ID EFP_JANSC Reviewed; 187 AA. AC Q28M91; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 1. DT 10-JUN-2008, entry version 21. DE Elongation factor P (EF-P). GN Name=efp; OrderedLocusNames=Jann_3254; OS Jannaschia sp. (strain CCS1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Jannaschia. OX NCBI_TaxID=290400; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E., RA Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., RA Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.; RT "Complete sequence of chromosome of Jannaschia sp. CCS1."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. 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. 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; CP000264; ABD56171.1; -; Genomic_DNA. DR RefSeq; YP_511196.1; -. DR GeneID; 3935726; -. DR GenomeReviews; CP000264_GR; Jann_3254. DR KEGG; jan:Jann_3254; -. DR HOGENOM; Q28M91; -. DR BioCyc; JSP290400:JANN_3254-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. DR GO; GO:0003746; F:translation elongation factor activity; IEA:HAMAP. DR GO; GO:0006414; P:translational elongation; IEA:HAMAP. DR HAMAP; MF_00141; -; 1. DR InterPro; IPR015365; Elong-fact-P_C. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR011768; Transl_elong_EFP. 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; IPR014722; Transl_SH3_like_sub. 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 TIGRFAMs; TIGR00038; efp; 1. DR PROSITE; PS01275; EFP; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Elongation factor; Protein biosynthesis. FT CHAIN 1 187 Elongation factor P. FT /FTId=PRO_1000010764. SQ SEQUENCE 187 AA; 20896 MW; 87B3A4176AF2A2D0 CRC64; MPKINGNEIR PGNVLEHNGG LWAAVKVDHV KPGKGGAFAQ VELRNLRNGS KLNERFRSAD KVERVRLEQK DQQFLYESDG MLVFMDAETY EQIELPAELL GERRPFLQDG MTIVVEFHDD EALNASLPQK VVCKVVETEP VVKGQTAANS FKPAILDNGV KVMVPPFVGQ DEDIVVNTET MDYSERA //