v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | This entry represents D-alanyl carrier protein DltC, which is part of the operon for incorporation of D-Ala residues into lipoteichoic acids (LTAs), which requires the activity of four gene products (DltA to DltD). DltA is a cytoplasmic D-alanine-D-alanyl carrier protein ligase that catalyses the D-alanylation of the D-alanyl carrier protein DltC (or Dcp); DltB is a transmembrane protein thought to be involved in the efflux of activated D-alanine to the site of acylation; and DltD is thought to be a membrane-associated protein that may have multifunctional activities (hydrolysis of mischarged DltC, facilitation of D-alanine ligation to DltC and D-alanylation of LTAs) [ , ].These proteins are involved in the biosynthesis of D-alanyl-lipoteichoic acid in bacteria. They are major wall and membrane components of most Gram-positive bacteria [ ]. Streptococcus pneumoniae is one of the few species of low-G and C Gram-positive bacteria that do not contain d-alanine in teichoic acids []. d-alanine residues are thought to protect this human pathogen against the actions of cationic antimicrobial peptides. Mammals use antimicrobial peptides to protect themselves from invasive infectious agents such as Group A streptococcus (GAS), which causes necrotising fasciitis and toxic shock syndrome []. Teichoic acids and D-alanylation of teichoic acids are required for colony spreading in Staphylococcus aureus []. |
| Short Name | DltC |