ID D8GJ42_CLOLD Unreviewed; 397 AA. AC D8GJ42; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAR-2024, entry version 72. DE RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118}; GN Name=tuf1 {ECO:0000313|EMBL:ADK17130.1}; GN Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118}, tuf2 GN {ECO:0000313|EMBL:ADK17144.1}; GN OrderedLocusNames=CLJU_c41060 {ECO:0000313|EMBL:ADK17130.1}, GN CLJU_c41200 {ECO:0000313|EMBL:ADK17144.1}; OS Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=748727 {ECO:0000313|EMBL:ADK17130.1, ECO:0000313|Proteomes:UP000001656}; RN [1] {ECO:0000313|EMBL:ADK17130.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 13528 {ECO:0000313|EMBL:ADK17130.1}; RA Koepke M., Hujer S., Held C., Wiezer A., Liesegang H., Ehrenreich A., RA Gottschalk G., Duerre P.; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADK17130.1, ECO:0000313|Proteomes:UP000001656} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55383 / DSM 13528 / RC PETC {ECO:0000313|Proteomes:UP000001656}, and DSM 13528 RC {ECO:0000313|EMBL:ADK17130.1}; RX PubMed=20616070; DOI=10.1073/pnas.1004716107; RA Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A., RA Ehrenreich A., Liebl W., Gottschalk G., Durre P.; RT "Clostridium ljungdahlii represents a microbial production platform based RT on syngas."; RL Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- CC tRNA to the A-site of ribosomes during protein biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00118}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP- CC 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; CP001666; ADK17130.1; -; Genomic_DNA. DR EMBL; CP001666; ADK17144.1; -; Genomic_DNA. DR RefSeq; WP_013240693.1; NC_014328.1. DR AlphaFoldDB; D8GJ42; -. DR STRING; 748727.CLJU_c41060; -. DR KEGG; clj:CLJU_c41060; -. DR KEGG; clj:CLJU_c41200; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_9; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000001656; 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 {ECO:0000256|HAMAP-Rule:MF_00118}; KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP- KW Rule:MF_00118}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_00118}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00118}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00118}. FT DOMAIN 10..206 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT BINDING 19..26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 81..85 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 136..139 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" SQ SEQUENCE 397 AA; 43791 MW; D3E4795EB815DA8A CRC64; MSKEKYERTK PHVNIGTIGH VDHGKTTLTA AITMVLSKEG KAAATKYDEI DKAPEEKERG ITINTAHVEY ETDKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI LLASRVGVQY IVVFLNKSDQ VDDPELLELV EMEVRELLSE YGFPGDDVPI IVGSALKVLE NPDDPETTKC IHELMDAVDE YIPTPERPTD KDFLMPIEDV FTITGRGTVA TGRVESGVLK IGDELEIVGL KEEKKKTTCT GVEMFRKLLD QAMAGDNIGV LLRGIQRDEV ERGQVLAKPG TVHPHKKFVG QVYVLKKEEG GRHTPFFNGY RPQFYFRTTD VTGSIALPEG VEMVMPGDHI DMNVELITPV AMHEGLRFAI REGGRTVGSG VVTTITE //