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bacteria:t3e:xopk [2025/02/14 16:36] – [References] rkoebnik | bacteria:t3e:xopk [2025/03/31 15:54] (current) – [Biological function] rkoebnik | ||
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Preceded by both a PIP box and a -10 box-like motif (Schulze //et al//., 2012; Furutani //et al//., 2006). | Preceded by both a PIP box and a -10 box-like motif (Schulze //et al//., 2012; Furutani //et al//., 2006). | ||
- | qRT-PCR revealed that transcript levels of 15 out of 18 tested non-TAL effector genes (as well as the regulatory genes //hrpG// and //hrpX//), including //xopK//, were significantly reduced in the // | + | qRT-PCR revealed that transcript levels of 15 out of 18 tested non-TAL effector genes (as well as the regulatory genes //hrpG// and //hrpX//), including //xopK//, were significantly reduced in the // |
=== Phenotypes === | === Phenotypes === | ||
- | * Deletion of XopK has been shown not to affect the virulence of //X. oryzae// pv. // | + | * Deletion of XopK has been shown not to affect the virulence of //X. oryzae// |
- | * A ∆//xopK// mutant strain of // | + | * A ∆// |
- | * XopK inhibits pathogen-associated molecular pattern-triggered immunity upstream of mitogen-activated protein kinase cascades (Qin //et al.//, 2018) | + | * XopK< |
+ | * Transgenic strawberries expressing XopK exhibit increased susceptibility to // | ||
=== 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 |
=== 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 === | ||
- | XopK interacted with and directly ubiquitinated rice somatic embryogenic receptor kinase 2 (OsSERK2), resulting in its degradation (Qin //et al//., 2018) | + | XopK< |
===== Conservation ===== | ===== Conservation ===== | ||
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=== In xanthomonads === | === In xanthomonads === | ||
- | Yes (based on EDGAR; e.g., //X. oryzae// pvs. oryzae and oryzicola, //X. citri// pvs. citri, malvacearum, | + | Yes (based on EDGAR [[https:// |
=== In other plant pathogens/ | === In other plant pathogens/ | ||
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Cai XL, Zhang W, Yu H, Wen YQ, Feng JY (2024). The // | Cai XL, Zhang W, Yu H, Wen YQ, Feng JY (2024). The // | ||
- | < | + | < |
Furutani A, Nakayama T, Ochiai H, Kaku H, Kubo Y, Tsuge S (2006). Identification of novel HrpXo regulons preceded by two // | Furutani A, Nakayama T, Ochiai H, Kaku H, Kubo Y, Tsuge S (2006). Identification of novel HrpXo regulons preceded by two // |