wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.
Comment:Based on the structures of E. coli galactoside acetyltransferase and Enterococcus faecium streptogramin acetyltransferase Vat(D) bound to CoA and their respective substrates.
Comment:Active acetyltransferases in this family are trimeric, with active sites located at the interface between two LbH subunits. The trimer structure contains three active sites and each subunit contributes to two active sites via residues located on two surfaces.
Jiyao W et al.(2023). "The conserved domain database in 2023.",