ID EFP_STREM Reviewed; 185 AA. AC B4U161; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 13-JUL-2010, entry version 16. DE RecName: Full=Elongation factor P; DE Short=EF-P; GN Name=efp; OrderedLocusNames=Sez_0352; OS Streptococcus equi subsp. zooepidemicus (strain MGCS10565). OC Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=552526; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18716664; DOI=10.1371/journal.pone.0003026; RA Beres S.B., Sesso R., Pinto S.W.L., Hoe N.P., Porcella S.F., RA Deleo F.R., Musser J.M.; RT "Genome sequence of a lancefield group C Streptococcus zooepidemicus RT strain causing epidemic nephritis: new information about an old RT disease."; RL PLoS ONE 3:E3026-E3026(2008). 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 (By CC similarity). CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). 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; CP001129; ACG61728.1; -; Genomic_DNA. DR RefSeq; YP_002122741.1; -. DR EnsemblBacteria; EBSTRT00000008827; EBSTRP00000008388; EBSTRG00000008827. DR GeneID; 6760491; -. DR GenomeReviews; CP001129_GR; Sez_0352. DR KEGG; sez:Sez_0352; -. DR HOGENOM; HBG303311; -. DR OMA; DNAECIV; -. DR ProtClustDB; PRK00529; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003746; F:translation elongation factor activity; IEA:HAMAP. DR GO; GO:0006414; P:translational elongation; IEA:HAMAP. 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; Elongation factor; Protein biosynthesis. FT CHAIN 1 185 Elongation factor P. FT /FTId=PRO_1000096207. SQ SEQUENCE 185 AA; 20608 MW; D83139598F2535F8 CRC64; MIEASKLRAG MTFEAEGKLI RVLEASHHKP GKGNTIMRMK LRDVRTGSTF DTTYRPDEKF EQAIIETVPA QYLYKMDDTA YFMNTETYDQ YEIPVANVEQ ELLYILENSD VKIQFYGTEV IGVQVPTTVE LTVTETQPSI KGATVTGSGK PATLETGLVV NVPDFIEVGQ KLIINTAEGT YVSRA //