ID EFP_ECOLI STANDARD; PRT; 187 AA. AC P0A6N4; P33398; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 10-MAY-2005 (Rel. 47, Last annotation update) DE Elongation factor P (EF-P). GN Name=efp; OrderedLocusNames=b4147; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 1-32; 70-79 AND 85-116. RX MEDLINE=92066471; PubMed=1956781; 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. RC STRAIN=K12 / MG1655; RX MEDLINE=95334362; PubMed=7610040; 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; 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 PROTEIN SEQUENCE OF 1-12. 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 [5] 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. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. 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 PIR; S34443; S34443. DR EchoBASE; EB2023; -. DR EcoGene; EG12099; efp. DR HAMAP; MF_00141; -; 1. DR Pfam; PF01132; EFP; 1. DR PIRSF; PIRSF005901; EF-P; 1. DR PROSITE; PS01275; EFP; 1. KW Complete proteome; Direct protein sequencing; Elongation factor; KW Protein biosynthesis. FT INIT_MET 0 0 FT CONFLICT 80 80 F -> P (in Ref. 1). SQ SEQUENCE 187 AA; 20460 MW; 1C9E75B6FEB2D0D4 CRC64; ATYYSNDFRA GLKIMLDGEP YAVEASEFVK PGKGQAFARV KLRRLLTGTR VEKTFKSTDS AEGADVVDMN LTYLYNDGEF WHFMNNETFE QLSADAKAIG DNAKWLLDQA ECIVTLWNGQ PISVTPPNFV ELEIVDTDPG LKGDTAGTGG KPATLSTGAV VKVPLFVQIG EVIKVDTRSG EYVSRVK //