ID F2NCP5_DESAR Unreviewed; 397 AA. AC F2NCP5; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 65. 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 OrderedLocusNames=Desac_1458 {ECO:0000313|EMBL:AEB09313.1}, Desac_1471 GN {ECO:0000313|EMBL:AEB09326.1}; OS Desulfobacca acetoxidans (strain ATCC 700848 / DSM 11109 / ASRB2). OC Bacteria; Thermodesulfobacteriota; Desulfobaccia; Desulfobaccales; OC Desulfobaccaceae; Desulfobacca. OX NCBI_TaxID=880072 {ECO:0000313|EMBL:AEB09326.1, ECO:0000313|Proteomes:UP000000483}; RN [1] {ECO:0000313|EMBL:AEB09326.1, ECO:0000313|Proteomes:UP000000483} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700848 / DSM 11109 / ASRB2 RC {ECO:0000313|Proteomes:UP000000483}, and DSM 11109 RC {ECO:0000313|EMBL:AEB09326.1}; RX PubMed=21886866; RA Goker M., Teshima H., Lapidus A., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., RA Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K., RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Brambilla E.M., Rohde M., Spring S., Detter J.C., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of the acetate-degrading sulfate reducer RT Desulfobacca acetoxidans type strain (ASRB2)."; RL Stand. Genomic Sci. 4:393-401(2011). RN [2] {ECO:0000313|Proteomes:UP000000483} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700848 / DSM 11109 / ASRB2 RC {ECO:0000313|Proteomes:UP000000483}; 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., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Desulfobacca acetoxidans DSM 11109."; RL Submitted (MAR-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; CP002629; AEB09313.1; -; Genomic_DNA. DR EMBL; CP002629; AEB09326.1; -; Genomic_DNA. DR RefSeq; WP_013706424.1; NC_015388.1. DR AlphaFoldDB; F2NCP5; -. DR STRING; 880072.Desac_1458; -. DR KEGG; dao:Desac_1458; -. DR KEGG; dao:Desac_1471; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_7; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000000483; 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:UP000000483}. FT DOMAIN 10..207 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; 43680 MW; 0984DB67A9F5875D CRC64; MAKKKFERKK PHVNIGTIGH IDHGKTTLTA AITKHLSLKG MAEYVPFDQI DKAPEEKERG ITIATAHVEY ETDNRHYAHV DCPGHADYIK NMITGAAQMD GAILVVGADD GPMPQTREHI LLARQVGVPY IVVFLNKVDM VDDPELIELV ELELRELLSK YDFPGDDIPI VKGSALKALE SDDPKSEAAA CIFELMKAVD GYIPEPVRDV DKPFLMPIED VFSISGRGTV VTGRVERGII KVQEEVEIVG FGPTFKTVCT GVEMFRKILD QGQAGDNIGI LLRGTKKDEV ERGQVVAKPG SITPHTKFKA EVYVLNKEEG GRHTPFFSGY RPQFYLRTTD VTGVVTLPEG VEMVMPGDNV AIEVHLITPV ALEKELRFAI REGGRTVGAG VVTEIVE //