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Literature summary for 2.7.13.3 extracted from

  • Xu, L.; Venkataramani, P.; Ding, Y.; Liu, Y.; Deng, Y.; Yong, G.L.; Xin, L.; Ye, R.; Zhang, L.; Yang, L.; Liang, Z.X.
    A cyclic di-GMP-binding adaptor protein interacts with histidine kinase to regulate two-component signaling (2016), J. Biol. Chem., 291, 16112-16123 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q9I019
-
-

Synonyms

Synonyms Comment Organism
PA2824
-
 Pseudomonas aeruginosa
SagS
-
 Pseudomonas aeruginosa

General Information

General Information Comment Organism
physiological function free-standing PilZ protein PA2799 interacts directly with the histidine kinase SagS. PA2799 binds directly to the phosphoreceiver domain of SagS, and the SagS-HapZ interaction is further enhanced at elevated c-di-GMP concentration. Binding of HapZ to SagS inhibits the phosphotransfer between SagS and the downstream protein HptB in a c-di-GMP-dependent manner. HapZ impacts surface attachment and biofilm formation most likely by regulating the expression of a large number of genes Pseudomonas aeruginosa