ID B2TIG1_CLOBB Unreviewed; 397 AA. AC B2TIG1; U4P1I3; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 93. 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=tuf {ECO:0000256|HAMAP-Rule:MF_00118, GN ECO:0000313|EMBL:ACD24211.1}; GN OrderedLocusNames=CLL_A0224 {ECO:0000313|EMBL:ACD24211.1}, CLL_A0236 GN {ECO:0000313|EMBL:ACD23275.1}; OS Clostridium botulinum (strain Eklund 17B / Type B). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD24211.1, ECO:0000313|Proteomes:UP000001195}; RN [1] {ECO:0000313|Proteomes:UP000001195} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195}; RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., RA Smith T.J., Sutton G., Brettin T.S.; RT "Complete sequence of Clostridium botulinum strain Eklund."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACD24211.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Eklund 17B {ECO:0000313|EMBL:ACD24211.1}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., RA Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Gronow S., Klenk H.-P., Eisen J.A.; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ACD24211.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Eklund 17B {ECO:0000313|EMBL:ACD24211.1}; RA Shrivastava S., Brinkac L.M., Dodson R.J., Harkins D.M., Durkin A.S., RA Sutton G.; RL Submitted (AUG-2009) 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: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; CP001056; ACD23275.1; -; Genomic_DNA. DR EMBL; CP001056; ACD24211.1; -; Genomic_DNA. DR AlphaFoldDB; B2TIG1; -. DR KEGG; cbk:CLL_A0224; -. DR KEGG; cbk:CLL_A0236; -. DR PATRIC; fig|935198.13.peg.197; -. DR HOGENOM; CLU_007265_0_1_9; -. DR Proteomes; UP000001195; 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; 43569 MW; 34E040177E382AB7 CRC64; MSKEKFERSK PHVNIGTIGH VDHGKTTLTA AITTVLANRG FAEAFNYAEI DKAPEEKERG ITINTAHVEY ETENRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI LLASRVGVDY IVVFLNKADM VDDEELLELV EMEVRELLSE YNFPGDDIPV IKGSALKALE NPTDETAIAP ILELMEAVDS YIPTPERATD KPFIMPVEDV FTITGRGTVA TGRVETGILH VGDEVEIVGL SEEKKKVVVT GIEMFRKLLD EAQAGDNIGA LLRGVQRADI ERGQVIAVPN SVHPHTKFVG QVYVLKKEEG GRHTPFFDGY RPQFYFRTTD VTGSIKLPDG MEMVMPGDHI DMNVELITPV AMDEGLRFAI REGGRTVGSG VVTKINA //