Activating Compound | Comment | Organism | Structure |
---|---|---|---|
paraquat | enhances DgcZ-dependent biofilm formation in an FRD-dependent fashion | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
gene dgcZ, recombinant expression of an DgcZ-mVENUS fusion protein which localizes at one bacterial cell pole in response to alkaline pH and carbon starvation | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
H79L/H83L | site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme, cellular localization is unaltered | Escherichia coli |
H79L/H83L/E208Q | site-directed mutagenesis, inactive mutant, cellular localization is unaltered | Escherichia coli |
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 | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell pole | polar localization of DgcZ is independent of protein activity and concentration. Polar localization of DgcZ is induced by carbon starvation and alkaline pH | Escherichia coli | 60187 | - |
additional information | 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 | Escherichia coli | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | involved in enzyme activity regulation | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 GTP | Escherichia coli | - |
2 diphosphate + cyclic di-3',5'-guanylate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P31129 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 GTP | - |
Escherichia coli | 2 diphosphate + cyclic di-3',5'-guanylate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DgcZ | - |
Escherichia coli |
YdeH | - |
Escherichia coli |
Organism | Comment | Expression |
---|---|---|
Escherichia coli | gene dgcZ transcription is activated by the transcriptional regulator CpxR | up |
General Information | Comment | Organism |
---|---|---|
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 | Escherichia coli |
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 | Escherichia coli |
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 | Escherichia coli |