light scattering
tetramer
-
transient intermediate state between active, compact dimer and product-inhibited, elongated dimer, induced by high enzyme concentration, nucleotide-depleted wild-type, coupled gel-filtration/multiangle light scattering
tetramer
-
transient intermediate state between active, compact dimer and product-inhibited, elongated dimer, induced by high enzyme concentration, nucleotide-depleted wild-type, coupled gel-filtration/multiangle light scattering
-
tetramer
-
transient intermediate state between active, compact dimer and product-inhibited, elongated dimer, induced by high enzyme concentration, nucleotide-depleted wild-type, coupled gel-filtration/multiangle light scattering
tetramer
-
transient intermediate state between active, compact dimer and product-inhibited, elongated dimer, induced by high enzyme concentration, nucleotide-depleted wild-type, coupled gel-filtration/multiangle light scattering
-
tetramer
-
transient intermediate state between active, compact dimer and product-inhibited, elongated dimer, induced by high enzyme concentration, nucleotide-depleted wild-type, coupled gel-filtration/multiangle light scattering
tetramer
-
transient intermediate state between active, compact dimer and product-inhibited, elongated dimer, induced by high enzyme concentration, nucleotide-depleted wild-type, coupled gel-filtration/multiangle light scattering
-
additional information
-
the GGDEF domain is sufficient to encode catalytic activity, which is highly regulated by the adjacent sensory protein domain
additional information
-
dimer is the catalytically active state of enzyme
additional information
dimer is the catalytically active state of enzyme
additional information
-
the GGDEF domain is sufficient to encode catalytic activity, which is highly regulated by the adjacent sensory protein domain
additional information
-
the GGDEF domain is sufficient to encode catalytic activity, which is highly regulated by the adjacent sensory protein domain
-
additional information
-
the GGDEF domain is responsible for the diguanylate cyclase activity
additional information
the inactive heme-free H93A mutant is primarily octameric, suggesting that catalytically active dimer formation requires heme binding. The dimer to tetramer ratios for MBP-tagged YddV in the presence and absence of GTP (and therefore of c-di-GMP) are 3.7:1 and 4.3:1, respectively. Like the Fe(III) form, the Fe(II)-O2, Fe(III)-CN- and Fe(III)-imidazole forms of YddV-MBP exist primarily as dimers, with tetramers being minor components
additional information
-
the inactive heme-free H93A mutant is primarily octameric, suggesting that catalytically active dimer formation requires heme binding. The dimer to tetramer ratios for MBP-tagged YddV in the presence and absence of GTP (and therefore of c-di-GMP) are 3.7:1 and 4.3:1, respectively. Like the Fe(III) form, the Fe(II)-O2, Fe(III)-CN- and Fe(III)-imidazole forms of YddV-MBP exist primarily as dimers, with tetramers being minor components
additional information
-
the GGDEF domain is responsible for the diguanylate cyclase activity
additional information
enzyme Lcd1 has an N-terminal cGMP-specific phosphodiesterase domain, an adenylyl cyclase domain, a FhlA (GAF) domain, and a C-terminal GGDEF domain. The N-terminal GAF domain comprises residues 28-165 and the C-terminal GGDEF domain residues 178-326, with a predicted linker (residues 166-177) between them. The full-length Lcd1 and its GAF domain form dimers in solution. The dimer interface involves 48 residues, mainly from alpha1 and alpha6. The dimerization interface involves many hydrogen bonds. On their own, these intermolecular H-bonds can be replaced with protein-solvent hydrogen bonds with little energetic penalty if it is not for additional intersubunit interactions involving hydrophobic and aromatic residues I11, Y14, L25, V152, F160, I162, H167, and Y171. In the full-length protein, the C-terminus of the GAF domain is linked to the N-terminus of the GGDEF domain. In the Lcd1GAF-cAMP dimer, the two C-terminal alpha6 helices are pointing in the same direction, and the Calpha atoms of the C-terminal T174 residues are separated by only 6.4 A
additional information
protein PGN_1932 contains a GGDEF domain
additional information
-
protein PGN_1932 contains a GGDEF domain
additional information
-
protein PGN_1932 contains a GGDEF domain
-
additional information
-
compact and elongated dimeric conformation correspond to catalytically active and inactive state, respectively
additional information
-
higher-order oligomerisation depends on interactions of stalk motifs
additional information
full-length Dcsbis protein contains an N-terminal GAF domain and a C-terminal GGDEF domain
additional information
-
full-length Dcsbis protein contains an N-terminal GAF domain and a C-terminal GGDEF domain
additional information
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
-
additional information
-
full-length Dcsbis protein contains an N-terminal GAF domain and a C-terminal GGDEF domain
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
-
additional information
-
the GGDEF domain of SadC has a typical GGDEF structure and the alpha-helix connecting the transmembrane domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers. The alpha-helix of amino acid residues 300-322 is necessary for SadC300-487 to form active hexamers, hexameric and monomeric structures. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. Enzyme mutants structure-function analysis, overview
-
additional information
-
compact and elongated dimeric conformation correspond to catalytically active and inactive state, respectively
additional information
-
compact and elongated dimeric conformation correspond to catalytically active and inactive state, respectively
-
additional information
-
compact and elongated dimeric conformation correspond to catalytically active and inactive state, respectively
additional information
-
enzyme GcsA consists of two per-ARNT-sim (PAS) domains, followed by a canonical conserved central sequence pattern (GGDEF) domain and a truncated EAL domain
additional information
enzyme GcsA consists of two per-ARNT-sim (PAS) domains, followed by a canonical conserved central sequence pattern (GGDEF) domain and a truncated EAL domain
additional information
-
enzyme GcsA consists of two per-ARNT-sim (PAS) domains, followed by a canonical conserved central sequence pattern (GGDEF) domain and a truncated EAL domain
-
additional information
-
enzyme GcsA consists of two per-ARNT-sim (PAS) domains, followed by a canonical conserved central sequence pattern (GGDEF) domain and a truncated EAL domain
-
additional information
-
compact and elongated dimeric conformation correspond to catalytically active and inactive state, respectively
-
additional information
-
enzyme GcsA consists of two per-ARNT-sim (PAS) domains, followed by a canonical conserved central sequence pattern (GGDEF) domain and a truncated EAL domain
-
additional information
-
compact and elongated dimeric conformation correspond to catalytically active and inactive state, respectively
additional information
-
compact and elongated dimeric conformation correspond to catalytically active and inactive state, respectively
-
additional information
-
proteon contains a GGDEF domain
additional information
-
proteon contains a GGDEF domain
-
additional information
-
the GGDEF domain is responsible for the diguanylate cyclase activity
additional information
Thermosynechococcus vestitus
protein contains a GGDEFdomain
additional information
the periplasmic portion of CdgH forms a type I homodimer in solution which undergoes conformational changes upon L-arginine binding. The dimerization mode requires both tandem PBPb domains. Homodimerization leads to alignment of the two GGDEF domains, resulting in 2fold symmetry that enables the enzyme to catalyze c-diGMP synthesis
additional information
-
the periplasmic portion of CdgH forms a type I homodimer in solution which undergoes conformational changes upon L-arginine binding. The dimerization mode requires both tandem PBPb domains. Homodimerization leads to alignment of the two GGDEF domains, resulting in 2fold symmetry that enables the enzyme to catalyze c-diGMP synthesis
-
additional information
-
the periplasmic portion of CdgH forms a type I homodimer in solution which undergoes conformational changes upon L-arginine binding. The dimerization mode requires both tandem PBPb domains. Homodimerization leads to alignment of the two GGDEF domains, resulting in 2fold symmetry that enables the enzyme to catalyze c-diGMP synthesis
-
additional information
-
the HD-GYP phosphodiesterase domain of RpfG, which is part of a system necessary for the diffusible signalling factor dependent production of extracellular pathogenicity, interacts directly with diguanylate cyclase GGDEF domain-containing proteins. Physical linkage between quorum-sensing and cyclic diguanylate signalling pathways
additional information
at micromolar concentrations, the protein exists predominantly as a dimeric species
additional information
-
at micromolar concentrations, the protein exists predominantly as a dimeric species
additional information
DgcA contains an intact GGDEF domain that functions as an active diguanylate cyclase
additional information
-
DgcA contains an intact GGDEF domain that functions as an active diguanylate cyclase
additional information
-
DgcA contains an intact GGDEF domain that functions as an active diguanylate cyclase
-
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F42A
site-directed mutagenesis
K226A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
M69A
site-directed mutagenesis
S68A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
Y43A
site-directed mutagenesis, biofilm formation of the mutant is partially inhibited, and cell motility is inhibited
F42A
-
site-directed mutagenesis
-
K226A
-
site-directed mutagenesis, biofilm formation of the mutant is inhibited
-
S68A
-
site-directed mutagenesis, biofilm formation of the mutant is inhibited
-
Y43A
-
site-directed mutagenesis, biofilm formation of the mutant is partially inhibited, and cell motility is inhibited
-
F42A
-
site-directed mutagenesis
-
K226A
-
site-directed mutagenesis, biofilm formation of the mutant is inhibited
-
S68A
-
site-directed mutagenesis, biofilm formation of the mutant is inhibited
-
Y43A
-
site-directed mutagenesis, biofilm formation of the mutant is partially inhibited, and cell motility is inhibited
-
F42A
-
site-directed mutagenesis
-
K226A
-
site-directed mutagenesis, biofilm formation of the mutant is inhibited
-
S68A
-
site-directed mutagenesis, biofilm formation of the mutant is inhibited
