bacteria:t3e:xopk
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bacteria:t3e:xopk [2020/07/03 10:14] rkoebnik |
bacteria:t3e:xopk [2020/07/08 19:31] rkoebnik [Biological function] |
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| ====== XopK ====== | ====== XopK ====== | ||
| - | Author: [[https:// | + | Author: [[https:// |
| Internal reviewer: [[https:// | Internal reviewer: [[https:// | ||
| Expert reviewer: FIXME | Expert reviewer: FIXME | ||
| Line 7: | Line 7: | ||
| Class: XopK\\ | Class: XopK\\ | ||
| Family: XopK\\ | Family: XopK\\ | ||
| - | Prototype: | + | Prototype: |
| RefSeq ID: [[https:// | RefSeq ID: [[https:// | ||
| 3D structure: Unknown | 3D structure: Unknown | ||
| 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 ===== | ||
| Line 51: | Line 53: | ||
| 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). // | ||
bacteria/t3e/xopk.txt · Last modified: 2020/12/06 21:56 by rbart_danforthcenter.org
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