bacteria:t3e:xopk
Differences
This shows you the differences between two versions of the page.
| Both sides previous revision Previous revision Next revision | Previous revision Last revision Both sides next revision | ||
|
bacteria:t3e:xopk [2020/07/03 09:49] rkoebnik |
bacteria:t3e:xopk [2020/12/06 21:50] rbart_danforthcenter.org |
||
|---|---|---|---|
| Line 1: | Line 1: | ||
| ====== XopK ====== | ====== XopK ====== | ||
| - | Author: Joël F. Pothier & Trainees from the 2< | + | Author: |
| - | Internal reviewer: Alexandre de Menezes\\ | + | Internal reviewer: |
| - | Expert reviewer: | + | Expert reviewer: |
| Class: XopK\\ | Class: XopK\\ | ||
| Family: XopK\\ | Family: XopK\\ | ||
| - | Prototype: | + | Prototype: |
| RefSeq ID: [[https:// | RefSeq ID: [[https:// | ||
| 3D structure: Unknown | 3D structure: Unknown | ||
| Line 18: | Line 18: | ||
| === (Experimental) evidence for being a T3E === | === (Experimental) evidence for being a T3E === | ||
| - | Mutation of a putative ubiquitin-conjugation enzyme (E2) binding site abolished XopK-induced degradation of rice somatic receptor kinase 2 (OsSERK2) and compromised XopK-dependent virulence (Qin //et al//., 2018). | + | Mutation of a putative ubiquitin-conjugation enzyme (E2) binding site abolished XopK-induced degradation of rice somatic receptor kinase 2 (OsSERK2) and compromised XopK-dependent virulence (Qin //et al//., 2018). Expression of XopK is HrpX-dependent (Furutani //et al//., 2006) and was observed to translocate using a Cya reporter system (Furutani //et al//., 2009). |
| === Regulation === | === Regulation === | ||
| Line 26: | Line 26: | ||
| === 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 // | ||
| - | |||
| - | // | ||
| === 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 === | ||
| XopK interacted with and directly ubiquitinated rice somatic embryogenic receptor kinase 2 (OsSERK2), resulting in its degradation (Qin //et al//., 2018) | XopK interacted with and directly ubiquitinated rice somatic embryogenic receptor kinase 2 (OsSERK2), resulting in its degradation (Qin //et al//., 2018) | ||
| + | |||
| ===== Conservation ===== | ===== Conservation ===== | ||
| === 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; e.g., //X. oryzae// |
| === 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< |
bacteria/t3e/xopk.txt · Last modified: 2020/12/06 21:56 by rbart_danforthcenter.org
Except where otherwise noted, content on this wiki is licensed under the following license: CC Attribution-Share Alike 4.0 International