-
Y43A
-
site-directed mutagenesis, biofilm formation of the mutant is partially inhibited, and cell motility is inhibited
-
D327A
inactive due to loss of coordination of Mg2+
DELTAR359/DELTAD362
mutations in allosteric binding site of cyclic diguanylate, abolish cyclic diguanylate binding, strong decrease in catalytic activity
EE370GG
mutation in active site, complete loss of catalytic activity without effect on allosteric binding of cyclic diguanylate
R148A
increase in allosteric binding of cyclic diguanylate and increase in catalytic activity
R148A/R178A/R313A
triple mutant, KD for binding of cyclic di-3,5-guanylate: 4 microM (10fold higher than wild-type), 60fold increased KI for product inhibition by cyclic di-3,5-guanylate, residual catalytic activity
R178A
increase in allosteric binding of cyclic diguanylate and increase in catalytic activity
R313A
part of inhibitory site
R359A
mutation in allosteric binding site of cyclic diguanylate, strong decrease in cyclic diguanylate binding, strong decrease in catalytic activity
R359V
strong decrease in catalytic activity
R390A
mutation in allosteric binding site of cyclic diguanylate, strong decrease in cyclic diguanylate binding. Catalytic activity comaprable to wild-type
A68T
site-directed mutagenesis, the mutant cell motility and biofilm formation are partially inhibited
D333A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
D342A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
D350A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
D368A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
D368K
site-directed mutagenesis, biofilm formation of the mutant is inhibited
D376A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
E377A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
F337A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
F378A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
F42A
site-directed mutagenesis
G374A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
G375A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
H223A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
H79L/H83L
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme, cellular localization is unaltered
H79L/H83L/E208Q
site-directed mutagenesis, inactive mutant, cellular localization is unaltered
H93A
site-directed mutagenesis, the mutant has no heme and is inactive
H98A
site-directed mutagenesis
K224A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
K338A
site-directed mutagenesis, the mutant cell motility and biofilm formation are partially inhibited
L300A
site-directed mutagenesis, the mutant biofilm formation is partially inhibited
L300D
site-directed mutagenesis, the mutant cell motility is inhibited, biofilm formation of the mutant is inhibited
L353A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
L353D
site-directed mutagenesis, the mutant cell motility is inhibited, and biofilm formation of the mutant is inhibited
L65G
site-directed mutagenesis, heme distal amino acid replacement leading to reduced activity compared to wild-type
L65M
site-directed mutagenesis, heme distal amino acid replacement
L65Q
site-directed mutagenesis, heme distal amino acid replacement leading to reduced activity compared to wild-type
L65T
site-directed mutagenesis, heme distal amino acid replacement
M69A
site-directed mutagenesis
N341A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
R306A
site-directed mutagenesis, biofilm formation of the mutant is inhibited
R365A
site-directed mutagenesis
R372A
site-directed mutagenesis, the mutant cell motility is inhibited, and biofilm formation of the mutant is inhibited
Y43F
site-directed mutagenesis, heme distal amino acid replacement
D609A
site-directed mutagenesis, inactive mutant
D626A
site-directed mutagenesis, inactive mutant
D652A
site-directed mutagenesis, inactive mutant
D70A
mutated in the response regulator domain, no significant formation of clusters
E253A
mutated in active site, protein forms subcellular clusters in broth-grown cells
GGAAF
-
catalytically dead mutant of active site motif GGEEF, inactive, able to bind cyclic di-3,5-guanylate although nucleotide-free when purified, compact dimer-tetramer equilibrium like nucleotide-free wild-type
K614A
site-directed mutagenesis, inactive mutant
K722A
site-directed mutagenesis, inactive mutant
R198/242A
-
double mutant of inhibitory site RxxD, highly active
R595A
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
R641A
site-directed mutagenesis, inactive mutant
R641A/R644A
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
R672A
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme
V72D
mutated in the response regulator domain, no significant formation of clusters
K614A
-
site-directed mutagenesis, inactive mutant
-
R595A
-
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
-
R641A
-
site-directed mutagenesis, inactive mutant
-
R672A
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme
-
K614A
-
site-directed mutagenesis, inactive mutant
-
R595A
-
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
-
R641A
-
site-directed mutagenesis, inactive mutant
-
R672A
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme
-
K614A
-
site-directed mutagenesis, inactive mutant
-
R595A
-
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
-
R641A
-
site-directed mutagenesis, inactive mutant
-
R672A
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme
-
K614A
-
site-directed mutagenesis, inactive mutant
-
R595A
-
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
-
R641A
-
site-directed mutagenesis, inactive mutant
-
R672A
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme
-
K614A
-
site-directed mutagenesis, inactive mutant
-
R595A
-
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
-
R641A
-
site-directed mutagenesis, inactive mutant
-
R672A
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme
-
K614A
-
site-directed mutagenesis, inactive mutant
-
R595A
-
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
-
R641A
-
site-directed mutagenesis, inactive mutant
-
R672A
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme
-
K614A
-
site-directed mutagenesis, inactive mutant
-
R595A
-
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
-
R641A
-
site-directed mutagenesis, inactive mutant
-
R672A
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme
-
D413K
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
E360R
site-directed mutagenesis, the mutant shows about 50% increased activity compared to wild-type, but reduced biofilm formation despite elevated levels of c-di-GMP production
E429R
site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type, but reduced biofilm formation despite elevated levels of c-di-GMP production
R363E
site-directed mutagenesis, the I-site mutant shows a 20fold increase in c-di-GMP production
R366E
site-directed mutagenesis, the I-site mutant shows a 16fold increase in c-di-GMP production
D413K
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type
-
E360R
-
site-directed mutagenesis, the mutant shows about 50% increased activity compared to wild-type, but reduced biofilm formation despite elevated levels of c-di-GMP production
-
E429R
-
site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type, but reduced biofilm formation despite elevated levels of c-di-GMP production
-
R366E
-
site-directed mutagenesis, the I-site mutant shows a 16fold increase in c-di-GMP production
-
WspGCN4-RGGDEF
-
fusion protein, coiled-coil segment of GCN4 from Saccharomyces cerevisiae, C-terminal diguanylate cyclase domain with the characteristic GGDEF motif and the active site
WspRD70N
-
mutant, point mutation at the predicted phosphorylation site in the REC domain
WspRGGDEF
-
residues 172-347, C-terminal diguanylate cyclase domain with the characteristic GGDEF motif and the active site
WspRstalk-GGDEF
-
residues 140-347, catalytic activity is modulated by the helical stalk motif, C-terminal diguanylate cyclase domain with the characteristic GGDEF motif and the active site
D287A/E288A
-
mutant has no cyclase activity
E415A
-
mutant has cyclase activity but no phosphodiesterase activity
D177A
mutation in salt bridge, decrease in melting temperature by 12.3 degrees
E196A
mutation in salt bridge, decrease in melting temperature by 4.2 degrees
R233A
mutation in salt bridge, decrease in melting temperature by 8.6 degrees
D177A
-
mutation in salt bridge, decrease in melting temperature by 12.3 degrees
-
E196A
-
mutation in salt bridge, decrease in melting temperature by 4.2 degrees
-
R158A
-
mutation at the inhibitory site, abolishing product inhibition and unproductive dimerization
-
R233A
-
mutation in salt bridge, decrease in melting temperature by 8.6 degrees
-
D484E
RXXD allosteric inhibition site of the protein is mutated (VC2370(142)-D484E) because it is shown, using HPLC-MS-MS, that c-di-GMP copurifies with native VC2370. Mutation of this RXXD site prevents c-di-GMP copurification. Also, mutation of the site ensures that c-di-GMP produced during the in vitro reaction is not able to inhibit enzyme activity
K759A
mutagenesis of a conserved lysine residue, results in a severe reduction in dihuanylate cyclase activity, kcat value is almost 100fold lower than that of the wild-type protein while the K1 and K2 values do not change very much
D53N
less than 1% of wild-type activity
D53N
no activation by BeF3, lack of phosphoryl acceptor site
E370Q
mutation in active site, complete loss of catalytic activity without effect on allosteric binding of cyclic diguanylate
E370Q
mainly dimeric, inactive mutant of the guanylate cyclase domain GG(D/E)EF (Mg2+ coordination), no activation by BeF3 or protein concentration above 50 microM
R148A/R178A
increase in allosteric binding of cyclic diguanylate and increase in catalytic activity
R148A/R178A
double mutant
Y26A
almost complete loss of activity
Y26A
dimerisation mutant, nearly inactive, mainly monomeric
D418A
-
site-directed mutagenesis, replacing the essential aspartic acid residue with alanine (SGAEF), resulting in a mutant that is not defective for growth when compared with the wild-type strain, but the enzyme is catalytically inactive and shows abolished negative Pel regulation, instead the mutation of the GcpA A-site enhances the production of Pel
D418A
-
site-directed mutagenesis, replacing the essential aspartic acid residue with alanine (SGAEF), resulting in a mutant that is not defective for growth when compared with the wild-type strain, but the enzyme is catalytically inactive and shows abolished negative Pel regulation, instead the mutation of the GcpA A-site enhances the production of Pel
-
Y43A
site-directed mutagenesis
Y43A
