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bacteria:t3e:xopah [2025/01/29 23:11] – [Biological function] jfpothier | bacteria:t3e:xopah [2025/02/21 11:35] (current) – [Conservation] rkoebnik | ||
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AvrXccC was described during a genome comparison analysis between // | AvrXccC was described during a genome comparison analysis between // | ||
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=== (Experimental) evidence for being a T3E === | === (Experimental) evidence for being a T3E === | ||
Secreted XopAH (AvrXccC) proteins were detected in culture fluid from //Xcc// 8004 and //hrcV// mutant complemented strains but not from the //hrcV// mutant (Wang //et al//., 2007). Insertion and deletion mutants affecting the locus (Xcc2109) in the type strain (Xcc 528) resulted in loss of virulence on the host Florida Broad Leaf Mustard (Castañeda //et al//., 2005). | Secreted XopAH (AvrXccC) proteins were detected in culture fluid from //Xcc// 8004 and //hrcV// mutant complemented strains but not from the //hrcV// mutant (Wang //et al//., 2007). Insertion and deletion mutants affecting the locus (Xcc2109) in the type strain (Xcc 528) resulted in loss of virulence on the host Florida Broad Leaf Mustard (Castañeda //et al//., 2005). | ||
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=== Regulation === | === Regulation === | ||
Promoter activity assays showed that the expression of XopAH (// | Promoter activity assays showed that the expression of XopAH (// | ||
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=== Phenotypes === | === Phenotypes === | ||
- | This effector is required for full virulence in the susceptible host cabbage (//Brassica oleracea//) (Wang //et al//., 2007) and results in avirulence in the resistant host mustard (//Brassica napiformis// | + | This effector is required for full virulence in the susceptible host cabbage (//Brassica oleracea//) (Wang //et al//., 2007) and results in avirulence in the resistant host mustard (//Brassica napiformis// |
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- | In the interaction // | + | |
+ | In the interaction // | ||
=== Localization === | === Localization === | ||
- | XopAH (AvrXccC) is anchored to the plant plasma membrane, and the N‐terminal myristoylation site (amino acids 2–7: GLcaSK) is essential for its localization (Wang //et al//., 2007). | + | XopAH (AvrXccC) is anchored to the plant plasma membrane, and the N‐terminal myristoylation site (amino acids 2–7: GLcaSK) is essential for its localization (Wang //et al.//, 2007). |
=== Enzymatic function === | === Enzymatic function === | ||
- | XopAH has a Fido/AvrB domain derived from the fic (cyclic adenosine monophosphate (cAMP)-induced filamentation and doc (death on curing) domains (Kinch //et al//., 2009). Structural comparisons resulted in the inclusion of similar segments of the T3 effector AvrB from // | + | XopAH has a Fido/AvrB domain derived from the fic (cyclic adenosine monophosphate (cAMP)-induced filamentation and doc (death on curing) domains (Kinch //et al//., 2009). Structural comparisons resulted in the inclusion of similar segments of the T3 effector AvrB from // |
=== Interaction partners === | === Interaction partners === | ||
- | Not known ? | + | Not known. |
===== Conservation ===== | ===== Conservation ===== | ||
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=== In xanthomonads === | === In xanthomonads === | ||
- | In // | + | In // |
=== In other plant pathogens/ | === In other plant pathogens/ | ||
Yes (AvrB // | Yes (AvrB // | ||
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===== References ===== | ===== References ===== | ||