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Literature summary extracted from

  • Cho, Y.H.; Fadle Aziz, M.R.; Malpass, A.; Sutradhar, T.; Bashal, J.; Cojocari, V.; McPhee, J.B.
    Omptin proteases of enterobacterales show conserved regulation by the PhoPQ two-component system but exhibit divergent protection from antimicrobial host peptides and complement (2023), Infect. Immun., 91, e0051822.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.49 Citrobacter rodentium
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3.4.23.49 Citrobacter rodentium DBS100
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3.4.23.49 Escherichia coli
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3.4.23.49 Escherichia coli BW25113
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Expression

EC Number Organism Comment Expression
3.4.23.49 Escherichia coli expression is induced by growth in low Mg21, and deletion of PhoP dramatically reduces omptin protease activity, transcriptional regulation, and protein levels. Mutation of the putative PhoP-binding site in the ompT promoter abrogates PhoP-dependent expression up
3.4.23.49 Citrobacter rodentium expression is induced by growth in low Mg21, and deletion of PhoP dramatically reduces omptin protease activity, transcriptional regulation, and protein levels. Mutation of the putative PhoP-binding site in the ompT promoter abrogates PhoP-dependent expression up