site-directed mutagenesis, heme distal amino acid replacement leading to reduced activity compared to wild-type
L167D
-
predominantly monomeric, weakly associated dimer, purifies cyclic di-3,5-guanylate-bound, inactive (also upon cyclic di-3,5-guanylate hydrolysis)
L167D
mutated in linker stalk, low formation of clusters
L170D
-
highly active also in cyclic di-3,5-guanylate-bound state, in compact dimer-tetramer equilibrium like nucleotide-free wild-type
L170D
mutated in linker stalk, protein forms subcellular clusters in broth-grown cells
R198A
-
mutant of side chain complementing the inhibitory site R242xxD, highly active, low cyclic di-3,5-guanylate affinity, nucleotide-free, in compact dimer-tetramer equilibrium like nucleotide-free wild-type
R198A
mutated in I site, protein forms subcellular clusters in broth-grown cells
R242A
-
mutant of inhibitory site RxxD, highly active, low cyclic di-3,5-guanylate affinity, nucleotide-free, in compact dimer-tetramer equilibrium like nucleotide-free wild-type
R242A
-
mutant sows activity and is used as a target enzyme. Mutation locks the enzyme in a constitutively active state
R158A
mutation of a key residue in the putative regulatory I-site, product inhibition is substantially alleviated
R158A
-
mutant shows increased enzymatic activity compared to wild-type, mutant shows 4fold lower expression level compared to wild-type which might be due to higher enzymatic activity of mutant R158A and its increased toxicity for cells
R158A
mutation at the inhibitory site, abolishing product inhibition and unproductive dimerization
additional information
-
enzyme disruption mutants of MifA or MifB show increased flagellin levels, while mutlicopy expression decreases them
additional information
generation of truncated enzyme mutants BpeGReg1-155, BpeGReg1-266, BpeGReg1-296, BpeGReg156-475, BpeGReg267-475, and BpeGReg297-475
additional information
-
generation of truncated enzyme mutants BpeGReg1-155, BpeGReg1-266, BpeGReg1-296, BpeGReg156-475, BpeGReg267-475, and BpeGReg297-475
additional information
-
generation of truncated enzyme mutants BpeGReg1-155, BpeGReg1-266, BpeGReg1-296, BpeGReg156-475, BpeGReg267-475, and BpeGReg297-475
-
additional information
-
generation of truncated enzyme mutants BpeGReg1-155, BpeGReg1-266, BpeGReg1-296, BpeGReg156-475, BpeGReg267-475, and BpeGReg297-475
-
additional information
-
generation of truncated enzyme mutants BpeGReg1-155, BpeGReg1-266, BpeGReg1-296, BpeGReg156-475, BpeGReg267-475, and BpeGReg297-475
-
additional information
-
cells overexpressing diguanylate cyclase YddV display an abnormal cell division process when high levels of cyclic diguanylate are present. Gene yvvD is co-transcribed with dos, a heme based oxygen sensor with cyclic diguanylate phosphodiesterase activity
additional information
-
a mutant, carrying an adrA mutation resulting in GGDEF -> GGAAF change in AdrA protein catalytic site, is constructed
additional information
chromosomal replacement of the corresponding wild-type gene by mVENUS fusions to dgcZ wild-type or mutant variants, as well as by mCHERRY fusions to frdA and frdB, are achieved by standardFRED-mediated recombineering. In each case, the PRham-ccdB-kan element replaced the wild-type locus in the precursor strain. The dgcZ(+) and frdA(+) control strains are obtained by replacing the PRham-ccdBkan element with the dgcZ and frdA genes amplified from Escherichia coli strain MG1655
additional information
-
chromosomal replacement of the corresponding wild-type gene by mVENUS fusions to dgcZ wild-type or mutant variants, as well as by mCHERRY fusions to frdA and frdB, are achieved by standardFRED-mediated recombineering. In each case, the PRham-ccdB-kan element replaced the wild-type locus in the precursor strain. The dgcZ(+) and frdA(+) control strains are obtained by replacing the PRham-ccdBkan element with the dgcZ and frdA genes amplified from Escherichia coli strain MG1655
additional information
-
disruption of dgc genes markedly reduces in vivo cellulose production in Acetobacter xylinum
additional information
Marinobacter nauticus
isolated G-A1U3W3 domain (residues 155312) has full enzymatic activity and synthesize c-di-GMP
additional information
-
deletion of gene PA4367 results in severe defect in swarming motility and a hyperbiofilm phenotype. Mutant exhibits increased cellular pools of cyclic di-3,5-guanylate, increased synthesis of a polysaccharide produced by the pel locus and decreased flagellar reversals. GGDQF and EAL domains of BifA are both required for complementation of the mutant
additional information
mutating the critical GGEEF motif to GGAAF results in loss of stimulation of Pel polysaccharide production and biofilm formation
additional information
mutating the critical GGEEF motif to GGAAF results in loss of stimulation of Pel polysaccharide production and biofilm formation
additional information
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mutating the critical GGEEF motif to GGAAF results in loss of stimulation of Pel polysaccharide production and biofilm formation
additional information
construction and expression of the PA0847 transposon mutants DELTAPA0847-1 and DELTAPA0847-2 in Pseudomonas aeruginosa strain PAO1, comparison to wild-type, phenotypes, overview. Generation of an enzyme deletion mutant, DELTAPA0847
additional information
construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
additional information
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construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
additional information
construction of DELTAPPA3177 deletion strain, phenotype, overview
additional information
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construction of DELTAPPA3177 deletion strain, phenotype, overview
additional information
generation of a catalytically inactive HsbD GGAAF mutant which does not trigger the intracellular c-di-GMP output. Engineering of hsbD deletion in the Pseudomonas aeruginosa wild-type and DELTAhptB (hptB deletion) background, phenotypes, overview. In the DELTAhptBDELTAhsbD background, both c-di-GMP levels and the expression of the cdrA-gfp fusion are reduced when compared to the DELTAhptB background and they are similar to the wild-type strain. Differences in c-di-GMP levels or in the expression of the reporter construct between a DELTAhsbD mutant and the wild-type strain are not observed
additional information
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generation of a catalytically inactive HsbD GGAAF mutant which does not trigger the intracellular c-di-GMP output. Engineering of hsbD deletion in the Pseudomonas aeruginosa wild-type and DELTAhptB (hptB deletion) background, phenotypes, overview. In the DELTAhptBDELTAhsbD background, both c-di-GMP levels and the expression of the cdrA-gfp fusion are reduced when compared to the DELTAhptB background and they are similar to the wild-type strain. Differences in c-di-GMP levels or in the expression of the reporter construct between a DELTAhsbD mutant and the wild-type strain are not observed
additional information
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construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
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additional information
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construction of DELTAPPA3177 deletion strain, phenotype, overview
-
additional information
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construction and expression of the PA0847 transposon mutants DELTAPA0847-1 and DELTAPA0847-2 in Pseudomonas aeruginosa strain PAO1, comparison to wild-type, phenotypes, overview. Generation of an enzyme deletion mutant, DELTAPA0847
-
additional information
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construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
-
additional information
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generation of a catalytically inactive HsbD GGAAF mutant which does not trigger the intracellular c-di-GMP output. Engineering of hsbD deletion in the Pseudomonas aeruginosa wild-type and DELTAhptB (hptB deletion) background, phenotypes, overview. In the DELTAhptBDELTAhsbD background, both c-di-GMP levels and the expression of the cdrA-gfp fusion are reduced when compared to the DELTAhptB background and they are similar to the wild-type strain. Differences in c-di-GMP levels or in the expression of the reporter construct between a DELTAhsbD mutant and the wild-type strain are not observed
-
additional information
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construction of DELTAPPA3177 deletion strain, phenotype, overview
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additional information
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construction and expression of the PA0847 transposon mutants DELTAPA0847-1 and DELTAPA0847-2 in Pseudomonas aeruginosa strain PAO1, comparison to wild-type, phenotypes, overview. Generation of an enzyme deletion mutant, DELTAPA0847
-
additional information
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construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
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additional information
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construction of DELTAPPA3177 deletion strain, phenotype, overview
-
additional information
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construction and expression of the PA0847 transposon mutants DELTAPA0847-1 and DELTAPA0847-2 in Pseudomonas aeruginosa strain PAO1, comparison to wild-type, phenotypes, overview. Generation of an enzyme deletion mutant, DELTAPA0847
-
additional information
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construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
-
additional information
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construction of DELTAPPA3177 deletion strain, phenotype, overview
-
additional information
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construction and expression of the PA0847 transposon mutants DELTAPA0847-1 and DELTAPA0847-2 in Pseudomonas aeruginosa strain PAO1, comparison to wild-type, phenotypes, overview. Generation of an enzyme deletion mutant, DELTAPA0847
-
additional information
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construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
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additional information
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construction of DELTAPPA3177 deletion strain, phenotype, overview
-
additional information
