ID C9LTC7_SELS3 Unreviewed; 395 AA. AC C9LTC7; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 27-MAR-2024, entry version 80. 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:EEX77973.1}; GN OrderedLocusNames=Selsp_1492 {ECO:0000313|EMBL:AEC00449.1}; GN ORFNames=SELSPUOL_00710 {ECO:0000313|EMBL:EEX77973.1}; OS Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28). OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae; OC Selenomonas. OX NCBI_TaxID=546271 {ECO:0000313|EMBL:EEX77973.1, ECO:0000313|Proteomes:UP000003505}; RN [1] {ECO:0000313|EMBL:EEX77973.1, ECO:0000313|Proteomes:UP000003505} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35185 {ECO:0000313|EMBL:EEX77973.1}, and ATCC 35185 / DSM RC 20758 / VPI D19B-28 {ECO:0000313|Proteomes:UP000003505}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L., RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C., RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A., RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AEC00449.1, ECO:0000313|Proteomes:UP000011124} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35185 {ECO:0000313|EMBL:AEC00449.1}, and ATCC 35185 / DSM RC 20758 / VPI D19B-28 {ECO:0000313|Proteomes:UP000011124}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., RA Wellnitz S., Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of Selenomonas sputigena DSM 20758."; RL Submitted (APR-2011) 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; CP002637; AEC00449.1; -; Genomic_DNA. DR EMBL; ACKP02000012; EEX77973.1; -; Genomic_DNA. DR RefSeq; WP_006191715.1; NZ_GG698596.1. DR AlphaFoldDB; C9LTC7; -. DR STRING; 546271.Selsp_1492; -. DR KEGG; ssg:Selsp_1492; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_9; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000003505; Unassembled WGS sequence. DR Proteomes; UP000011124; 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}; Reference proteome {ECO:0000313|Proteomes:UP000011124}. FT DOMAIN 10..204 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 395 AA; 43616 MW; 9437545888BA9615 CRC64; MAKQKFERNK PHVNIGTIGH VDHGKTTLTA AITKVLSKKG MAQFEDYADI DKAPEERERG ITINTAHVEY ETEKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI LLARQVGVPA IVVFLNKVDQ VDDPELLELV EMEVRDLLTA YEFPGDDIPV IAGSALKALE DDAEQEKKIL ELMDAVDEYI PTPTRDTEKP FLMPVEDVFT ITGRGTVATG RVERGELKLN DTVEIVGLED ETKSTVVTGI EMFRKMLDTA VAGDNIGALL RGVDRKDIVR GQVLAKPGSI NPHTKFKAQV YVLKKEEGGR HTPFFTNYRP QFYFRTTDVT GVVRLPEGTE MVMPGDNVEM EVELITPIAI EKGLRFAIRE GGHTVGAGRV TEIEG //