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--- bacteria:t3e:xopae [2025/03/10 10:16] – [Biological function] rkoebnik
+++ bacteria:t3e:xopae [2025/03/10 10:23] (current) – [The Type III Effector XopAE from //Xanthomonas//] rkoebnik
@@ Line 2: / Line 2: @@
 Author: [[https://www.researchgate.net/profile/Guido_Sessa|Guido Sessa]]\\
-Internal reviewer: [[https://www.researchgate.net/profile/David_Studholme|David J. Studholme]]\\
+Internal reviewers: [[https://www.researchgate.net/profile/David_Studholme|David J. Studholme]], [[https://www.researchgate.net/profile/Ralf-Koebnik|Ralf Koebnik]]\\
-Expert reviewer: [[https://www.researchgate.net/profile/Laurent_Noel|Laurent D. Noël]]\\
+Expert reviewer: [[https://www.researchgate.net/profile/Laurent_Noel|Laurent D. Noël]]
 Class: XopAE\\
@@ Line 10: / Line 10: @@
 GenBank ID: [[https://www.ncbi.nlm.nih.gov/protein/AAL78290.1|AAL78290.1]] (197 aa) / [[https://www.ncbi.nlm.nih.gov/protein/AAL78291.1|AAL78291.1]] (432 aa)\\
 RefSeq ID: [[https://www.ncbi.nlm.nih.gov/protein/WP_011050288.1|WP_011050288.1]] (547 aa)\\
-Synonyms: XopAE was also referred to as HpaF (Kim //et al.//, 2003; Sugio //et al.//, 2005). In //Xcv// strain 85-10, the gene is bipartite and the two parts were first coined //hpaF// and //hpaG// (Noël //et al.//, 2002). Be careful: //hpaG// was also used in other Xanthomonas to designate the homolog of //hpa1// (//X. campestris//, //X. oryzae//) and //xopA// (//Xcv// 85-10) (Kim //et al.//, 2003).\\
+Synonyms: XopAE was also referred to as HpaF (Kim //et al.//, 2003; Sugio //et al.//, 2005). In //Xee// strain 85-10, the gene is bipartite and the two parts were first coined //hpaF// and //hpaG// (Noël //et al.//, 2002). Be careful: //hpaG// was also used in other //Xanthomonas// to designate the homolog of //hpa1// (//X. campestris//, //X. oryzae//) and //xopA// (//Xcv// 85-10) (Kim //et al.//, 2003).\\
-D structure: Most XopAE possesses a N-terminal leucine-rich repeat (LRR) domain and a C-terminal XL box motif with an E3 ubiquitin ligase fold, based on homology modelling (Popov //et al//., 2018). Predicted fold of XopAE C terminus is similar to that of XopL (Popov //et al//., 2018).
+D structure: Most XopAE possesses a N-terminal leucine-rich repeat (LRR) domain and a C-terminal XL box motif with an E3 ubiquitin ligase fold, based on homology modelling (Popov //et al.//., 2018). Predicted fold of XopAE C terminus is similar to that of XopL (Popov //et al.//, 2018).
 ===== The locus =====

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