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construction and expression of the PA0847 transposon mutants DELTAPA0847-1 and DELTAPA0847-2 in Pseudomonas aeruginosa strain PAO1, comparison to wild-type, phenotypes, overview. Generation of an enzyme deletion mutant, DELTAPA0847
-
additional information
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construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
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additional information
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construction of DELTAPPA3177 deletion strain, phenotype, overview
-
additional information
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construction and expression of the PA0847 transposon mutants DELTAPA0847-1 and DELTAPA0847-2 in Pseudomonas aeruginosa strain PAO1, comparison to wild-type, phenotypes, overview. Generation of an enzyme deletion mutant, DELTAPA0847
-
additional information
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construction of an N-terminally truncated SadC containing amino acid residue 300-487, which included the entire GGDEF domain and 23 amino acid residues at the N-terminus to link GGDEF domain with the transmembrane domains. Recombinant strain PAO1/pSadC300-487 fails to promote bacterial cell aggregation even if its expression is induced by 2% arabinose. Moreover, SadC300-487 does not significantly enhance the biofilm formation of PAO1 although SadC300-487 can increase Psl production to a level close to the full-length SadC when induced by 2% arabinose. The crystal structure of SadC323-487 indicates that this truncated SadC is a monomer in the asymmetric unit. The structure of SadC323-487 contains five beta-sheets sandwiched by five alpha-helices, which is a typical GGDEF structure. SadC300-487 can catalyze the synthesis of c-di-GMP in vitro, but SadC323-487 cannot, structure-function analysis, overview
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additional information
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construction of DELTAPPA3177 deletion strain, phenotype, overview
-
additional information
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construction and expression of the PA0847 transposon mutants DELTAPA0847-1 and DELTAPA0847-2 in Pseudomonas aeruginosa strain PAO1, comparison to wild-type, phenotypes, overview. Generation of an enzyme deletion mutant, DELTAPA0847
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additional information
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mutant bearing a GGDEF-to-GGAAF mutation is able to complement a deletion mutant
additional information
mutant bearing a GGDEF-to-GGAAF mutation is able to complement a deletion mutant
additional information
mutant bearing a GGDEF-to-GGAAF mutation is able to complement a deletion mutant
additional information
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mutant bearing a GGDEF-to-GGAAF mutation is not able to complement a deletion mutant
additional information
mutant bearing a GGDEF-to-GGAAF mutation is not able to complement a deletion mutant
additional information
mutant bearing a GGDEF-to-GGAAF mutation is not able to complement a deletion mutant
additional information
a mutagenic bacterial two-hybrid (B2H) screen is conducted to identify alleles of GcbC that fail to interact with LapD. Disruption of the I-site of GcbC leads to deregulation of c-di-GMP production
additional information
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a mutagenic bacterial two-hybrid (B2H) screen is conducted to identify alleles of GcbC that fail to interact with LapD. Disruption of the I-site of GcbC leads to deregulation of c-di-GMP production
additional information
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generation of the adrA mutant harbouring the pCdrA::gfpC biosensor vector, the adrA mutant shows enhanced fliC expression
additional information
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generation of the adrA mutant harbouring the pCdrA::gfpC biosensor vector, the adrA mutant shows enhanced fliC expression
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additional information
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a mutagenic bacterial two-hybrid (B2H) screen is conducted to identify alleles of GcbC that fail to interact with LapD. Disruption of the I-site of GcbC leads to deregulation of c-di-GMP production
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additional information
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construction of a gcsA-deletion mutant. The deletion and complementation of gcsA shows no obvious influence on the growth rate of the strains in liquid LB broth. The normalized GFP fluorescence in the gcsA-deletion strain and complemented strain shows no significant difference compared to that in the wild-type strain at 24 h after inoculation. The gcsA deletion mutant contains about a 27% lower amount of c-di-GMP, and the gcsA-complemented strain contains about a 30% higher amount of c-di-GMP compared to the wild-type strain at the 5 h time point. Comparison of swimming motility, biofilm formation, and surface morphology of the gcsA mutant and complemented strain, overview
additional information
construction of a gcsA-deletion mutant. The deletion and complementation of gcsA shows no obvious influence on the growth rate of the strains in liquid LB broth. The normalized GFP fluorescence in the gcsA-deletion strain and complemented strain shows no significant difference compared to that in the wild-type strain at 24 h after inoculation. The gcsA deletion mutant contains about a 27% lower amount of c-di-GMP, and the gcsA-complemented strain contains about a 30% higher amount of c-di-GMP compared to the wild-type strain at the 5 h time point. Comparison of swimming motility, biofilm formation, and surface morphology of the gcsA mutant and complemented strain, overview
additional information
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mutation in the GGDEF motif from GGDEF to GGAAF abolishes the cyclic diguanylate synthesis ability of GcsA
additional information
mutation in the GGDEF motif from GGDEF to GGAAF abolishes the cyclic diguanylate synthesis ability of GcsA
additional information
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construction of a gcsA-deletion mutant. The deletion and complementation of gcsA shows no obvious influence on the growth rate of the strains in liquid LB broth. The normalized GFP fluorescence in the gcsA-deletion strain and complemented strain shows no significant difference compared to that in the wild-type strain at 24 h after inoculation. The gcsA deletion mutant contains about a 27% lower amount of c-di-GMP, and the gcsA-complemented strain contains about a 30% higher amount of c-di-GMP compared to the wild-type strain at the 5 h time point. Comparison of swimming motility, biofilm formation, and surface morphology of the gcsA mutant and complemented strain, overview
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additional information
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mutation in the GGDEF motif from GGDEF to GGAAF abolishes the cyclic diguanylate synthesis ability of GcsA
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additional information
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construction of a gcsA-deletion mutant. The deletion and complementation of gcsA shows no obvious influence on the growth rate of the strains in liquid LB broth. The normalized GFP fluorescence in the gcsA-deletion strain and complemented strain shows no significant difference compared to that in the wild-type strain at 24 h after inoculation. The gcsA deletion mutant contains about a 27% lower amount of c-di-GMP, and the gcsA-complemented strain contains about a 30% higher amount of c-di-GMP compared to the wild-type strain at the 5 h time point. Comparison of swimming motility, biofilm formation, and surface morphology of the gcsA mutant and complemented strain, overview
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additional information
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construction of a gcsA-deletion mutant. The deletion and complementation of gcsA shows no obvious influence on the growth rate of the strains in liquid LB broth. The normalized GFP fluorescence in the gcsA-deletion strain and complemented strain shows no significant difference compared to that in the wild-type strain at 24 h after inoculation. The gcsA deletion mutant contains about a 27% lower amount of c-di-GMP, and the gcsA-complemented strain contains about a 30% higher amount of c-di-GMP compared to the wild-type strain at the 5 h time point. Comparison of swimming motility, biofilm formation, and surface morphology of the gcsA mutant and complemented strain, overview
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additional information
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mutating the Chp8 GGDEF motif impairs cyclic di-GMP production and biofilm formation. Inactivation of the Chp8 phosphodiesterase domain also interferes with cyclic di-GMP production despite an unmodified DGC domain
additional information
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mutating the Chp8 GGDEF motif impairs cyclic di-GMP production and biofilm formation. Inactivation of the Chp8 phosphodiesterase domain also interferes with cyclic di-GMP production despite an unmodified DGC domain
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additional information
generation of knockout DELTAslr1143 mutants of Cph2. Whereas wild-type cells are non-motile under high-intensity red light of 640 nm, the mutant DELTAslr1143 displays positive phototaxis. This phenotype can be complemented by overexpression of full-length Slr1143, which also results in an increased cellular c-di-GMP concentration. However, the non-motile phenotype of wild-type cells under high-intensity red light appears not to be due to an elevated cellular c-di-GMP content
additional information
ITC analysis of interactions between different amino acids and the periplasmic portion of CdgH with different truncations and mutants, overview
additional information
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ITC analysis of interactions between different amino acids and the periplasmic portion of CdgH with different truncations and mutants, overview
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additional information
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ITC analysis of interactions between different amino acids and the periplasmic portion of CdgH with different truncations and mutants, overview
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Ausmees, N.; Mayer, R.; Weinhouse, H.; Volman, G.; Amikam, D.; Benziman, M.; Lindberg, M.
Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity
FEMS Microbiol. Lett.
204
163-167
2001
Escherichia coli, Komagataeibacter xylinus, Rhizobium leguminosarum
brenda
Paul, R.; Weiser, S.; Amiot, N.C.; Chan, C.; Schirmer, T.; Giese, B.; Jenal, U.
Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain
Genes Dev.
18
715-727
2004
Caulobacter vibrioides
brenda
Tal, R.; Wong, H.C.; Calhoon, R.; Gelfand, D.; Fear, A.L.; Volman, G.; Mayer, R.; Ross, P.; Amikam, D.; Weinhouse, H.; Cohen, A.; Sapir, S.; Ohana, P.; Benziman, M.
Three cdg operons control cellular turnover of cyclic di-GMP in Acetobacter xylinum: genetic organization and occurrence of conserved domains in isoenzymes
J. Bacteriol.
180
4416-4425
1998
Komagataeibacter xylinus
brenda
Ryjenkov, D.A.; Tarutina, M.; Moskvin, O.V.; Gomelsky, M.
Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain
J. Bacteriol.
187
1792-1798
2005
Borreliella burgdorferi, Cereibacter sphaeroides, Cereibacter sphaeroides RSP3513
brenda
O'Shea, T.M.; Klein, A.H.; Geszvain, K.; Wolfe, A.J.; Visick, K.L.
Diguanylate cyclases control magnesium-dependent motility of Vibrio fischeri
J. Bacteriol.
188
8196-8205
2006
Aliivibrio fischeri
brenda
Kuchma, S.L.; Brothers, K.M.; Merritt, J.H.; Liberati, N.T.; Ausubel, F.M.; O'Toole, G.A.
BifA, a cyclic-Di-GMP phosphodiesterase, inversely regulates biofilm formation and swarming motility by Pseudomonas aeruginosa PA14
J. Bacteriol.
189
8165-8178
2007
Pseudomonas aeruginosa
brenda
Christen, B.; Christen, M.; Paul, R.; Schmid, F.; Folcher, M.; Jenoe, P.; Meuwly, M.; Jenal, U.
Allosteric control of cyclic di-GMP signaling
J. Biol. Chem.
281
32015-32024
2006
Caulobacter vibrioides (Q9A3B9)
brenda
Mendez-Ortiz, M.M.; Hyodo, M.; Hayakawa, Y.; Membrillo-Hernandez, J.
Genome-wide transcriptional profile of Escherichia coli in response to high levels of the second messenger 3', 5'-cyclic diguanylic acid. [Erratum to document cited in CA144:426702]
J. Biol. Chem.
282
22248
2007
Escherichia coli
-
brenda
Paul, R.; Abel, S.; Wassmann, P.; Beck, A.; Heerklotz, H.; Jenal, U.
Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization
J. Biol. Chem.
282
29170-29177
2007
Caulobacter vibrioides, Caulobacter vibrioides (Q9A5I5)
brenda
Andrade, M.O.; Alegria, M.C.; Guzzo, C.R.; Docena, C.; Rosa, M.C.P.; Ramos, C.H.I.; Farah, C.S.
The HD-GYP domain of RpfG mediates a direct linkage between the Rpf quorum-sensing pathway and a subset of diguanylate cyclase proteins in the phytopathogen Xanthomonas axonopodis pv citri
Mol. Microbiol.
62
537-551
2006
Xanthomonas axonopodis
brenda
Ohana, P.; Delmer, D.P.; Carlson, R.W.; Glushka, J.; Azadi, P.; Bacic, T.; Benziman, M.
Identification of a novel triterpenoid saponin from Pisum sativum as a specific inhibitor of the diguanylate cyclase of Acetobacter xylinum
Plant Cell Physiol.
39
144-152
1998
Komagataeibacter xylinus
brenda
Ohana, P.; Delmer, D.P.; Volman, G.; Benziman, M.
Glycosylated triterpenoid saponin: a specific inhibitor of diguanylate cyclase from Acetobacter xylinum. Biological activity and distribution
Plant Cell Physiol.
39
153-159
1998
Komagataeibacter xylinus
-
brenda
Chan, C.; Paul, R.; Samoray, D.; Amiot, N.C.; Giese, B.; Jenal, U.; Schirmer, T.
Structural basis of activity and allosteric control of diguanylate cyclase
Proc. Natl. Acad. Sci. USA
101
17084-17089
2004
Caulobacter vibrioides
brenda
Wassmann, P.; Chan, C.; Paul, R.; Beck, A.; Heerklotz, H.; Jenal, U.; Schirmer, T.
Structure of BeF3--modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition
Structure
15
915-927
2007
Caulobacter vibrioides, Caulobacter vibrioides (Q9A5I5)
brenda
Neunuebel, M.R.; Golden, J.W.
The Anabaena sp. strain PCC 7120 gene all2874 encodes a diguanylate cyclase and is required for normal heterocyst development under high-light growth conditions
J. Bacteriol.
190
6829-6836
2008
Anabaena sp.
brenda
De, N.; Pirruccello, M.; Krasteva, P.V.; Bae, N.; Raghavan, R.V.; Sondermann, H.
Phosphorylation-independent regulation of the diguanylate cyclase WspR
PLoS Biol.
6
601-617
2008
Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas fluorescens, Pseudomonas syringae, Pseudomonas syringae DC3000, Pseudomonas putida KT 2240, Pseudomonas fluorescens PfO-1
brenda
Rao, F.; Pasunooti, S.; Ng, Y.; Zhuo, W.; Lim, L.; Liu, A.W.; Liang, Z.X.
Enzymatic synthesis of c-di-GMP using a thermophilic diguanylate cyclase
Anal. Biochem.
389
138-142
2009
Thermotoga maritima (Q9X2A8)
brenda
Antoniani, D.; Bocci, P.; Maciag, A.; Raffaelli, N.; Landini, P.
Monitoring of diguanylate cyclase activity and of cyclic-di-GMP biosynthesis by whole-cell assays suitable for high-throughput screening of biofilm inhibitors
Appl. Microbiol. Biotechnol.
85
1095-1104
2010
Escherichia coli
brenda
Tuckerman, J.R.; Gonzalez, G.; Sousa, E.H.; Wan, X.; Saito, J.A.; Alam, M.; Gilles-Gonzalez, M.A.
