ID F0RJL0_DEIPM Unreviewed; 405 AA. AC F0RJL0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 70. 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=Deipr_0392 {ECO:0000313|EMBL:ADY25562.1}, Deipr_1438 GN {ECO:0000313|EMBL:ADY26580.1}; OS Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / NBRC OS 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703 / MRP). OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae; OC Deinococcus. OX NCBI_TaxID=693977 {ECO:0000313|EMBL:ADY26580.1, ECO:0000313|Proteomes:UP000007718}; RN [1] {ECO:0000313|Proteomes:UP000007718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / RC VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., RA Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete sequence of chromosome of Deinococcus proteolyticus DSM RT 20540."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADY26580.1, ECO:0000313|Proteomes:UP000007718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / RC VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718}, and RC MRP {ECO:0000313|EMBL:ADY26580.1}; RX PubMed=22768367; DOI=10.4056/sigs.2756060; RA Copeland A., Zeytun A., Yassawong M., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S., RA Mavromatis K., Liolios K., Pagani I., Ivanova N., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brambilla E.M., RA Rohde M., Sikorski J., Pukall R., Goker M., Detter J.C., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Lapidus A.; RT "Complete genome sequence of the orange-red pigmented, radioresistant RT Deinococcus proteolyticus type strain (MRP(T))."; RL Stand. Genomic Sci. 6:240-250(2012). 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; CP002536; ADY25562.1; -; Genomic_DNA. DR EMBL; CP002536; ADY26580.1; -; Genomic_DNA. DR RefSeq; WP_013614171.1; NC_015161.1. DR AlphaFoldDB; F0RJL0; -. DR STRING; 693977.Deipr_0392; -. DR KEGG; dpt:Deipr_0392; -. DR KEGG; dpt:Deipr_1438; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_0; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000007718; 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:UP000007718}. FT DOMAIN 10..215 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 82..86 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 137..140 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" SQ SEQUENCE 405 AA; 44304 MW; 465887B7121B638A CRC64; MAKGTFERTK PHVNVGTIGH VDHGKTTLTA AITFTAAAMD DTVETLAYDQ IDKAPEEKAR GITINTSHVE YNTEGRHYSH VDCPGHADYV KNMITGAAQM DGAILVVSSA DGPMPQTREH ILLARQVGVP YIVVFMNKVD MVDDEELLEL VEMEVRELLS NYEFPGDDLP IVKGSALKAL EALQANPKTA RGQDEWVDRI WELLDAIDSY IPTPERDTDK AFLMPVEDVF TITGRGTVAT GRVERGIVKV GDEVEIVGLT DTKKTTVTGV EMHRKLLDSG MAGDNVGVLL RGVSRDDVER GQVLAKPGSI TPHTQFEASV YVLSKDEGGR HSAFFGGYRP QFYFRTTDVT GVVELKEGVE MVMPGDNVEF TVELIKPIAM EEGLRFAIRE GGRTVGAGVV TKVIK //