ID EFTU_CHLP8 Reviewed; 393 AA. AC P42473; B3QR65; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 136. DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118}; GN Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=Cpar_0175; OS Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme OS subsp. thiosulfatophilum). OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=517417; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8085791; DOI=10.1007/bf00873088; RA Ludwig W., Neumaier J., Klugbauer N., Brockmann E., Roller C., RA Klugbauer S., Reetz K., Schachtner I., Ludvigsen A., Bachleitner M., RA Fischer U., Schleifer K.H.; RT "Phylogenetic relationships of Bacteria based on comparative sequence RT analysis of elongation factor Tu and ATP-synthase beta-subunit genes."; RL Antonie Van Leeuwenhoek 64:285-305(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 263 / NCIMB 8327; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J., RA Bryant D.A., Richardson P.; RT "Complete sequence of Chlorobaculum parvum NCIB 8327."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- CC tRNA to the A-site of ribosomes during protein biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00118}. 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; X77033; CAA54322.1; -; Genomic_DNA. DR EMBL; CP001099; ACF10602.1; -; Genomic_DNA. DR RefSeq; WP_012501437.1; NC_011027.1. DR AlphaFoldDB; P42473; -. DR SMR; P42473; -. DR STRING; 517417.Cpar_0175; -. DR KEGG; cpc:Cpar_0175; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_10; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000008811; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule. DR CDD; cd01884; EF_Tu; 1. DR CDD; cd03697; EFTU_II; 1. DR CDD; cd03707; EFTU_III; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 2. DR HAMAP; MF_00118_B; EF_Tu_B; 1. DR InterPro; IPR041709; EF-Tu_GTP-bd. DR InterPro; IPR004161; EFTu-like_2. DR InterPro; IPR033720; EFTU_2. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel_sf. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org. DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C. DR NCBIfam; TIGR00485; EF-Tu; 1. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1. DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF03143; GTP_EFTU_D3; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding; KW Protein biosynthesis. FT CHAIN 1..393 FT /note="Elongation factor Tu" FT /id="PRO_0000091311" FT DOMAIN 10..203 FT /note="tr-type G" FT REGION 19..26 FT /note="G1" FT /evidence="ECO:0000250" FT REGION 60..64 FT /note="G2" FT /evidence="ECO:0000250" FT REGION 81..84 FT /note="G3" FT /evidence="ECO:0000250" FT REGION 136..139 FT /note="G4" FT /evidence="ECO:0000250" FT REGION 173..175 FT /note="G5" FT /evidence="ECO:0000250" FT BINDING 19..26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT BINDING 81..85 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT BINDING 136..139 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" SQ SEQUENCE 393 AA; 42699 MW; 8F3C4838353CEF31 CRC64; MAKESYKRDK PHVNIGTIGH VDHGKTTLTA AITSVLAKSG KAAAREFGDI DKAPEERERG ITISTAHVEY QTDKRHYAHI DCPGHADYIK NMITGAAQMD GAILVVAGTD GPMPQTREHI LLARQVNVPA LVVFLNKVDI ADPELLELVE MELRELLTEY GFPGDDIPII KGSALNALNG DPEGEKAIME LMDAVDDYIP EPVRDVDKPF LMPVEDVFSI SGRGTVGTGR IERGIIKVGN EVEIVGIKPT TKSVVTGIEM FQKTLDEGQA GDNAGLLLRG VDKEALERGM VIAKPGSITP HTKFKAEVYI LKKEEGGRHT PFFNGYRPQF YFRTTDVTGS VTLPEGVEMV MPGDNLSVDV ELIAPIAMEE SLRFAIREGG RTVGAGSVTK IVE //