Protein Domain : IPR009875

Type:  Domain Name:  PilZ domain
Description:  The ubiquitous bacterial second messenger cyclic-di-GMP (c-di-GMP) is associated with the regulation of biofilm formation, the control of exopolysaccharide synthesis, flagellar- and pili-based motility, gene expression, interactions of bacteria with eukaryotic hosts and multicellular behaviour in diverse bacteria.With the exception of bacterial cellulose synthases, the identities of c-di-GMP receptors and end targets of the proteins having one or more PilZ domains are mostly uncharacterised. However it was suggested that the PilZ domains present in the BcsA subunits of bacterial cellulose synthases function in c-di-GMP binding []. More recently YcgR (see ) was found to bind c-di-GMP tightly and specifically; also isolated PilZ domains from YcgR and BcsA bound c-di-GMP indicating that the PilZ domain was sufficient for binding of c-di-GMP and significantly that site-directed mutagenesis performed on YcgR implicated the most conserved residues in the PilZ domain directly in c-di-GMP binding []. It was suggested that c-di-GMP binding to PilZ brings about conformational changes in the protein that stabilise the bound ligand and probability initiates the downstream signal transduction cascade. In the case of YcgR, c-di-GMP binding regulates flagellum-based motility in a c-di-GMP-dependent manner (see ) []. The association of the PilZ domain with a variety of other domains, including likely components of bacterial multidrug secretion system, could provide clues to multiple functions of the c-di-GMP in bacterial pathogenesis and cell development.Binding and mutagenesis studies of several PilZ domain proteins have confirmed this observation and demonstrated that c-di-GMP binding depends on residues in RxxxR and D/NxSxxG sequence motifs. The crystal structure, at 1.7 A, of a PilZ domain::c-di-GMP complex from Vibrio cholerae shows c-di-GMP contacting seven of nine strongly conserved residues. Binding of c-di-GMP causes a conformational switch whereby the C- and N-terminal domains are brought into close opposition forming a new allosteric interaction surface that spans these domains and the c-di-GMP at their interface []. Short Name:  PilZ_domain
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1 Child Features

DB identifier Type Name
IPR011752 Domain PilZ domain, deltaproteobacteria

0 Contains

1 Cross References

Identifier
PF07238

1 Found In

DB identifier Type Name
IPR003919 Family Cellulose synthase, subunit A

1 GO Annotation

GO Term Gene Name
GO:0035438 IPR009875

1 Ontology Annotations

GO Term Gene Name
GO:0035438 IPR009875

0 Parent Features

6 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
32997.m000034 B9TCY3 PAC:16825639 Ricinus communis 282  
47909.m000020 B9TP92 PAC:16828037 Ricinus communis 105  
28810.m000044 B9TAL2 PAC:16801723 Ricinus communis 106  
Brdisv1pangenome1010541m.p PAC:33655635 Brachypodium distachyon Pangenome 295  
Brdisv1BdTR11A1048557m.p PAC:35688407 Brachypodium distachyon BdTR11a 295  
Brdisv1BdTR11A1045306m.p PAC:35690159 Brachypodium distachyon BdTR11a 355  

3 Publications

First Author Title Year Journal Volume Pages PubMed ID
            18034161
            16920715
            16249258