LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | The biochemically characterised members of this group are enzymes that transfer organic acids, typically fatty acids, onto hydroxyl groups of membrane-embedded targets. They contain a characteristic domain for O-acyl transferases, , in which a conserved histidine has been suggested to be the active site residue [ ]. These enzymes are multispan membrane proteins involved in the modification of bacterial surface and extracellular polyliposaccharides that play a variety of roles in bacterial survival. Based on sequence similarity this family has been classified into two subgroups:1. DltB ( ): DltB orthologues are present in Gram-positive bacteria. The dlt operon is responsible for D-alanine esterification of both lipoteichoic acid and wall teichoic acid. The dlt operon contains five genes, dltA-dltE; dltB codes for the enzyme that transfers D-alanine to the wall lipotechtoic acids [ ].2. AlgI ( ): AlgI homologues are present mainly in Gram-negative bacteria, though there are a few members from Gram-positive bacteria. The algIgene is often linked to genes for type II membrane proteins that have the conserved amino acid motifs: P[x]K and RTD[x]HW. In Gram-negative bacteria, AlgI is involved in the synthesis of alginate (linear polymer of alpha L-gulunorate and beta-D-mannuronate linked by beta1-4 glycosidic bonds) [ ]. AlgI paralogues in Pseudomonas syringae and Pseudomonas fluorescens are involved in the O-acetylation of cellulose [, ]. In the Gram-positive strain Clostridium acetobutylicum, an algIhomologue is also adjacent to the cellulose biosynthetic genes. |
| Short Name | Ac/AlaTfrase_AlgI/DltB |