An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-di-GMP control
Biochemistry
48
9764-9774
2009
Escherichia coli (P0AA89), Escherichia coli
brenda
Sawai, H.; Yoshioka, S.; Uchida, T.; Hyodo, M.; Hayakawa, Y.; Ishimori, K.; Aono, S.
Molecular oxygen regulates the enzymatic activity of a heme-containing diguanylate cyclase (HemDGC) for the synthesis of cyclic di-GMP
Biochim. Biophys. Acta
1804
166-172
2010
Desulfotalea psychrophila (Q6ARU5), Desulfotalea psychrophila
brenda
Lai, T.H.; Kumagai, Y.; Hyodo, M.; Hayakawa, Y.; Rikihisa, Y.
The Anaplasma phagocytophilum PleC histidine kinase and PleD diguanylate cyclase two-component system and role of cyclic Di-GMP in host cell infection
J. Bacteriol.
191
693-700
2009
Anaplasma phagocytophilum (Q2GKF8), Anaplasma phagocytophilum
brenda
De, N.; Navarro, M.V.; Raghavan, R.V.; Sondermann, H.
Determinants for the activation and autoinhibition of the diguanylate cyclase response regulator WspR
J. Mol. Biol.
393
619-633
2009
Pseudomonas syringae
brenda
Sambanthamoorthy, K.; Sloup, R.E.; Parashar, V.; Smith, J.M.; Kim, E.E.; Semmelhack, M.F.; Neiditch, M.B.; Waters, C.M.
Identification of small molecules that antagonize diguanylate cyclase enzymes to inhibit biofilm formation
Antimicrob. Agents Chemother.
56
5202-5211
2012
Pseudomonas aeruginosa, Vibrio cholerae (Q9KPJ7), Vibrio cholerae
brenda
Zaehringer, F.; Massa, C.; Schirmer, T.
Efficient enzymatic production of the bacterial second messenger c-di-GMP by the diguanylate cyclase YdeH from E. coli
Appl. Biochem. Biotechnol.
163
71-79
2011
Escherichia coli
brenda
Tran, N.T.; Den Hengst, C.D.; Gomez-Escribano, J.P.; Buttner, M.J.
Identification and characterization of CdgB, a diguanylate cyclase involved in developmental processes in Streptomyces coelicolor
J. Bacteriol.
193
3100-3108
2011
Streptomyces coelicolor
brenda
Newell, P.; Yoshioka, S.; Hvorecny, K.; Monds, R.; OToole, G.
Systematic analysis of diguanylate cyclases that promote biofilm formation by Pseudomonas fluorescens Pf0-1
J. Bacteriol.
193
4685-4698
2011
Pseudomonas fluorescens, Pseudomonas fluorescens (Q3K751), Pseudomonas fluorescens (Q3KFC4)
brenda
Korovashkina, A.; Rymko, A.; Kvach, S.; Zinchenko, A.
Enzymatic synthesis of c-di-GMP using inclusion bodies of Thermotoga maritima full-length diguanylate cyclase
J. Biotechnol.
164
276-280
2013
Thermotoga maritima
brenda
Pasunooti, S.; Surya, W.; Tan, S.; Liang, Z.
Sol-gel immobilization of a thermophilic diguanylate cyclase for enzymatic production of cyclic-di-GMP
J. Mol. Catal. B
67
98-103
2010
Thermotoga maritima
-
brenda
Spangler, C.; Kaever, V.; Seifert, R.
Interaction of the diguanylate cyclase YdeH of Escherichia coli with 2,(3)-substituted purine and pyrimidine nucleotides
J. Pharmacol. Exp. Ther.
336
234-241
2011
Escherichia coli
brenda
Vorobiev, S.M.; Neely, H.; Yu, B.; Seetharaman, J.; Xiao, R.; Acton, T.B.; Montelione, G.T.; Hunt, J.F.
Crystal structure of a catalytically active GG(D/E)EF diguanylate cyclase domain from Marinobacter aquaeolei with bound c-di-GMP product
J. Struct. Funct. Genomics
13
177-183
2012
Marinobacter nauticus (A1U3W3)
brenda
Merritt, J.; Ha, D.; Cowles, K.; Lu, W.; Morales, D.; Rabinowitz, J.; Gitai, Z.; O'Toole, G.
Specific control of Pseudomonas aeruginosa surface-associated behaviors by two c-di-GMP diguanylate cyclases
mBio
1
e00183
2010
Pseudomonas aeruginosa (Q9HW69), Pseudomonas aeruginosa (Q9I4M8), Pseudomonas aeruginosa
brenda
Tagliabue, L.; Antoniani, D.; Maciag, A.; Bocci, P.; Raffaelli, N.; Landini, P.
The diguanylate cyclase YddV controls production of the exopolysaccharide poly-N-acetylglucosamine (PNAG) through regulation of the PNAG biosynthetic pgaABCD operon
Microbiology
156
2901-2911
2010
Escherichia coli
brenda
Liu, N.; Pak, T.; Boon, E.M.
Characterization of a diguanylate cyclase from Shewanella woodyi with cyclase and phosphodiesterase activities
Mol. Biosyst.
6
1561-1564
2010
Shewanella woodyi
brenda
Kostick, J.L.; Szkotnicki, L.T.; Rogers, E.A.; Bocci, P.; Raffaelli, N.; Marconi, R.T.
The diguanylate cyclase, Rrp1, regulates critical steps in the enzootic cycle of the Lyme disease spirochetes
Mol. Microbiol.
81
219-231
2011
Borreliella burgdorferi
brenda
Tarnawski, M.; Barends, T.R.; Schlichting, I.
Structural analysis of an oxygen-regulated diguanylate cyclase
Acta Crystallogr. Sect. D
71
2158-2177
2015
Escherichia coli (P0AA89), Escherichia coli
brenda
Hunter, J.; Severin, G.; Koestler, B.; Waters, C.
The Vibrio cholerae diguanylate cyclase VCA0965 has an AGDEF active site and synthesizes cyclic di-GMP
BMC Microbiol.
14
22
2014
Vibrio cholerae serotype O1, Vibrio cholerae serotype O1 C6706str2
brenda
Aragon, I.M.; Perez-Mendoza, D.; Moscoso, J.A.; Faure, E.; Guery, B.; Gallegos, M.T.; Filloux, A.; Ramos, C.
Diguanylate cyclase DgcP is involved in plant and human Pseudomonas spp. infections
Environ. Microbiol.
17
4332-4351
2015
Pseudomonas savastanoi pv. savastanoi, Pseudomonas aeruginosa (S0JAX7), Pseudomonas aeruginosa, Pseudomonas savastanoi pv. savastanoi NCPPB 3335, Pseudomonas aeruginosa PAK (S0JAX7)
brenda
Chaudhuri, S.; Pratap, S.; Paromov, V.; Li, Z.; Mantri, C.K.; Xie, H.
Identification of a diguanylate cyclase and its role in Porphyromonas gingivalis virulence
Infect. Immun.
82
2728-2735
2014
Porphyromonas gingivalis (B2RM56), Porphyromonas gingivalis, Porphyromonas gingivalis DSM 20709 (B2RM56)
brenda
Barnhart, D.M.; Su, S.; Farrand, S.K.
A signaling pathway involving the diguanylate cyclase CelR and the response regulator DivK controls cellulose synthesis in Agrobacterium tumefaciens
J. Bacteriol.
196
1257-1274
2014
Agrobacterium tumefaciens
brenda
Petrova, O.E.; Cherny, K.E.; Sauer, K.
The Pseudomonas aeruginosa diguanylate cyclase GcbA, a homolog of P. fluorescens GcbA, promotes initial attachment to surfaces, but not biofilm formation, via regulation of motility
J. Bacteriol.
196
2827-2841
2014
Pseudomonas aeruginosa, Pseudomonas fluorescens
brenda
Enomoto, G.; Nomura, R.; Shimada, T.; Ni-Ni-Win, T.; Narikawa, R.; Ikeuchi, M.
Cyanobacteriochrome SesA is a diguanylate cyclase that induces cell aggregation in Thermosynechococcus
J. Biol. Chem.
289
24801-24809
2014
Thermosynechococcus vestitus (Q8DKD5)
brenda
Oliveira, M.C.; Teixeira, R.D.; Andrade, M.O.; Pinheiro, G.M.; Ramos, C.H.; Farah, C.S.
Cooperative substrate binding by a diguanylate cyclase
J. Mol. Biol.
427
415-432
2015
Xanthomonas citri pv. citri (Q8PPS5), Xanthomonas citri pv. citri
brenda
Huangyutitham, V.; Guevener, Z.T.; Harwood, C.S.
