ID A0A7U4NS51_MYCPM Unreviewed; 190 AA. AC A0A7U4NS51; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 29-SEP-2021, entry version 2. DE RecName: Full=Elongation factor P {ECO:0000256|HAMAP-Rule:MF_00141}; DE Short=EF-P {ECO:0000256|HAMAP-Rule:MF_00141}; GN Name=efp {ECO:0000256|HAMAP-Rule:MF_00141}; GN ORFNames=F537_00160 {ECO:0000313|EMBL:ALA34131.1}; OS Mycoplasma pneumoniae 85084. OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=1263762 {ECO:0000313|EMBL:ALA34131.1, ECO:0000313|Proteomes:UP000057765}; RN [1] {ECO:0000313|EMBL:ALA34131.1, ECO:0000313|Proteomes:UP000057765} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=85084 {ECO:0000313|EMBL:ALA34131.1, RC ECO:0000313|Proteomes:UP000057765}; RX PubMed=26275904; DOI=10.1186/s12864-015-1801-0; RA Xiao L., Ptacek T., Osborne J.D., Crabb D.M., Simmons W.L., Lefkowitz E.J., RA Waites K.B., Atkinson T.P., Dybvig K.; RT "Comparative genome analysis of Mycoplasma pneumoniae."; RL BMC Genomics 16:610-610(2015). 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:0000256|HAMAP- CC Rule:MF_00141}. CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation. CC {ECO:0000256|ARBA:ARBA00004815, ECO:0000256|HAMAP-Rule:MF_00141}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00141}. CC -!- SIMILARITY: Belongs to the elongation factor P family. CC {ECO:0000256|ARBA:ARBA00009479, ECO:0000256|HAMAP-Rule:MF_00141, CC ECO:0000256|RuleBase:RU004389}. 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; CP010544; ALA34131.1; -; Genomic_DNA. DR RefSeq; WP_010874386.1; NZ_CP010544.1. DR GeneID; 45595891; -. DR UniPathway; UPA00345; -. DR Proteomes; UP000057765; Chromosome. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00141}; KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP- KW Rule:MF_00141}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00141}. FT DOMAIN 70..124 FT /note="EFP" FT /evidence="ECO:0000259|SMART:SM01185" FT DOMAIN 132..187 FT /note="Elong-fact-P_C" FT /evidence="ECO:0000259|SMART:SM00841" SQ SEQUENCE 190 AA; 21810 MW; 547284880C514BCA CRC64; MADMIEAKSL RSGQTIFGPN KEILLVLENT FNKTAMRQGI VKTKVKNLRT GAIVWIEFTG DKLEQVIIDK KKMTFLYKDG ANYVFMDQQD YSQIEIPEKQ LEWEKNFITE DSEVTIISYQ SEILGVNLPE LVPIEVEFAE EAVQGNTANM ARKRARLVSG YELDVPQFIR TGDKIVISTI DGSYRERYNK //