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 08-MAR-2011, entry version 55. DE RecName: Full=Elongation factor P; DE Short=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; DOI=10.1002/elps.1150180807; 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). RN [7] RP DISRUPTION PHENOTYPE. RX PubMed=9405429; DOI=10.1074/jbc.272.51.32254; RA Aoki H., Dekany K., Adams S.L., Ganoza M.C.; RT "The gene encoding the elongation factor P protein is essential for RT viability and is required for protein synthesis."; RL J. Biol. Chem. 272:32254-32259(1997). RN [8] RP COPY NUMBER. RX PubMed=7011506; RA An G., Glick B.R., Friesen J.D., Ganoza M.C.; RT "Identification and quantitation of elongation factor EF-P in RT Escherichia coli cell-free extracts."; RL Can. J. Biochem. 58:1312-1314(1980). RN [9] RP PUTATIVE PTM, AND RIBOSOME-BINDING. RX PubMed=18201202; DOI=10.1111/j.1742-4658.2007.06228.x; RA Aoki H., Xu J., Emili A., Chosay J.G., Golshani A., Ganoza M.C.; RT "Interactions of elongation factor EF-P with the Escherichia coli RT ribosome."; RL FEBS J. 275:671-681(2008). CC -!- FUNCTION: Involved in peptide bond synthesis, probably at an early CC stage of protein synthesis. Has stimulatory effects on peptide CC bond formation between ribosome-bound initiator tRNA(fMet) and CC puromycin, and N-acetyl-Phe tRNA(Phe)-primed poly(U)-directed CC poly(Phe) synthesis. CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation. CC -!- SUBUNIT: Binds 30S, 50S and 70S ribosomes, possibly near the A CC site, note that T.thermophilus structures show binding between the CC P and E sites (PDB 3HUW and 3HUY). Proportionally less EF-P binds CC to larger polysomes, suggesting it has a role early in CC translation. It is present in 1 copy per 10 ribosomes. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- PTM: Has been seen to be partially modified on residues 32-34 by CC an unidentified entity with a mass difference of 143.77 Da. CC -!- DISRUPTION PHENOTYPE: Lethality. CC -!- SIMILARITY: Belongs to the elongation factor P family. CC -!- CAUTION: The ptm may be an artifact. 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; AC_000091.1. DR RefSeq; NP_418571.1; NC_000913.2. DR ProteinModelPortal; P0A6N4; -. DR SMR; P0A6N4; 3-187. DR DIP; DIP-31834N; -. DR STRING; P0A6N4; -. DR PRIDE; P0A6N4; -. DR EnsemblBacteria; EBESCT00000001595; EBESCP00000001595; EBESCG00000001316. DR EnsemblBacteria; EBESCT00000016420; EBESCP00000015711; EBESCG00000015480. DR GeneID; 948661; -. DR GenomeReviews; AP009048_GR; JW4107. DR GenomeReviews; U00096_GR; b4147. DR KEGG; ecj:JW4107; -. DR KEGG; eco:b4147; -. DR EchoBASE; EB2023; -. DR EcoGene; EG12099; efp. DR eggNOG; COG0231; -. DR GeneTree; EBGT00050000010829; -. DR HOGENOM; HBG303311; -. DR OMA; DNAECIV; -. DR ProtClustDB; PRK00529; -. DR BioCyc; EcoCyc:EG12099-MONOMER; -. DR Genevestigator; P0A6N4; -. DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc. DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki. DR GO; GO:0043022; F:ribosome binding; IDA:EcoCyc. DR GO; GO:0043022; F:ribosome binding; IDA:EcoliWiki. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. DR HAMAP; MF_00141; EF-P; 1; -. DR InterPro; IPR015365; Elong-fact-P_C. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR016027; NA-bd_OB-fold-like. DR InterPro; IPR020599; Transl_elong_fac_P/YeiP. DR InterPro; IPR013185; Transl_elong_KOW-like. DR InterPro; IPR001059; Transl_elong_P/YeiP_cen. DR InterPro; IPR013852; Transl_elong_P/YeiP_CS. DR InterPro; IPR011768; Transl_elongation_fac_P. DR InterPro; IPR014722; Transl_SH3-like_sub. DR InterPro; IPR008991; Translation_prot_SH3-like. 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 SMART; SM00841; Elong-fact-P_C; 1. DR SUPFAM; SSF50249; Nucleic_acid_OB; 2. DR SUPFAM; SSF50104; Transl_SH3_like; 1. DR TIGRFAMs; TIGR00038; efp; 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. 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 //