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bacteria:t3e:xopk [2020/07/08 19:27] rkoebnik old revision restored (2020/07/08 19:21) |
bacteria:t3e:xopk [2020/07/08 19:30] rkoebnik [References] |
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+ | ====== XopK ====== | ||
+ | |||
+ | Author: [[https:// | ||
+ | Internal reviewer: [[https:// | ||
+ | Expert reviewer: FIXME | ||
+ | |||
+ | Class: XopK\\ | ||
+ | Family: XopK\\ | ||
+ | Prototype: XOO1669 (// | ||
+ | RefSeq ID: [[https:// | ||
+ | 3D structure: Unknown | ||
+ | |||
===== Biological function ===== | ===== Biological function ===== | ||
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=== Phenotypes === | === Phenotypes === | ||
- | * Deletion of XopK has been shown not to affect the virulence of //X. oryzae// | + | 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). |
- | * 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 === | ||
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=== In xanthomonads === | === In xanthomonads === | ||
- | Yes (based on EDGAR; e.g., //X. oryzae// | + | Yes (based on EDGAR; e.g., //X. oryzae// pvs. oryzae and oryzicola, //X. citri// pvs. citri, malvacearum, |
=== In other plant pathogens/ | === In other plant pathogens/ | ||
- | Yes (e.g., // | + | Yes (e.g., // |
===== References ===== | ===== References ===== | ||
- | 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 // |
+ | |||
+ | Furutani A, Takaoka M, Sanada H, Noguchi Y, Oku T, Tsuno K, Ochiai H, Tsuge S (2009). Identification of novel type III secretion effectors in // | ||
- | Liu Y, Long J, Shen D, Song C (2016). // | + | Liu Y, Long J, Shen D, Song C (2016). // |
Mutka AM, Fentress SJ, Sher SW, Berry JC, Pretz C, Nusinow DA, Bart R (2016). Quantitative, | Mutka AM, Fentress SJ, Sher SW, Berry JC, Pretz C, Nusinow DA, Bart R (2016). Quantitative, | ||
- | Qin J, Zhou X, Sun L, Wang K, Yang F, Liao H, Rong W, Yin J, Chen H, Chen X, Zhang J (2018). The // | + | Qin J, Zhou X, Sun L, Wang K, Yang F, Liao H, Rong W, Yin J, Chen H, Chen X, Zhang J (2018). The // |
- | Schulze S, Kay S, Büttner D, Egler M, Eschen-Lippold L, Hause G, Krüger A, Lee J, Müller O, Scheel D, Szczesny R, Thieme F, Bonas U (2012). Analysis of new type III effectors from // | + | Schulze S, Kay S, Büttner D, Egler M, Eschen-Lippold L, Hause G, Krüger A, Lee J, Müller O, Scheel D, Szczesny R, Thieme F, Bonas U (2012). Analysis of new type III effectors from // |
- | Song C, Yang B (2010). Mutagenesis of 18 type III effectors reveals virulence function of XopZ< | + | Song C, Yang B (2010). Mutagenesis of 18 type III effectors reveals virulence function of XopZ< |