This shows you the differences between two versions of the page.
Both sides previous revision Previous revision Next revision | Previous revision Next revision Both sides next revision | ||
bacteria:t3e:xopk [2020/07/02 16:14] rkoebnik [References] |
bacteria:t3e:xopk [2020/07/08 19:31] rkoebnik [Biological function] |
||
---|---|---|---|
Line 1: | Line 1: | ||
====== XopK ====== | ====== XopK ====== | ||
- | Author: | + | Author: |
- | Internal reviewer: Alexandre de Menezes\\ | + | Internal reviewer: |
Expert reviewer: FIXME | Expert reviewer: FIXME | ||
Class: XopK\\ | Class: XopK\\ | ||
Family: XopK\\ | Family: XopK\\ | ||
- | Prototype: | + | Prototype: |
RefSeq ID: [[https:// | RefSeq ID: [[https:// | ||
3D structure: Unknown | 3D structure: Unknown | ||
Line 23: | Line 23: | ||
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// |
+ | * A ∆// | ||
+ | * XopK inhibits pathogen-associated molecular pattern-triggered immunity upstream of mitogen-activated protein kinase cascades (Qin //et al.//, 2018) | ||
- | 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) | ||
=== 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 === | ||
Line 50: | 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). // |