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bacteria:t3e:xopk [2020/07/08 19:30] rkoebnik [References] |
bacteria:t3e:xopk [2020/07/08 19:31] rkoebnik [Biological function] |
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=== Phenotypes === | === Phenotypes === | ||
- | Deletion of XopK has been shown not to affect the virulence of //X. oryzae// pv. //oryzae// PXO99A in rice IR24 plants; these differential results could be attributed to different genotypes of the rice cultivar or field conditions for plant growth (Song & Yang, 2010). | + | * Deletion of XopK has been shown not to affect the virulence of //X. oryzae// |
+ | * A ∆// | ||
+ | * XopK inhibits pathogen-associated molecular pattern-triggered immunity upstream of mitogen-activated protein kinase cascades (Qin //et al.//, 2018) | ||
- | A ∆//xopK// mutant strain of // | ||
- | |||
- | XopK inhibits pathogen-associated molecular pattern-triggered immunity upstream of mitogen-activated protein kinase cascades (Qin //et al.//, 2018) | ||
=== Localization === | === Localization === | ||
The XopK sequence contains 54% hydrophobic residues and several predicted transmembrane domains. Thus, it is possible this protein is associated with host cell membranes following secretion (Mutka //et al//., 2016) | The XopK sequence contains 54% hydrophobic residues and several predicted transmembrane domains. Thus, it is possible this protein is associated with host cell membranes following secretion (Mutka //et al//., 2016) | ||
+ | |||
=== Enzymatic function === | === Enzymatic function === | ||
- | The protein has E3 ubiquinol ligase activity. The putative E2-binding site is highly conserved in the majority of members from different // | + | The protein has E3 ubiquinol ligase activity. The putative E2-binding site is highly conserved in the majority of members from different // |
=== Interaction partners === | === Interaction partners === | ||