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T6SS, Phospholipase effector Tle1-like, C-terminal domain
This domain is found in the type VI secretion system (T6SS) Phospholipase effector Tle1 from Pseudomonas aeruginosa (Swiss:Q9HYV3), which hydrolyse membrane phospholipids. Tle1 is organised into two distinct parts, the phospholipase catalytic module (Pfam:PF09994) and the putative membrane-anchoring module (this entry), that can be divided into three independent domains: a three-helix bundle, a six-helix bundle and an alpha/beta mixed fold with a two-layer sandwich structure [1]. Paper describing PDB structure 4o5p. [1]. 25084336. Structure of the type VI secretion phospholipase effector Tle1 provides insight into its hydrolysis and membrane targeting. Hu H, Zhang H, Gao Z, Wang D, Liu G, Xu J, Lan K, Dong Y;. Acta Crystallogr D Biol Crystallogr. 2014;70:2175-2185. (from Pfam)
phospholipase effector Tle1 domain-containing protein
This domain, found in various hypothetical bacterial proteins, has no known function. This domain is found in the type VI secretion system (T6SS) Phospholipase effector Tle1 from Pseudomonas aeruginosa (Swiss:Q9HYV3), which hydrolyse membrane phospholipids. Tle1 is organised into two distinct parts, the phospholipase catalytic module (this entry) and the putative membrane-anchoring module (Pfam:PF22137). This domain adopts a compact conformation with a classical mixed alpha/beta-hydrolase fold that shows of seven central parallel beta-sheets and 13 alpha-helices [1]. [1]. 25084336. Structure of the type VI secretion phospholipase effector Tle1 provides insight into its hydrolysis and membrane targeting. Hu H, Zhang H, Gao Z, Wang D, Liu G, Xu J, Lan K, Dong Y;. Acta Crystallogr D Biol Crystallogr. 2014;70:2175-2185. (from Pfam)
DUF2235 and Aldose_epim domain-containing protein
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