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Literature summary for 3.4.11.5 extracted from

  • Kan, J.; An, L.; Wu, Y.; Long, J.; Song, L.; Fang, R.; Jia, Y.
    A dual role for proline iminopeptidase in the regulation of bacterial motility and host immunity (2018), Mol. Plant Pathol., 19, 2011-2024 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.11.5

Cloned(Commentary)

Cloned (Comment) Organism
gene pip, recombinant expression in transgenic Arabidopsis thaliana plants, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Xanthomonas campestris pv. campestris

Protein Variants

Protein Variants Comment Organism
D246A site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished Xanthomonas campestris pv. campestris
H273A site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished Xanthomonas campestris pv. campestris
additional information disruption and overexpression of gene pip in Xanthomonas campestris pv. campestris altering the bacterial motility via the c-di-GMP levels, phenotypes, overview Xanthomonas campestris pv. campestris
S106A site-directed mutagenesis, active site residue mutant, the enzyme activity is almost completely abolished Xanthomonas campestris pv. campestris

Organism

Organism UniProt Comment Textmining
Xanthomonas campestris pv. campestris Q8PC98
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Xanthomonas campestris pv. campestris ATCC 33913 Q8PC98
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Xanthomonas campestris pv. campestris DSM 3586 Q8PC98
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Xanthomonas campestris pv. campestris LMG 568 Q8PC98
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Xanthomonas campestris pv. campestris NCPPB 528 Q8PC98
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Xanthomonas campestris pv. campestris P 25 Q8PC98
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Xanthomonas campestris pv. campestris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-proline 4-nitroanilide + H2O
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 Xanthomonas campestris pv. campestris L-proline + 4-nitroaniline
-
 ?
L-proline 4-nitroanilide + H2O
-
 Xanthomonas campestris pv. campestris P 25 L-proline + 4-nitroaniline
-
 ?
L-proline 4-nitroanilide + H2O
-
 Xanthomonas campestris pv. campestris NCPPB 528 L-proline + 4-nitroaniline
-
 ?
L-proline 4-nitroanilide + H2O
-
 Xanthomonas campestris pv. campestris LMG 568 L-proline + 4-nitroaniline
-
 ?
L-proline 4-nitroanilide + H2O
-
 Xanthomonas campestris pv. campestris ATCC 33913 L-proline + 4-nitroaniline
-
 ?
L-proline 4-nitroanilide + H2O
-
 Xanthomonas campestris pv. campestris DSM 3586 L-proline + 4-nitroaniline
-
 ?

Synonyms

Synonyms Comment Organism
PIP
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 Xanthomonas campestris pv. campestris
proline iminopeptidase
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 Xanthomonas campestris pv. campestris

General Information

General Information Comment Organism
evolution the pip gene is genetically conserved in many plant-associated bacteria. Enzyme PIP belongs to the prolyl aminopeptidase S33 family, which preferentially releases an N-terminal proline residue from peptides Xanthomonas campestris pv. campestris
malfunction disruption of pip in Xanthomonas campestris pv. campestris enhances the flagella-mediated bacterial motility by decreasing intracellular bis-(3',5')-cyclic dimeric guanosine monophosphate (c-di-GMP) levels, whereas overexpression of pip in Xanthomonas campestris pv. campestris restricts the bacterial motility by elevating c-di-GMP levels. Lack of functional gene pip leads to an extensive induction of flagellum genes in XOLN medium. Of the three classes of flagella-related genes, half of the tested genes are significantly increased in the pip-deficient mutant. Class II genes, such as fleN, fliA, and flgH, are significantly increased by 5.42fold, 28.93fold and 84.21fold, respectively. The expression levels of fliQ and flgB genes are increased even more, by as much as 141.06fold and 130.84fold, respectively, whereas the levels of the other tested flagella-related genes remain unchanged. The levels of Class III genes, such as fliC and fliD, increase by 49.43fold and 9.45fold, respectively. The expression levels of the same genes in the pip-/-pLAFR3-pip strain are complemented or increased compared with that in wild-type Xcc 8004, except for fleN. In contrast, pip overexpression in Xcc 8004 restricts gene expression to even lower levels compared with the pip-/pLAFR3-pip strain Xanthomonas campestris pv. campestris
metabolism PIP interferes with the salicylic acid signalling pathway to benefit bacterial growth Xanthomonas campestris pv. campestris
additional information three residues, S106, D246 and H273, comprise the enzymatic active site of PIP. Mutational alteration of any of these three residues almost completely abolish the enzyme's proline residue-releasing ability from the substrate, demonstrating that these three amino acids are equally essential for the enzymatic activity of PIP Xanthomonas campestris pv. campestris
physiological function enzyme PIP is a type III secretion system-dependent effector capable of eliciting a hypersensitive response in non-host, but not in host plants, e.g. Arabidopsis thaliana. The repressive function of PIP on plant immunity is dependent on PIP's enzymatic activity and acts through interference with the salicylic acid (SA) biosynthetic and regulatory genes. Thus, PIP simultaneously regulates two distinct regulatory networks during plant-microbe interactions, i.e. it affects intracellular c-di-GMP levels to coordinate bacterial behaviour, such as motility, and functions as a type III effector translocated into plant cells to suppress plant immunity. PIP is a repressor or negative regulator of flagellum-mediated motility. Both processes provide the bacteria with the regulatory potential to rapidly adapt to complex environments, to utilize limited resources for growth and survival in a cost-efficient manner and to improve the chances of bacterial survival by helping pathogens to inhabit the internal tissues of host plants Xanthomonas campestris pv. campestris