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 28-MAR-2018, entry version 110. 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; Enterobacterales; 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 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 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 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 277:1453-1462(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 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 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 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). RN [10] RP BETA-LYSYLATION AT LYS-34 BY EPMA. RC STRAIN=K12; RX PubMed=21841797; DOI=10.1038/nchembio.632; RA Roy H., Zou S.B., Bullwinkle T.J., Wolfe B.S., Gilreath M.S., RA Forsyth C.J., Navarre W.W., Ibba M.; RT "The tRNA synthetase paralog PoxA modifies elongation factor-P with RT (R)-beta-lysine."; RL Nat. Chem. Biol. 7:667-669(2011). RN [11] RP BETA-LYSYLATION AT LYS-34 BY EPMA AND EPMB, AND MUTAGENESIS OF LYS-34. RC STRAIN=K12 / MG1655 / ATCC 47076, and MRE-600; RX PubMed=22128152; DOI=10.1074/jbc.M111.309633; RA Park J.H., Johansson H.E., Aoki H., Huang B.X., Kim H.Y., Ganoza M.C., RA Park M.H.; RT "Post-translational modification by beta-lysylation is required for RT activity of Escherichia coli elongation factor P (EF-P)."; RL J. Biol. Chem. 287:2579-2590(2012). RN [12] RP BETA-LYSYLATION AT LYS-34 BY EPMC, AND MASS SPECTROMETRY. RC STRAIN=K12 / AT713, K12 / BW25113, RC K12 / MC4100 / ATCC 35695 / DSM 6574, and MRE-600; RX PubMed=22706199; DOI=10.1038/nchembio.1001; RA Peil L., Starosta A.L., Virumae K., Atkinson G.C., Tenson T., RA Remme J., Wilson D.N.; RT "Lys34 of translation elongation factor EF-P is hydroxylated by RT YfcM."; RL Nat. Chem. Biol. 8:695-697(2012). RN [13] RP FUNCTION IN POLY-PRO TRANSLATION, DISRUPTION PHENOTYPE, AND RP MUTAGENESIS OF LYS-34. RC STRAIN=K12 / BW25113, and K12 / MG1655 / ATCC 47076; RX PubMed=23239623; DOI=10.1126/science.1228985; RA Ude S., Lassak J., Starosta A.L., Kraxenberger T., Wilson D.N., RA Jung K.; RT "Translation elongation factor EF-P alleviates ribosome stalling at RT polyproline stretches."; RL Science 339:82-85(2013). RN [14] RP FUNCTION IN TRANSLATION, AND PTM. RC STRAIN=B / BL21-DE3, and MRE-600; RX PubMed=23239624; DOI=10.1126/science.1229017; RA Doerfel L.K., Wohlgemuth I., Kothe C., Peske F., Urlaub H., RA Rodnina M.V.; RT "EF-P is essential for rapid synthesis of proteins containing RT consecutive proline residues."; RL Science 339:85-88(2013). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH LYSYL-ADENYLATE RP ANALOG AND EMPA, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-31; RP GLY-33 AND LYS-34. RC STRAIN=K12 / BW25113, and K12 / MC4100 / ATCC 35695 / DSM 6574; RX PubMed=20729861; DOI=10.1038/nsmb.1889; RA Yanagisawa T., Sumida T., Ishii R., Takemoto C., Yokoyama S.; RT "A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine RT residue in translation elongation factor P."; RL Nat. Struct. Mol. Biol. 17:1136-1143(2010). CC -!