InterPro : IPR006297

Name  Elongation factor 4 Short Name  EF-4
Type  Family Description  Elongation factor 4, also known as ribosomal back-translocase LepA, is required for accurate and efficient protein synthesis under certain stress conditions. It may act as a fidelity factor of the translation reaction, by catalysing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly [, ]. Elongation factor 4 binds to ribosomes in a GTP-dependent manner.The eukaryotic homologue is known as GUF1 and promotes protein synthesis in chloroplasts and mitochondria [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



1 Child Features

Id Name Short Name Type
IPR027518 Translation factor GUF1 homologue, organellar chromatophore GUFP Family

6 Contains

Id Name Short Name Type
IPR009022 Elongation factor G, III-V domain EFG_III-V Domain
IPR000640 Translation elongation factor EFG, V domain EFG_V Domain
IPR009000 Translation protein, beta-barrel domain Transl_B-barrel Domain
IPR004161 Translation elongation factor EFTu/EF1A, domain 2 Transl_elong_EFTu/EF1A_2 Domain
IPR000795 Elongation factor, GTP-binding domain EF_GTP-bd_dom Domain
IPR013842 GTP-binding protein LepA, C-terminal LepA_GTP-bd_C Domain

0 Found In

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Qin Y The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome. 2006 Cell 127 721-33
Liu H Interrupted catalysis: the EF4 (LepA) effect on back-translocation. 2010 J Mol Biol 396 1043-52
Bauerschmitt H The membrane-bound GTPase Guf1 promotes mitochondrial protein synthesis under suboptimal conditions. 2008 J Biol Chem 283 17139-46

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)