ID EFP_ECOLI Reviewed; 188 AA. AC P0A6N4; P33398; Q2M6F7; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-OCT-2007, entry version 29. DE Elongation factor P (EF-P). GN Name=efp; OrderedLocusNames=b4147, JW4107; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-33; 71-80 RP AND 86-117. RX MEDLINE=92066471; PubMed=1956781; DOI=10.1093/nar/19.22.6215; RA Aoki H., Adams S.-L., Chung D.-G., Yaguchi M., Chuang S.-E., RA Ganoza M.C.; RT "Cloning, sequencing and overexpression of the gene for prokaryotic RT factor EF-P involved in peptide bond synthesis."; RL Nucleic Acids Res. 19:6215-6220(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=95334362; PubMed=7610040; DOI=10.1093/nar/23.12.2105; RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., RA Blattner F.R.; RT "Analysis of the Escherichia coli genome VI: DNA sequence of the RT region from 92.8 through 100 minutes."; RL Nucleic Acids Res. 23:2105-2119(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP PROTEIN SEQUENCE OF 2-13. RC STRAIN=K12 / EMG2; RX MEDLINE=97443975; PubMed=9298646; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded RT in the genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [6] RP CHARACTERIZATION. RX MEDLINE=97338480; PubMed=9195040; DOI=10.1016/S0300-9084(97)87619-5; RA Aoki H., Adams S.-L., Turner M.A., Ganoza M.C.; RT "Molecular characterization of the prokaryotic efp gene product RT involved in a peptidyltransferase reaction."; RL Biochimie 79:7-11(1997). CC -!- FUNCTION: Involved in peptide bond synthesis. Stimulates efficient CC translation and peptide-bond synthesis on native or reconstituted CC 70S ribosomes in vitro. Probably functions indirectly by altering CC the affinity of the ribosome for aminoacyl-tRNA, thus increasing CC their reactivity as acceptors for peptidyl transferase. CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the elongation factor P family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X61676; CAA43851.1; -; Genomic_DNA. DR EMBL; U14003; AAA97046.1; -; Genomic_DNA. DR EMBL; U00096; AAC77107.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78149.1; -; Genomic_DNA. DR PIR; S34443; S34443. DR RefSeq; AP_004648.1; -. DR RefSeq; NP_418571.1; -. DR IntAct; P0A6N4; -. DR GeneID; 948661; -. DR GenomeReviews; U00096_GR; b4147. DR GenomeReviews; AP009048_GR; JW4107. DR KEGG; ecj:JW4107; -. DR KEGG; eco:b4147; -. DR EchoBASE; EB2023; -. DR EcoGene; EG12099; efp. DR BioCyc; EcoCyc:EG12099-MONOMER; -. DR GO; GO:0003746; F:translation elongation factor activity; IEA:HAMAP. DR GO; GO:0006414; P:translational elongation; IEA:HAMAP. DR HAMAP; MF_00141; -; 1. DR InterPro; IPR015365; Elong-fact-P_C. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR011768; Transl_elong_EFP. DR InterPro; IPR013185; Transl_elong_KOW-like. DR InterPro; IPR013852; Transl_elong_P/YeiP_C. DR InterPro; IPR001059; Transl_elong_P/YeiP_cen. DR InterPro; IPR014722; Transl_SH3_like_sub. DR Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 2. DR Gene3D; G3DSA:2.30.30.30; Ribosomal_L2; 1. DR Pfam; PF01132; EFP; 1. DR Pfam; PF08207; EFP_N; 1. DR Pfam; PF09285; Elong-fact-P_C; 1. DR PIRSF; PIRSF005901; EF-P; 1. DR PROSITE; PS01275; EFP; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Direct protein sequencing; KW Elongation factor; Protein biosynthesis. FT INIT_MET 1 1 Removed. FT CHAIN 2 188 Elongation factor P. FT /FTId=PRO_0000094245. FT CONFLICT 81 81 F -> P (in Ref. 1). SQ SEQUENCE 188 AA; 20591 MW; E36E136D4399460F CRC64; MATYYSNDFR AGLKIMLDGE PYAVEASEFV KPGKGQAFAR VKLRRLLTGT RVEKTFKSTD SAEGADVVDM NLTYLYNDGE FWHFMNNETF EQLSADAKAI GDNAKWLLDQ AECIVTLWNG QPISVTPPNF VELEIVDTDP GLKGDTAGTG GKPATLSTGA VVKVPLFVQI GEVIKVDTRS GEYVSRVK //