Bioinformatics analysis reveals that LepA C-terminal domain is highly conserved in domain architectures and phylogenetic distribution

Abstract

LepA is a ribosomal elongation factor that catalyzes back-translocation of the ribosome during elongation cycle. LepA has a highly conserved and structural independent carboxyl terminal domain (LepA_CTD), but the structural and functional information of this domain remains elusive. Here, we collected all the LepA_CTD concerning information from protein databanks and found that: (1) LepA_CTD always coexists with the four LepA N-terminal domains, thus it is conserved in domain architectures; (2) LepA is conserved in almost all bacteria and eukaryote, but absent in archaea; (3) the C-terminal part of LepA_CTD has highly conserved and positively charged motifs could be responsible for its back-translocase function.