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 29-SEP-2021, entry version 73. DE RecName: Full=Elongation factor P {ECO:0000255|HAMAP-Rule:MF_00141}; DE Short=EF-P {ECO:0000255|HAMAP-Rule:MF_00141}; GN Name=efp {ECO:0000255|HAMAP-Rule:MF_00141}; OrderedLocusNames=Sez_0352; OS Streptococcus equi subsp. zooepidemicus (strain MGCS10565). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=552526; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGCS10565; 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., Deleo F.R., RA Musser J.M.; RT "Genome sequence of a lancefield group C Streptococcus zooepidemicus strain RT causing epidemic nephritis: new information about an old 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 70S CC ribosomes in vitro. Probably functions indirectly by altering the CC affinity of the ribosome for aminoacyl-tRNA, thus increasing their CC reactivity as acceptors for peptidyl transferase. {ECO:0000255|HAMAP- CC Rule:MF_00141}. CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation. CC {ECO:0000255|HAMAP-Rule:MF_00141}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00141}. CC -!- SIMILARITY: Belongs to the elongation factor P family. CC {ECO:0000255|HAMAP-Rule:MF_00141}. 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; WP_012515004.1; NC_011134.1. DR SMR; B4U161; -. DR EnsemblBacteria; ACG61728; ACG61728; Sez_0352. DR GeneID; 64011708; -. DR KEGG; sez:Sez_0352; -. DR HOGENOM; CLU_074944_3_0_9; -. DR OMA; FMDNEDY; -. DR BioCyc; SEQU552526:G1GCI-382-MONOMER; -. DR UniPathway; UPA00345; -. DR Proteomes; UP000001873; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule. 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 3: Inferred from homology; KW Cytoplasm; Elongation factor; Protein biosynthesis. FT CHAIN 1..185 FT /note="Elongation factor P" FT /id="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 //