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 12-OCT-2022, entry version 132. 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 AND RP 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., Ganoza M.C.; RT "Cloning, sequencing and overexpression of the gene for prokaryotic factor RT 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., Blattner F.R.; RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region RT 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., Mau B., RA 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 MG1655 RT 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 in the RT 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 involved in RT 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; DOI=10.1139/o80-177; RA An G., Glick B.R., Friesen J.D., Ganoza M.C.; RT "Identification and quantitation of elongation factor EF-P in Escherichia RT 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, AND HYDROXYLATION AT LYS-34. 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., Forsyth C.J., RA Navarre W.W., Ibba M.; RT "The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)- RT beta-lysine."; RL Nat. Chem. Biol. 7:667-669(2011). RN [11] RP BETA-LYSYLATION AT LYS-34 BY EPMA AND EPMB, HYDROXYLATION AT LYS-34, AND RP 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 HYDROXYLATION AT LYS-34 BY EPMC, AND MASS SPECTROMETRY. RC STRAIN=K12 / AT713, K12 / BW25113, K12 / MC4100 / ATCC 35695 / DSM 6574, RC and MRE-600; RX PubMed=22706199; DOI=10.1038/nchembio.1001; RA Peil L., Starosta A.L., Virumae K., Atkinson G.C., Tenson T., Remme J., RA Wilson D.N.; RT "Lys34 of translation elongation factor EF-P is hydroxylated by YfcM."; RL Nat. Chem. Biol. 8:695-697(2012). RN [13] RP FUNCTION IN POLY-PRO TRANSLATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF RP 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., 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., Rodnina M.V.; RT "EF-P is essential for rapid synthesis of proteins containing consecutive RT 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; GLY-33 RP 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 the CC sequence PPG is present in a protein, possibly by augmenting the CC peptidyl transferase activity of the ribosome. Beta-lysylation at Lys- CC 34 is required for alleviation. The Pro codons and their context do not CC affect activity; only consecutive Pro residues (not another amino acid) CC are affected by EF-P. Has stimulatory effects on peptide bond formation CC between ribosome-bound initiator tRNA(fMet) and puromycin, and N- CC acetyl-Phe tRNA(Phe)-primed 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 site, CC note that T.thermophilus structures show binding between the P and E CC sites (PDB 3HUW and 3HUY). Proportionally less EF-P binds to larger CC polysomes, suggesting it has a role early in translation. It is present CC in 1 copy per 10 ribosomes. {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 the CC stimulatory effect of EF-P on peptide-bond formation. The lysylation CC moiety would extend toward the peptidyltransferase center and stabilize CC the terminal 3-CCA end of the tRNA. The hydroxylation of the C5 CC position on Lys-34 would allow additional potential stabilizing CC hydrogen-bond interactions with the P-tRNA (PubMed:21841797 CC PubMed:22128152 PubMed:22706199 and PubMed:20729861). CC {ECO:0000269|PubMed:21841797, ECO:0000269|PubMed:22128152, CC ECO:0000269|PubMed:22706199}. CC -!- MASS SPECTROMETRY: Mass=20591.6; Method=Electrospray; Note=With N6- CC (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 (PubMed:20729861). CC Required for the expression of poly-Pro-containing proteins. CC {ECO:0000269|PubMed:20729861, ECO:0000269|PubMed:23239623, CC ECO:0000269|PubMed:9405429}. CC -!- SIMILARITY: Belongs to the elongation factor P family. {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_STEB01000014.1. 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 AlphaFoldDB; P0A6N4; -. DR SMR; P0A6N4; -. DR BioGRID; 4260776; 791. DR DIP; DIP-31834N; -. DR IntAct; P0A6N4; 51. DR STRING; 511145.b4147; -. DR jPOST; P0A6N4; -. DR PaxDb; P0A6N4; -. DR PRIDE; P0A6N4; -. DR EnsemblBacteria; AAC77107; AAC77107; b4147. DR EnsemblBacteria; BAE78149; BAE78149; BAE78149. DR GeneID; 67414765; -. DR GeneID; 69473621; -. DR GeneID; 948661; -. DR KEGG; ecj:JW4107; -. DR KEGG; eco:b4147; -. DR PATRIC; fig|1411691.4.peg.2553; -. DR EchoBASE; EB2023; -. DR eggNOG; COG0231; Bacteria. DR HOGENOM; CLU_074944_0_0_6; -. DR InParanoid; P0A6N4; -. DR OMA; WSVVEFQ; -. DR PhylomeDB; P0A6N4; -. DR BioCyc; EcoCyc:EG12099-MON; -. DR BioCyc; MetaCyc:EG12099-MON; -. 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 Gene3D; 2.40.50.140; -; 2. 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; Cytoplasm; Direct protein sequencing; Elongation factor; KW Hydroxylation; Protein biosynthesis; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1956781, FT ECO:0000269|PubMed:9298646" FT CHAIN 2..188 FT /note="Elongation factor P" FT /id="PRO_0000094245" FT MOD_RES 34 FT /note="N6-(3,6-diaminohexanoyl)-5-hydroxylysine" FT /evidence="ECO:0000269|PubMed:21841797, FT ECO:0000269|PubMed:22128152, ECO:0000269|PubMed:22706199" FT MUTAGEN 31 FT /note="K->A: No lysylation." FT /evidence="ECO:0000269|PubMed:20729861" FT MUTAGEN 33 FT /note="G->K: No lysylation. Loss of in vivo EF-P function FT for cell growth." FT /evidence="ECO:0000269|PubMed:20729861" FT MUTAGEN 34 FT /note="K->A: No lysylation and loss of EF-P activity. No FT facilitation of translation of poly-Pro stretches." FT /evidence="ECO:0000269|PubMed:20729861, FT ECO:0000269|PubMed:22128152, ECO:0000269|PubMed:23239623" FT STRAND 4..6 FT /evidence="ECO:0007829|PDB:3A5Z" FT STRAND 14..17 FT /evidence="ECO:0007829|PDB:3A5Z" FT STRAND 20..30 FT /evidence="ECO:0007829|PDB:3A5Z" FT STRAND 38..45 FT /evidence="ECO:0007829|PDB:3A5Z" FT HELIX 46..48 FT /evidence="ECO:0007829|PDB:3A5Z" FT STRAND 51..57 FT /evidence="ECO:0007829|PDB:3A5Z" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:3A5Z" FT STRAND 67..70 FT /evidence="ECO:0007829|PDB:3A5Z" FT STRAND 73..77 FT /evidence="ECO:0007829|PDB:3A5Z" FT STRAND 82..85 FT /evidence="ECO:0007829|PDB:3A5Z" FT TURN 87..89 FT /evidence="ECO:0007829|PDB:3A5Z" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:3A5Z" FT HELIX 97..100 FT /evidence="ECO:0007829|PDB:3A5Z" FT TURN 102..106 FT /evidence="ECO:0007829|PDB:3A5Z" FT STRAND 109..112 FT /evidence="ECO:0007829|PDB:3A5Z" FT STRAND 114..118 FT /evidence="ECO:0007829|PDB:3A5Z" FT STRAND 121..126 FT /evidence="ECO:0007829|PDB:3A5Z" FT STRAND 152..156 FT /evidence="ECO:0007829|PDB:3A5Z" FT STRAND 161..164 FT /evidence="ECO:0007829|PDB:3A5Z" FT STRAND 173..177 FT /evidence="ECO:0007829|PDB:3A5Z" FT TURN 178..181 FT /evidence="ECO:0007829|PDB:3A5Z" FT STRAND 182..186 FT /evidence="ECO:0007829|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 //