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Literature summary for 2.7.7.65 extracted from

  • 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 (2016), PLoS Genet., 12, e1006354 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.65

Cloned(Commentary)

Cloned (Comment) Organism
gene hsbD, phylogenetic analysis, the c-di-GMP synthase gene is encoded in the proximity of the hptB and flagellar genes cluster, recombinant overexpression in Escherichia coli leading to increased intracellular c-di-GMP levels. Recombinant expression of YFP-tagged enzyme, the YFP tag is bound to the DGC domain Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment Organism
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 Pseudomonas aeruginosa

Localization

Localization Comment Organism GeneOntology No. Textmining
cell pole HsbD localizes at the cell pole. HsbD and FlhF colocalize transiently at the pole Pseudomonas aeruginosa 60187
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additional information HptB affects the overall distribution of HsbD localization. The frequency of cells exhibiting HsbDC-ter-YFP at both cell poles is significantly increased in a hptB mutant Pseudomonas aeruginosa
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 GTP Pseudomonas aeruginosa
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 2 diphosphate + cyclic di-3',5'-guanylate
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 ?
2 GTP Pseudomonas aeruginosa ATCC 15692
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 2 diphosphate + cyclic di-3',5'-guanylate
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 ?
additional information Pseudomonas aeruginosa 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 ?
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additional information Pseudomonas aeruginosa ATCC 15692 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 ?
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Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q9HYQ2
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Pseudomonas aeruginosa ATCC 15692 Q9HYQ2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 GTP
-
 Pseudomonas aeruginosa 2 diphosphate + cyclic di-3',5'-guanylate
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 ?
2 GTP
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 Pseudomonas aeruginosa ATCC 15692 2 diphosphate + cyclic di-3',5'-guanylate
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 ?
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 Pseudomonas aeruginosa ?
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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 Pseudomonas aeruginosa ATCC 15692 ?
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Synonyms

Synonyms Comment Organism
DGC
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 Pseudomonas aeruginosa
GGDEF domain-containing protein UniProt Pseudomonas aeruginosa
HsbD
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 Pseudomonas aeruginosa

General Information

General Information Comment Organism
evolution the GGDEF domain of HsbD has the conserved RxxDmotif (293-296 aa), which forms the allosteric inhibitory site (I-site) of diguanylate cyclases Pseudomonas aeruginosa
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 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 Pseudomonas aeruginosa