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Literature summary for 2.7.7.65 extracted from

  • Huangyutitham, V.; Guevener, Z.T.; Harwood, C.S.
    Subcellular clustering of the phosphorylated WspR response regulator protein stimulates its diguanylate cyclase activity (2013), MBio, 4, e00242.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
D70A mutated in the response regulator domain, no significant formation of clusters Pseudomonas aeruginosa
E253A mutated in active site, protein forms subcellular clusters in broth-grown cells Pseudomonas aeruginosa
L167D mutated in linker stalk, low formation of clusters Pseudomonas aeruginosa
L170D mutated in linker stalk, protein forms subcellular clusters in broth-grown cells Pseudomonas aeruginosa
R198A mutated in I site, protein forms subcellular clusters in broth-grown cells Pseudomonas aeruginosa
V72D mutated in the response regulator domain, no significant formation of clusters Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q9HXT9
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein when activated by phosphorylation, yellow fluorescent protein (YFP)-tagged WspR forms clusters that are visible in individual cells by fluorescence microscopy. Unphosphorylated WspR is diffuse in cells and not visible. In general, increased cluster formation correlates with increased in vivo and in vitro diguanylate cyclase activities of variants. In addition, WspR specific activity is strongly concentration dependent in vitro, and the effect of the protein concentration on diguanylate cyclase activity is magnified when WspR is treated with the phosphor analog beryllium fluoride. Cluster formation appears to be an intrinsic property of phosphorylated WspR Pseudomonas aeruginosa

Synonyms

Synonyms Comment Organism
WspR
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Pseudomonas aeruginosa