AC   MF_00646;
DC   Protein; auto
TR   HAMAP; MF_00646; -; 1; level=0
XX
Names: EFPL
XX
ID   EFPL
DE   RecName: Full=Elongation factor protein EfpL;
GN   Name=efpL;
XX
CC   -!- FUNCTION: Involved in peptide bond synthesis. Alleviates ribosome
CC       stalling at di-proline-containing sequences; in rare cases stalled
CC       nascent peptides lacking di-Pro can also be rescued.
CC   -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
case <OC:Enterobacteriaceae> and <FTTag:acetyl>
CC   -!- PTM: Acetylation of #{Lys-51} inactivates rescue of stalled ribosomes.
end case
CC   -!- SIMILARITY: Belongs to the elongation factor P family. EfpL subfamily.
XX
DR   Pfam; PF01132; EFP; 1; trigger=no
DR   Pfam; PF08207; EFP_N; 1; trigger=no
DR   Pfam; PF09285; Elong-fact-P_C; 1; trigger=no
DR   NCBIfam; NF001810; PRK00529.1; 0-1; trigger=no
DR   NCBIfam; NF003392; PRK04542.1; 1; trigger=no
DR   NCBIfam; TIGR02178; yeiP; 0-1; trigger=no
DR   PROSITE; PS01275; EFP; 1; trigger=no
XX
KW   Cytoplasm
KW   Protein biosynthesis
KW   Elongation factor
KW   tRNA-binding
KW   RNA-binding
case <OC:Enterobacteriaceae> and <FTTag:acetyl>
KW   Acetylation
end case
XX
GO   GO:0072344; P:rescue of stalled ribosome
GO   GO:0003746; F:translation elongation factor activity
GO   GO:0006414; P:translational elongation
GO   GO:0005737; C:cytoplasm
XX
FT   From: EFPL_ECOLI (P0A6N8)
FT   SITE            33
FT                   /note="Probably interacts with 3' end of the P-site tRNA"
FT   Condition: R
case <OC:Enterobacteriaceae>
FT   MOD_RES         51
FT                   /note="N6-acetyllysine"
FT   Tag: acetyl; Optional; Condition: K
end case
XX
Size: 170-210;
Related: MF_00141;
Template: P0A6N8;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Version: 14
# Last updated date: 2025-07-25
# Created date: 2005-02-28
//