ID B1I1K8_DESAP Unreviewed; 399 AA. AC B1I1K8; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 94. 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=Daud_0207 {ECO:0000313|EMBL:ACA58768.1}; OS Desulforudis audaxviator (strain MP104C). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae; OC Desulforudis. OX NCBI_TaxID=477974 {ECO:0000313|EMBL:ACA58768.1, ECO:0000313|Proteomes:UP000008544}; RN [1] {ECO:0000313|Proteomes:UP000008544} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP104C {ECO:0000313|Proteomes:UP000008544}; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L., RA Hauser L., Kyrpides N., Ivanova N.N., Richardson P.; RT "Complete sequence of chromosome of Desulforudis audaxviator MP104C."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACA58768.1, ECO:0000313|Proteomes:UP000008544} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MP104C {ECO:0000313|EMBL:ACA58768.1, RC ECO:0000313|Proteomes:UP000008544}; RX PubMed=18845759; DOI=10.1126/science.1155495; RA Chivian D., Brodie E.L., Alm E.J., Culley D.E., Dehal P.S., Desantis T.Z., RA Gihring T.M., Lapidus A., Lin L.H., Lowry S.R., Moser D.P., RA Richardson P.M., Southam G., Wanger G., Pratt L.M., Andersen G.L., RA Hazen T.C., Brockman F.J., Arkin A.P., Onstott T.C.; RT "Environmental genomics reveals a single-species ecosystem deep within RT Earth."; RL Science 322:275-278(2008). 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; CP000860; ACA58768.1; -; Genomic_DNA. DR RefSeq; WP_012301361.1; NC_010424.1. DR AlphaFoldDB; B1I1K8; -. DR STRING; 477974.Daud_0207; -. DR KEGG; dau:Daud_0207; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_9; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000008544; 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:UP000008544}. FT DOMAIN 10..209 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 399 AA; 43651 MW; E90F488B9B18DEB3 CRC64; MAKPKFVRTK PHVNVGTIGH VDHGKTTLTA AITLVLSKLG QAEYKKYDDI DAAPEEKARG ITINTAHVEY ETEKRHYAHV DCPGHADYIK NMITGAAQMD GAILVVSAAD GPMPQTREHI LLARQVAVPS IVVYLNKADM VDDPELLELV EMEVRELLSN YEFPGDDTPI VTGSALKALE CGCANRECAH CKSIWELMDA VDNYIPTPER DIDKPFLMPV EDVFSITGRG TVGTGRVERG TVKTGDEVEI VGFAAKPRKT VVTGVEMFRK VLDYAQAGDN VGCLLRGVDR TELERGQVLA KPGSIKPLTE FTANVYVLSK EEGGRHTPFF NGYRPQFYFR TTDVTGVIHL PEGVEMVMPG DNLQMDVSLI TPIAIEEGLR FAIREGGRTV GAGVVTAIK //