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Literature summary for 3.4.23.49 extracted from

  • Le Sage, V.; Zhu, L.; Lepage, C.; Portt, A.; Viau, C.; Daigle, F.; Gruenheid, S.; Le Moual, H.
    An outer membrane protease of the omptin family prevents activation of the Citrobacter rodentium PhoPQ two-component system by antimicrobial peptides (2009), Mol. Microbiol., 74, 98-111.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Citrobacter rodentium ICC168

Organism

Organism UniProt Comment Textmining
Citrobacter rodentium ICC168 D2TNS3 PhoPQ
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ALYKKLLKKLLKSAKKLG + H2O synthetic alpha-antimicrobial peptide L-C18G, D-amino acids are not degraded by CroP Citrobacter rodentium ICC168 ?
-
?
GLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPEQ + H2O synthetic alpha-antimicrobial peptide CRAMP Citrobacter rodentium ICC168 ?
-
?

Synonyms

Synonyms Comment Organism
Citrobacter rodentium outer-membrane protease
-
Citrobacter rodentium ICC168

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Citrobacter rodentium ICC168

Expression

Organism Comment Expression
Citrobacter rodentium ICC168 croP trancription is reduced in DELTAPhoPQ (two-component system composed of the sensor kinase PhoQ and the cognate response regulator PhoP), indicating that croP expression is partly under under the control of PhoP down

General Information

General Information Comment Organism
malfunction deletion of croP in Citrobacter rodentium results in higher susceptibility to alpha-helical antimicrobial peptides, indicating a direct role of CroP in antimicrobial peptide resistance. Transcriptional activation of PhoP-regulated genes by alpha-helical antimicrobial peptides is restored in the croP mutant Citrobacter rodentium ICC168
physiological function CroP greatly contributes to the protection of the outer membrane from antimicrobial peptides damage by actively degrading alpha-helical antimicrobial peptides before they reach the periplasmic space. Resistance to alpha-helical antimicrobial peptides by the extracellular pathogen Citrobacter rodentium relies primarily on the CroP outer membrane protease Citrobacter rodentium ICC168