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Literature summary for 3.4.21.53 extracted from

  • Zhou, X.; Teper, D.; Andrade, M.O.; Zhang, T.; Chen, S.; Song, W.Y.; Wang, N.
    A phosphorylation switch on Lon protease regulates bacterial type III secretion system in host (2018), mBio, 9, e02146-17 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.53

Protein Variants

Protein Variants Comment Organism
S654A site-directed mutagenesis, LonS654A is no longer able to be phosphorylated and the mutant loses its virulence. Pathogenicity can fully be restored by addition of exogenous wild-type N-terminally His-tagged HrpG, although not by C-terminally His-tagged HrpG Xanthomonas citri pv. citri
S654D site-directed mutagenesis, the mutant partially retaines its pathogenicity Xanthomonas citri pv. citri
S654E site-directed mutagenesis, the mutant retaines its pathogenicity Xanthomonas citri pv. citri

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Xanthomonas citri pv. citri

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
HrpG + H2O Xanthomonas citri pv. citri the degradation tag is located at the N-terminus of the substrate. The N-terminal moiety of HrpG is required for Lon recognition ?
-
 ?

Organism

Organism UniProt Comment Textmining
Xanthomonas citri pv. citri
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation of Lon at conserved serine 654, which is located in the middle of the second alpha-helix, occurs in the Citrus host. Phosphorylation at Ser654 deactivates Lon proteolytic activity Xanthomonas citri pv. citri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
HrpG + H2O the degradation tag is located at the N-terminus of the substrate. The N-terminal moiety of HrpG is required for Lon recognition Xanthomonas citri pv. citri ?
-
 ?
HrpG + H2O the degradation tag is located at the N-terminus of the substrate Xanthomonas citri pv. citri ?
-
 ?

Synonyms

Synonyms Comment Organism
ATP-dependent protease lon
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 Xanthomonas citri pv. citri
lon
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 Xanthomonas citri pv. citri
lon protease
-
 Xanthomonas citri pv. citri

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Xanthomonas citri pv. citri

General Information

General Information Comment Organism
malfunction substitution of alanine for Lon serine 654 results in repression of T3SS gene expression in the Citrus host through robust degradation of HrpG and reduced bacterial virulence Xanthomonas citri pv. citri
additional information homology modeling of the Xanthomonas citri subsp. citri Lon P domain by using the Escherichia coli Lon structure as a template. Structural simulation using a phosphomimetic aspartic acid at position 654 of the P domain reveals the formation of two new H bonds between two structurally adjacent residues, A655 and S658 after phosphorylation of Ser654 Xanthomonas citri pv. citri
physiological function a phosphorylation switch on Lon protease regulates bacterial type III secretion system in the host. Host-induced phosphorylation of the ATP-dependent protease Lon stabilizes HrpG, the master regulator of T3SS, conferring bacterial virulence. In rich medium, Lon represses the type III secretion system (T3SS) by degradation of HrpG via recognition of its N-terminus. Phosphorylation at Ser654 deactivates Lon proteolytic activity and attenuates HrpG proteolysis. Lon protease negatively regulates bacterial virulence by repressing hrc/hrp gene transcription. Phosphorylation of Lon is required for bacterial virulence and HR induction Xanthomonas citri pv. citri