Subcellular clustering of the phosphorylated WspR response regulator protein stimulates its diguanylate cyclase activity
MBio
4
e00242
2013
Pseudomonas aeruginosa (Q9HXT9), Pseudomonas aeruginosa
brenda
Engl, C.; Waite, C.J.; McKenna, J.F.; Bennett, M.H.; Hamann, T.; Buck, M.
Chp8, a diguanylate cyclase from Pseudomonas syringae pv. Tomato DC3000, suppresses the pathogen-associated molecular pattern flagellin, increases extracellular polysaccharides, and promotes plant immune evasion
MBio
5
e01168
2014
Pseudomonas syringae pv. tomato, Pseudomonas syringae pv. tomato DC3000
brenda
Dahlstrom, K.M.; Giglio, K.M.; Collins, A.J.; Sondermann, H.; OToole, G.A.
Contribution of physical interactions to signaling specificity between a diguanylate cyclase and its effector
MBio
6
e01978-15
2015
Pseudomonas fluorescens (Q3K751), Pseudomonas fluorescens, Pseudomonas fluorescens Pf0-1 (Q3K751)
brenda
Kim, H.; Harshey, R.
A diguanylate cyclase acts as a cell division inhibitor in a two-step response to reductive and envelope stresses
MBio
7
e00822
2016
Escherichia coli (P46139)
-
brenda
Rotcheewaphan, S.; Belisle, J.T.; Webb, K.J.; Kim, H.J.; Spencer, J.S.; Borlee, B.R.
Diguanylate cyclase activity of the Mycobacterium leprae T cell antigen ML1419c
Microbiology
162
1651-1661
2016
Mycobacterium leprae (Q7AQ57), Mycobacterium leprae, Mycobacterium leprae TN (Q7AQ57)
brenda
Deepthi, A.; Liew, C.W.; Liang, Z.X.; Swaminathan, K.; Lescar, J.
Structure of a diguanylate cyclase from Thermotoga maritima: insights into activation, feedback inhibition and thermostability
PLoS ONE
9
e110912
2014
Thermotoga maritima (Q9X2A8), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9X2A8)
brenda
Ramirez-Mata, A.; Lopez-Lara, L.I.; Xiqui-Vazquez, M.L.; Jijon-Moreno, S.; Romero-Osorio, A.; Baca, B.E.
The cyclic-di-GMP diguanylate cyclase CdgA has a role in biofilm formation and exopolysaccharide production in Azospirillum brasilense
Res. Microbiol.
167
190-201
2016
Azospirillum brasilense (A0A0Y0RFK5), Azospirillum brasilense, Azospirillum brasilense Sp7 (A0A0Y0RFK5), Azospirillum brasilense Sp7
brenda
Wu, C.; Cheng, Y.Y.; Yin, H.; Song, X.N.; Li, W.W.; Zhou, X.X.; Zhao, L.P.; Tian, L.J.; Han, J.C.; Yu, H.Q.
Oxygen promotes biofilm formation of Shewanella putrefaciens CN32 through a diguanylate cyclase and an adhesin
Sci. Rep.
3
1945
2013
Shewanella putrefaciens, Shewanella putrefaciens CN32
brenda
Su, J.; Zou, X.; Huang, L.; Bai, T.; Liu, S.; Yuan, M.; Chou, S.H.; He, Y.W.; Wang, H.; He, J.
DgcA, a diguanylate cyclase from Xanthomonas oryzae pv. oryzae regulates bacterial pathogenicity on rice
Sci. Rep.
6
25978
2016
Xanthomonas oryzae pv. oryzae (Q5GVN1), Xanthomonas oryzae pv. oryzae, Xanthomonas oryzae pv. oryzae KXO85 (Q5GVN1)
brenda
Chen, Y.; Liu, S.; Liu, C.; Huang, Y.; Chi, K.; Su, T.; Zhu, D.; Peng, J.; Xia, Z.; He, J.; Xu, S.; Hu, W.; Gu, L.
Dcsbis (PA2771) from Pseudomonas aeruginosa is a highly active diguanylate cyclase with unique activity regulation
Sci. Rep.
6
29499
2016
Pseudomonas aeruginosa (Q9I072), Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644 (Q9I072)
brenda
Zaehringer, F.; Lacanna, E.; Jenal, U.; Schirmer, T.; Boehm, A.
Structure and signaling mechanism of a zinc-sensory diguanylate cyclase
Structure
21
1149-1157
2013
Escherichia coli (P31129), Escherichia coli
brenda
Dahlstrom, K.M.; O'Toole, G.A.
A symphony of cyclases specificity in diguanylate cyclase signaling
Annu. Rev. Microbiol.
71
179-195
2017
Caulobacter vibrioides, Clostridioides difficile, Pseudomonas aeruginosa, Burkholderia cenocepacia, Vibrio cholerae serotype O1, Komagataeibacter xylinus (O87374), Escherichia coli (P0AA89), Vibrio cholerae serotype O1 A1552
brenda
Poudyal, B.; Sauer, K.
The PA3177 gene encodes an active diguanylate cyclase that contributes to biofilm antimicrobial tolerance but not biofilm formation by Pseudomonas aeruginosa
Antimicrob. Agents Chemother.
62
e01049-18
2018
Pseudomonas aeruginosa (Q9HZ57), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 (Q9HZ57), Pseudomonas aeruginosa 1C (Q9HZ57), Pseudomonas aeruginosa PRS 101 (Q9HZ57), Pseudomonas aeruginosa DSM 22644 (Q9HZ57), Pseudomonas aeruginosa CIP 104116 (Q9HZ57), Pseudomonas aeruginosa LMG 12228 (Q9HZ57), Pseudomonas aeruginosa JCM 14847 (Q9HZ57)
brenda
Zhu, B.; Liu, C.; Liu, S.; Cong, H.; Chen, Y.; Gu, L.; Ma, L.Z.
Membrane association of SadC enhances its diguanylate cyclase activity to control exopolysaccharides synthesis and biofilm formation in Pseudomonas aeruginosa
Environ. Microbiol.
18
3440-3452
2016
Pseudomonas aeruginosa (Q9HW69), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 (Q9HW69), Pseudomonas aeruginosa 1C (Q9HW69), Pseudomonas aeruginosa PRS 101 (Q9HW69), Pseudomonas aeruginosa DSM 22644 (Q9HW69), Pseudomonas aeruginosa CIP 104116 (Q9HW69), Pseudomonas aeruginosa LMG 12228 (Q9HW69), Pseudomonas aeruginosa JCM 14847 (Q9HW69)
brenda
Xiao, Y.; Liu, H.; He, M.; Nie, L.; Nie, H.; Chen, W.; Huang, Q.
A crosstalk between c-di-GMP and cAMP in regulating transcription of GcsA, a diguanylate cyclase involved in swimming motility in Pseudomonas putida
Environ. Microbiol.
22
142-157
2020
Pseudomonas putida, Pseudomonas putida (Q88GL0), Pseudomonas putida DSM 6125, Pseudomonas putida DSM 6125 (Q88GL0), Pseudomonas putida NCIMB 11950 (Q88GL0), Pseudomonas putida ATCC 47054 (Q88GL0)
brenda
Biswas, S.; Chouhan, O.; Bandekar, D.
Diguanylate cyclases in Vibrio cholerae essential regulators of lifestyle switching
Front. Cell. Infect. Microbiol.
10
582947
2020
Vibrio cholerae, Vibrio cholerae serotype O1 (A0A0H3AFM6), Vibrio cholerae serotype O1 (Q9KKY5), Vibrio cholerae serotype O1 El Tor Inaba N16961 (Q9KKY5), Vibrio cholerae serotype O1 Classical Ogawa 395 (A0A0H3AFM6), Vibrio cholerae serotype O1 ATCC 39541 (A0A0H3AFM6), Vibrio cholerae serotype O1 O395 (A0A0H3AFM6), Vibrio cholerae serotype O1 ATCC 39315 (Q9KKY5)
brenda
Biswas, S.; Chouhan, O.; Bandekar, D.
Diguanylate cyclases in Vibrio cholerae essential regulators of lifestyle switching
Front. Cell. Infect. Microbiol.
10
582947s
2020
Vibrio cholerae
brenda
Cho, K.H.; Tryon, R.G.; Kim, J.H.
Screening for diguanylate cyclase (DGC) inhibitors mitigating bacterial biofilm formation
Front. Chem.
