About: PilZ domain

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The PilZ protein family is named after the type IV pilus control protein first identified in Pseudomonas aeruginosa, expressed as part of the pil operon. It has a cytoplasmic location and is essential for type IV fimbrial, or pilus, biogenesis. PilZ is a c-di-GMP binding domain and PilZ domain-containing proteins represent the best studied class of c-di-GMP effectors. C-di-GMP, cyclic diguanosine monophosphate, the second messenger in cells, is widespread in and unique to the bacterial kingdom. Elevated intracellular levels of c-di-GMP generally cause bacteria to change from a motile single-cell state to a sessile, adhesive surface-attached multicellular state called biofilm.

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rdf:type	Thing Biomolecule Biomolecule Protein yago:Abstraction100002137 yago:Family108078020 yago:Group100031264 yago:Organization108008335 yago:YagoLegalActor yago:YagoLegalActorGeo yago:YagoPermanentlyLocatedEntity protein yago:SocialGroup107950920 yago:Unit108189659
rdfs:label	PilZ domain (en)
rdfs:comment	The PilZ protein family is named after the type IV pilus control protein first identified in Pseudomonas aeruginosa, expressed as part of the pil operon. It has a cytoplasmic location and is essential for type IV fimbrial, or pilus, biogenesis. PilZ is a c-di-GMP binding domain and PilZ domain-containing proteins represent the best studied class of c-di-GMP effectors. C-di-GMP, cyclic diguanosine monophosphate, the second messenger in cells, is widespread in and unique to the bacterial kingdom. Elevated intracellular levels of c-di-GMP generally cause bacteria to change from a motile single-cell state to a sessile, adhesive surface-attached multicellular state called biofilm. (en)
name	PilZ (en)
foaf:depiction
dct:subject	Protein domains
Wikipage page ID	31902906 (xsd:integer)
Wikipage revision ID	995942874 (xsd:integer)
Link from a Wikipage to another Wikipage	Biofilm Cytoplasm Protein–protein interaction Chemotaxis Sessility (zoology) Pseudomonas aeruginosa Vibrio cholerae Crystal structure Operon Lyme disease Torque Cell (biology) Multicellular organism Flagellar motor switch Carrier protein Protein Protein domains Adhesive surface forces Intracellular Pathogenicity Effector (biology) Borrelia burgdorferi Spirochaete Fimbria (bacteriology) Sequence motif Biogenesis Motile Flagellar motility Mutagenesis, site-directed Allosteric interaction Type IV pilus
sameAs	PilZ domain PilZ domain PilZ domain
dbp:wikiPageUsesTemplate	dbt:Infobox_protein_family dbt:InterPro_content dbt:Orphan dbt:Reflist
thumbnail	wiki-commons:Special:FilePath/PDB_1ywu_EBI.jpg?width=300
caption	the solution NMR structure of the protein of unknown function vca0042 from vibrio cholerae o1 (en)
InterPro	IPR009875 (en)
Pfam	PF07238 (en)
symbol	PilZ (en)
has abstract	The PilZ protein family is named after the type IV pilus control protein first identified in Pseudomonas aeruginosa, expressed as part of the pil operon. It has a cytoplasmic location and is essential for type IV fimbrial, or pilus, biogenesis. PilZ is a c-di-GMP binding domain and PilZ domain-containing proteins represent the best studied class of c-di-GMP effectors. C-di-GMP, cyclic diguanosine monophosphate, the second messenger in cells, is widespread in and unique to the bacterial kingdom. Elevated intracellular levels of c-di-GMP generally cause bacteria to change from a motile single-cell state to a sessile, adhesive surface-attached multicellular state called biofilm. Proteins which contain PilZ are known to interact with the flagellar switch-complex proteins FliG and FliM and this is mediated via the c-di-GMP-PliZ complex. This interaction results in a reduction of torque-generation and induces counterclockwise motor bias that slows the motor and induces counterclockwise rotation, inhibiting chemotaxis. Binding and mutagenesis studies of several PilZ domain proteins have shown 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. The PilZ domain is also implicated in the bacterial pathogenicity of the Lyme disease spirochaete, Borrelia burgdorferi, through its binding partner c-di-GMP. (en)
prov:wasDerivedFrom	wikipedia-en:PilZ_domain?oldid=995942874&ns=0
page length (characters) of wiki page	5492 (xsd:nonNegativeInteger)
Symbol	PilZ
foaf:isPrimaryTopicOf	wikipedia-en:PilZ_domain
is foaf:primaryTopic of	wikipedia-en:PilZ_domain

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