- FUNCTION: Involved in peptide bond synthesis. Alleviates ribosome CC stalling that occurs when 3 or more consecutive Pro residues or CC the sequence PPG is present in a protein, possibly by augmenting CC the peptidyl transferase activity of the ribosome. Beta-lysylation CC at Lys-34 is required for alleviation. The Pro codons and their CC context do not affect activity; only consecutive Pro residues (not CC another amino acid) are affected by EF-P. Has stimulatory effects CC on peptide bond formation between ribosome-bound initiator CC tRNA(fMet) and puromycin, and N-acetyl-Phe tRNA(Phe)-primed CC poly(U)-directed poly(Phe) synthesis. CC {ECO:0000269|PubMed:23239623, ECO:0000269|PubMed:23239624}. 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 {ECO:0000269|PubMed:20729861}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- PTM: Is beta-lysylated on the epsilon-amino group of Lys-34 by the CC combined action of EpmA and EpmB, and then hydroxylated on the C5 CC position of the same residue by EpmC. Lysylation is critical for CC the stimulatory effect of EF-P on peptide-bond formation. The CC lysylation moiety would extend toward the peptidyltransferase CC center and stabilize the terminal 3-CCA end of the tRNA. The CC hydroxylation of the C5 position on Lys-34 would allow additional CC potential stabilizing hydrogen-bond interactions with the P-tRNA CC (PubMed:21841797 PubMed:22128152 PubMed:22706199 and CC PubMed:20729861). {ECO:0000269|PubMed:21841797, CC ECO:0000269|PubMed:22128152, ECO:0000269|PubMed:22706199}. CC -!- MASS SPECTROMETRY: Mass=20591.6; Method=Electrospray; Range=2-188; CC Note=With N6-(3,6-diaminohexanoyl)-5-hydroxy-Lys-34.; CC Evidence={ECO:0000269|PubMed:22706199}; CC -!- DISRUPTION PHENOTYPE: Disruption of this gene leads to lethality CC (PubMed:9405429) or to a very slow growth phenotype CC (PubMed:20729861). Required for the expression of poly-Pro- CC containing proteins. {ECO:0000269|PubMed:20729861, CC ECO:0000269|PubMed:23239623, ECO:0000269|PubMed:9405429}. CC -!- SIMILARITY: Belongs to the elongation factor P family. CC {ECO:0000305}. CC -!- CAUTION: The modification on Lys-34 was initially thought to be a CC spermidine residue. {ECO:0000305|PubMed:18201202}. 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; NP_418571.1; NC_000913.3. DR RefSeq; WP_000257278.1; NZ_LN832404.1. DR PDB; 3A5Z; X-ray; 2.50 A; B/D/F/H=1-188. DR PDB; 6ENJ; EM; 3.70 A; w=1-188. DR PDB; 6ENU; EM; 3.10 A; w=1-188. DR PDBsum; 3A5Z; -. DR PDBsum; 6ENJ; -. DR PDBsum; 6ENU; -. DR ProteinModelPortal; P0A6N4; -. DR SMR; P0A6N4; -. DR BioGrid; 4260776; 791. DR DIP; DIP-31834N; -. DR IntAct; P0A6N4; 1. DR STRING; 316385.ECDH10B_4340; -. DR EPD; P0A6N4; -. DR PaxDb; P0A6N4; -. DR PRIDE; P0A6N4; -. DR EnsemblBacteria; AAC77107; AAC77107; b4147. DR EnsemblBacteria; BAE78149; BAE78149; BAE78149. DR GeneID; 948661; -. DR KEGG; ecj:JW4107; -. DR KEGG; eco:b4147; -. DR PATRIC; fig|1411691.4.peg.2553; -. DR EchoBASE; EB2023; -. DR EcoGene; EG12099; efp. DR eggNOG; ENOG4105DRH; Bacteria. DR