Protein Family Models

elongation factor P (EF-P) is an essential protein that stimulates ribosomal peptidyltransferase activity

Date:

2024-02-09

Members of this family of nucleic acid binding domains are predominantly found in elongation factor P, where they adopt an OB-fold, with five beta-strands forming a beta-barrel in a Greek-key topology [1]. [1]. 15210970. Crystal structure of elongation factor P from Thermus thermophilus HB8. Hanawa-Suetsugu K, Sekine S, Sakai H, Hori-Takemoto C, Terada T, Unzai S, Tame JR, Kuramitsu S, Shirouzu M, Yokoyama S;. Proc Natl Acad Sci U S A. 2004;101:9595-9600. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

Date:

2024-08-14

Involved in peptide bond synthesis; alters the affinity of the ribosome for aminoacyl-tRNA

Date:

2020-10-26

Elongation factor P (EF-P) alleviates stalling of protein translation at polyproline sites. EF-P (and its archaeal and eukaryotic homologs) are post-translationally modified, on a critical lysine or arginine residue, in different ways in different lineages. Residues are modified with beta-lysine, rhamnose, 5-aminopentanol, or hypusine. The trusted cutoff of this model is set high enough to exclude members of TIGR02178, the EFP-like protein YeiP found in certain Gammaproteobacteria.

Gene:

efp

Date:

2024-08-05