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 24-JAN-2024, entry version 99. 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=Jann_3254; OS Jannaschia sp. (strain CCS1). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Roseobacteraceae; Jannaschia. OX NCBI_TaxID=290400; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCS1; RG US DOE Joint Genome Institute; 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., Bruce D., RA Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J., RA Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W., RA 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 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; CP000264; ABD56171.1; -; Genomic_DNA. DR RefSeq; WP_011456373.1; NC_007802.1. DR AlphaFoldDB; Q28M91; -. DR SMR; Q28M91; -. DR STRING; 290400.Jann_3254; -. DR KEGG; jan:Jann_3254; -. DR eggNOG; COG0231; Bacteria. DR HOGENOM; CLU_074944_1_1_5; -. DR OMA; LYRMRMY; -. DR OrthoDB; 9801844at2; -. DR UniPathway; UPA00345; -. DR Proteomes; UP000008326; 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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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_uL2_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 NCBIfam; TIGR00038; efp; 1. DR PANTHER; PTHR30053:SF14; EFP_N DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR30053; ELONGATION FACTOR P; 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; SSF50249; Nucleic acid-binding proteins; 2. DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1. DR PROSITE; PS01275; EFP; 1. PE 3: Inferred from homology; KW Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome. FT CHAIN 1..187 FT /note="Elongation factor P" FT /id="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 //