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Literature summary extracted from

  • 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 (2016), J. Bacteriol., 198, 2524-2535 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.65 paraquat enhances DgcZ-dependent biofilm formation in an FRD-dependent fashion Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.65 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

EC Number Protein Variants Comment Organism
2.7.7.65 H79L/H83L site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme, cellular localization is unaltered Escherichia coli
2.7.7.65 H79L/H83L/E208Q site-directed mutagenesis, inactive mutant, cellular localization is unaltered Escherichia coli
2.7.7.65 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

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.7.65 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
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2.7.7.65 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
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-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.65 Zn2+ involved in enzyme activity regulation Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.65 2 GTP Escherichia coli
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 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.65 Escherichia coli P31129
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.65 2 GTP
-
 Escherichia coli 2 diphosphate + cyclic di-3',5'-guanylate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.7.65 DgcZ
-
 Escherichia coli
2.7.7.65 YdeH
-
 Escherichia coli

Expression

EC Number Organism Comment Expression
2.7.7.65 Escherichia coli gene dgcZ transcription is activated by the transcriptional regulator CpxR up

General Information

EC Number General Information Comment Organism
2.7.7.65 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
2.7.7.65 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
2.7.7.65 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