8
264
2020
Caulobacter vibrioides (A0A0H3CCZ8), Caulobacter vibrioides (B8GZM2), Clostridioides difficile (A0A170Y3L9), Komagataeibacter xylinus (O87374), Synechocystis sp. PCC 6803 (P73272), Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZNT5), Pseudomonas aeruginosa (Q9HT84), Pseudomonas aeruginosa (Q9HXT9), Vibrio cholerae serotype O1 (Q9KKZ4), Caulobacter vibrioides CB15N (A0A0H3CCZ8), Pseudomonas aeruginosa ATCC 15692 (Q9HT84), Pseudomonas aeruginosa ATCC 15692 (Q9HXT9), Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412 (Q8ZNT5), Caulobacter vibrioides NA1000 (A0A0H3CCZ8), Caulobacter vibrioides NA1000 (B8GZM2), Pseudomonas aeruginosa 1C (Q9HT84), Pseudomonas aeruginosa 1C (Q9HXT9), Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (Q8ZNT5), Pseudomonas aeruginosa PRS 101 (Q9HT84), Pseudomonas aeruginosa PRS 101 (Q9HXT9), Pseudomonas aeruginosa DSM 22644 (Q9HT84), Pseudomonas aeruginosa DSM 22644 (Q9HXT9), Pseudomonas aeruginosa CIP 104116 (Q9HT84), Pseudomonas aeruginosa CIP 104116 (Q9HXT9), Pseudomonas aeruginosa LMG 12228 (Q9HT84), Pseudomonas aeruginosa LMG 12228 (Q9HXT9), Vibrio cholerae serotype O1 El Tor Inaba N16961 (Q9KKZ4), Pseudomonas aeruginosa JCM 14847 (Q9HT84), Pseudomonas aeruginosa JCM 14847 (Q9HXT9), Vibrio cholerae serotype O1 ATCC 39315 (Q9KKZ4)
brenda
Zhang, Y.; Guo, J.; Zhang, N.; Yuan, W.; Lin, Z.; Huang, W.
Characterization and analysis of a novel diguanylate cyclase PA0847 from Pseudomonas aeruginosa PAO1
Infect. Drug Resist.
12
655-665
2019
Pseudomonas aeruginosa (Q9I594), Pseudomonas aeruginosa ATCC 15692 (Q9I594), Pseudomonas aeruginosa 1C (Q9I594), Pseudomonas aeruginosa PRS 101 (Q9I594), Pseudomonas aeruginosa DSM 22644 (Q9I594), Pseudomonas aeruginosa CIP 104116 (Q9I594), Pseudomonas aeruginosa LMG 12228 (Q9I594), Pseudomonas aeruginosa JCM 14847 (Q9I594)
brenda
Fernicola, S.; Paiardini, A.; Giardina, G.; Rampioni, G.; Leoni, L.; Cutruzzolxa0, F.; Rinaldo, S.
In silico discovery and in vitro validation of catechol-containing sulfonohydrazide compounds as potent inhibitors of the diguanylate cyclase PleD
J. Bacteriol.
198
147-156
2016
Pseudomonas aeruginosa (A0A0C7ADU5), Pseudomonas aeruginosa (Q9HXT9), Caulobacter vibrioides (Q9A5I5), Caulobacter vibrioides, Pseudomonas aeruginosa ATCC 15692 (Q9HXT9), Caulobacter vibrioides ATCC 19089 (Q9A5I5), Pseudomonas aeruginosa 1C (Q9HXT9), Caulobacter vibrioides CB15 (Q9A5I5), Pseudomonas aeruginosa PRS 101 (Q9HXT9), Pseudomonas aeruginosa DSM 22644 (Q9HXT9), Pseudomonas aeruginosa CIP 104116 (Q9HXT9), Pseudomonas aeruginosa LMG 12228 (Q9HXT9), Pseudomonas aeruginosa JCM 14847 (Q9HXT9)
brenda
Dahlstrom, K.M.; Giglio, K.M.; Sondermann, H.; OToole, G.A.
The inhibitory site of a diguanylate cyclase is a necessary element for interaction and signaling with an effector protein
J. Bacteriol.
198
1595-1603
2016
Pseudomonas fluorescens (Q3K751), Pseudomonas fluorescens, Pseudomonas fluorescens Pfl01 (Q3K751)
brenda
Lacanna, E.; Bigosch, C.; Kaever, V.; Boehm, A.; Becker, A.
Evidence for Escherichia coli diguanylate cyclase DgcZ interlinking surface sensing and adhesion via multiple regulatory routes
J. Bacteriol.
198
2524-2535
2016
Escherichia coli (P31129), Escherichia coli
brenda
Lengalova, A.; Fojtikova-Proskova, V.; Vavra, J.; Martinek, V.; Stranava, M.; Shimizu, T.; Martinkova, M.
Kinetic analysis of a globin-coupled diguanylate cyclase, YddV effects of heme iron redox state, axial ligands, and heme distal mutations on catalysis
J. Inorg. Biochem.
201
110833
2019
Escherichia coli (P0AA89), Escherichia coli
brenda
da Costa Vasconcelos, F.N.; Maciel, N.K.; Favaro, D.C.; de Oliveira, L.C.; Barbosa, A.S.; Salinas, R.K.; de Souza, R.F.; Farah, C.S.; Guzzo, C.R.
Structural and enzymatic characterization of a cAMP-dependent diguanylate cyclase from pathogenic Leptospira species
J. Mol. Biol.
429
2337-2352
2017
Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni Fiocruz L1-130 (Q72MQ6)
brenda
Angerer, V.; Schwenk, P.; Wallner, T.; Kaever, V.; Hiltbrunner, A.; Wilde, A.
The protein Slr1143 is an active diguanylate cyclase in Synechocystis sp. PCC 6803 and interacts with the photoreceptor Cph2
Microbiology
163
920-930
2017
Synechocystis sp. PCC 6803 (P73272)
brenda
Yuan, X.; Tian, F.; He, C.; Severin, G.B.; Waters, C.M.; Zeng, Q.; Liu, F.; Yang, C.H.
The diguanylate cyclase GcpA inhibits the production of pectate lyases via the H-NS protein and RsmB regulatory RNA in Dickeya dadantii
Mol. Plant Pathol.
19
1873-1886
2018
Dickeya dadantii, Dickeya dadantii 3937
brenda
Valentini, M.; Laventie, B.J.; Moscoso, J.; Jenal, U.; Filloux, A.
The diguanylate cyclase HsbD intersects with the HptB regulatory cascade to control Pseudomonas aeruginosa biofilm and motility
PLoS Genet.
12
e1006354
2016
Pseudomonas aeruginosa (Q9HYQ2), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 (Q9HYQ2)
brenda
Wan, X.; Saito, J.; Newhouse, J.; Hou, S.; Alam, M.
The importance of conserved amino acids in heme-based globin-coupled diguanylate cyclases
PLoS ONE
12
e0182782
2017
Escherichia coli (P0AA89), Escherichia coli, Bordetella pertussis (Q7VTL8), Bordetella pertussis, Bordetella pertussis Tohama I (Q7VTL8), Bordetella pertussis ATCC BAA-589 (Q7VTL8), Bordetella pertussis NCTC 13251 (Q7VTL8)
brenda
Kuang, S.; Yuan, Y.; Wu, Z.; Peng, R.
Expression, purification and characterization of diguanylate cyclase from Rhodococcus ruber
Protein Expr. Purif.
163
105441
2019
Rhodococcus ruber, Rhodococcus ruber SD3
brenda
Xu, M.; Wang, Y.Z.; Yang, X.A.; Jiang, T.; Xie, W.
Structural studies of the periplasmic portion of the diguanylate cyclase CdgH from Vibrio cholerae
Sci. Rep.
7
1861
2017
Vibrio cholerae serotype O1 (Q9KT38), Vibrio cholerae serotype O1 El Tor Inaba N16961 (Q9KT38), Vibrio cholerae serotype O1 ATCC 39315 (Q9KT38)
brenda
Muriel, C.; Blanco-Romero, E.; Trampari, E.; Arrebola, E.; Duran, D.; Redondo-Nieto, M.; Malone, J.G.; Martin, M.; Rivilla, R.
The diguanylate cyclase AdrA regulates flagellar biosynthesis in Pseudomonas fluorescens F113 through SadB
Sci. Rep.
9
8096
2019
Pseudomonas fluorescens, Pseudomonas fluorescens F113
brenda