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20  structures 7374  species 0  interactions 9379  sequences 22  architectures

Family: Elong-fact-P_C (PF09285)

Summary: Elongation factor P, C-terminal

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This is the Wikipedia entry entitled "Elongation factor P". More...

Elongation factor P Edit Wikipedia article

Elongation factor P (EF-P) KOW-like domain
PDB 1iz6 EBI.jpg
crystal structure of translation initiation factor 5a from pyrococcus horikoshii
Pfam clanCL0107
Elongation factor P (EF-P) OB domain
PDB 1ueb EBI.jpg
crystal structure of translation elongation factor p from thermus thermophilus hb8
Pfam clanCL0021
Elongation factor P, C-terminal
PDB 1ueb EBI.jpg
crystal structure of translation elongation factor p from thermus thermophilus hb8

EF-P (elongation factor P) is a prokaryotic protein translation factor required for efficient peptide bond synthesis on 70S ribosomes from fMet-tRNAfMet.[1] It probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.

EF-P consists of three domains:

  • An N-terminal KOW-like domain
  • A central OB domain, which forms an oligonucleotide-binding fold. It is not clear if this region is involved in binding nucleic acids[2]
  • A C-terminal domain which adopts an OB-fold, with five beta-strands forming a beta-barrel in a Greek-key topology[2]

eIF5A is the eukaryotic homolog of EF-P.


It has been suggested that after binding of the initiator tRNA to the P/I site, it is correctly positioned to the P site by binding of EF-P to the E site.[3] Additionally, EF-P has been shown to assist in efficient translation of three or more consecutive proline residues.[4]

See also


  1. ^ Aoki H, Adams SL, Turner MA, Ganoza MC (1997). "Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reaction". Biochimie. 79 (1): 7–11. doi:10.1016/S0300-9084(97)87619-5. PMID 9195040.
  2. ^ a b Hanawa-Suetsugu K, Sekine S, Sakai H, Hori-Takemoto C, Terada T, Unzai S, Tame JR, Kuramitsu S, Shirouzu M, Yokoyama S (June 2004). "Crystal structure of elongation factor P from Thermus thermophilus HB8". Proc. Natl. Acad. Sci. U.S.A. 101 (26): 9595–600. Bibcode:2004PNAS..101.9595H. doi:10.1073/pnas.0308667101. PMC 470720. PMID 15210970.
  3. ^ Leaps in Translational Elongation Science (2009) 326, 677.
  4. ^ Ude, Susanne; Lassak, Jürgen; Starosta, Agata L.; Kraxenberger, Tobias; Wilson, Daniel N.; Jung, Kirsten (2013-01-04). "Translation Elongation Factor EF-P Alleviates Ribosome Stalling at Polyproline Stretches". Science. 339 (6115): 82–85. Bibcode:2013Sci...339...82U. doi:10.1126/science.1228985. ISSN 0036-8075. PMID 23239623.
This article incorporates text from the public domain Pfam and InterPro: IPR001059
This article incorporates text from the public domain Pfam and InterPro: IPR015365

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Elongation factor P, C-terminal Provide feedback

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].

Literature references

  1. 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.: Crystal structure of elongation factor P from Thermus thermophilus HB8. PUBMED:15210970 EPMC:15210970

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR015365

Elongation factor P (EF-P) stimulates the peptidyltransferase activity in the prokaryotic 70S ribosome. EF-P enhances the synthesis of certain dipeptides with N-formylmethionyl-tRNA and puromycine in vitro. EF-P binds to both the 30S and 50S ribosomal subunits. EF-P binds near the streptomycine binding site of the 16S rRNA in the 30S subunit. EF-P interacts with domains 2 and 5 of the 23S rRNA. The L16 ribosomal protein of the 50S or its N-terminal fragment are required for EF-P mediated peptide bond synthesis, whereas L11, L15, and L7/L12 are not required in this reaction, suggesting that EF-P may function at a different ribosomal site than most other translation factors. EF-P is essential for cell viability and is required for protein synthesis [ PUBMED:9405429 , PUBMED:16928980 , PUBMED:15922593 , PUBMED:12932732 ]. EF-P is mainly present in bacteria. The EF-P homologs in archaea and eukaryotes are the initiation factors aIF5A and eIF5A, respectively. EF-P has 3 domains (domains I, II, and III). Domains II and III are S1-like domains. This entry includes domain III (the second S1 domain of EF_P). Domains II and III of have structural homology to the eIF5A domain C, suggesting that domains II and III evolved by duplication. These domains adopt an OB-fold, with five beta-strands forming a beta-barrel in a Greek-key topology [ PUBMED:15210970 ].

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Seed source: pdb_1ueb
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Sammut SJ
Number in seed: 372
Number in full: 9379
Average length of the domain: 56.00 aa
Average identity of full alignment: 48 %
Average coverage of the sequence by the domain: 29.42 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 25.0 25.6
Noise cut-off 24.8 24.9
Model length: 56
Family (HMM) version: 14
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Elong-fact-P_C domain has been found. There are 20 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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