eggNOG; COG0231; LUCA. DR HOGENOM; HOG000010047; -. DR InParanoid; P0A6N4; -. DR KO; K02356; -. DR OMA; NTFSAGH; -. DR PhylomeDB; P0A6N4; -. DR BioCyc; EcoCyc:EG12099-MONOMER; -. DR BioCyc; MetaCyc:EG12099-MONOMER; -. DR UniPathway; UPA00345; -. DR PRO; PR:P0A6N4; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0043022; F:ribosome binding; IDA:EcoCyc. DR GO; GO:0003746; F:translation elongation factor activity; IDA:EcoCyc. DR GO; GO:2001125; P:negative regulation of translational frameshifting; IMP:EcoCyc. DR GO; GO:0072344; P:rescue of stalled ribosome; IMP:EcoCyc. DR GO; GO:0006414; P:translational elongation; IDA:EcoCyc. DR CDD; cd04470; S1_EF-P_repeat_1; 1. DR CDD; cd05794; S1_EF-P_repeat_2; 1. DR Gene3D; 2.30.30.30; -; 1. DR HAMAP; MF_00141; EF_P; 1. DR InterPro; IPR015365; Elong-fact-P_C. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR014722; Rib_L2_dom2. 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; IPR008991; Translation_prot_SH3-like_sf. DR PANTHER; PTHR30053; PTHR30053; 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; SM01185; EFP; 1. DR SMART; SM00841; Elong-fact-P_C; 1. DR SUPFAM; SSF50104; SSF50104; 1. DR SUPFAM; SSF50249; SSF50249; 2. DR TIGRFAMs; TIGR00038; efp; 1. DR PROSITE; PS01275; EFP; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; KW Elongation factor; Hydroxylation; Protein biosynthesis; KW Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1956781, FT ECO:0000269|PubMed:9298646}. FT CHAIN 2 188 Elongation factor P. FT /FTId=PRO_0000094245. FT MOD_RES 34 34 N6-(3,6-diaminohexanoyl)-5-hydroxylysine. FT {ECO:0000269|PubMed:21841797, FT ECO:0000269|PubMed:22128152, FT ECO:0000269|PubMed:22706199}. FT MUTAGEN 31 31 K->A: No lysylation. FT {ECO:0000269|PubMed:20729861}. FT MUTAGEN 33 33 G->K: No lysylation. Loss of in vivo EF-P FT function for cell growth. FT {ECO:0000269|PubMed:20729861}. FT MUTAGEN 34 34 K->A: No lysylation and loss of EF-P FT activity. No facilitation of translation FT of poly-Pro stretches. FT {ECO:0000269|PubMed:20729861, FT ECO:0000269|PubMed:22128152, FT ECO:0000269|PubMed:23239623}. FT STRAND 4 6 {ECO:0000244|PDB:3A5Z}. FT STRAND 14 17 {ECO:0000244|PDB:3A5Z}. FT STRAND 20 30 {ECO:0000244|PDB:3A5Z}. FT STRAND 38 45 {ECO:0000244|PDB:3A5Z}. FT HELIX 46 48 {ECO:0000244|PDB:3A5Z}. FT STRAND 51 57 {ECO:0000244|PDB:3A5Z}. FT STRAND 61 64 {ECO:0000244|PDB:3A5Z}. FT STRAND 67 70 {ECO:0000244|PDB:3A5Z}. FT STRAND 73 77 {ECO:0000244|PDB:3A5Z}. FT STRAND 82 85 {ECO:0000244|PDB:3A5Z}. FT TURN 87 89 {ECO:0000244|PDB:3A5Z}. FT STRAND 92 95 {ECO:0000244|PDB:3A5Z}. FT HELIX 97 100 {ECO:0000244|PDB:3A5Z}. FT TURN 102 106 {ECO:0000244|PDB:3A5Z}. FT STRAND 109 112 {ECO:0000244|PDB:3A5Z}. FT STRAND 114 118 {ECO:0000244|PDB:3A5Z}. FT STRAND 121 126 {ECO:0000244|PDB:3A5Z}. FT STRAND 152 156 {ECO:0000244|PDB:3A5Z}. FT STRAND 161 164 {ECO:0000244|PDB:3A5Z}. FT STRAND 173 177 {ECO:0000244|PDB:3A5Z}. FT TURN 178 181 {ECO:0000244|PDB:3A5Z}. FT STRAND 182 186 {ECO:0000244|PDB:3A5Z}. 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 //