Protein Family Models

DltD is and integral membrane protein involved in the biosynthesis of D-alanyl-lipoteichoic acid. This is important in controlling the net ionic charge in lipoteichoic acid (LTA). This family is found in bacteria of the Bacillus/Clostridium group. DltD binds Dcp and ligates it with D-alanine. DltD does not ligate acyl carrier protein (ACP) with D-alanine. It also has thioesterase activity for mischarged D-alanyl-acyl carrier protein (ACP). DltD is thought to be responsible for discriminating between Dcp involved in the D-alanylation of LTA, and ACP involved in fatty acid biosynthesis [1]. [1]. 10781555. Biosynthesis of lipoteichoic acid in Lactobacillus rhamnosus: role of DltD in D-alanylation. Debabov DV, Kiriukhin MY, Neuhaus FC;. J Bacteriol 2000;182:2855-2864. (from Pfam)

Date:

2024-10-16

Members of this protein family are DltD, part of the DltABCD system widely distributed in the Firmicutes for D-alanylation of lipoteichoic acids. The most common form of LTA, as in Staphylococcus aureus, has a backbone of polyglycerolphosphate.

Gene:

dltD

Date:

2021-04-27

D-alanyl-lipoteichoic acid biosynthesis protein DltD is involved in the D-alanylation of lipoteichoic acid

Date:

2019-11-22