ID D3PN44_MEIRD Unreviewed; 405 AA. AC D3PN44; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, 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 OrderedLocusNames=Mrub_2621 {ECO:0000313|EMBL:ADD29371.1}; GN ORFNames=K649_09430 {ECO:0000313|EMBL:AGK05179.1}; OS Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus OS ruber). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus. OX NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK05179.1, ECO:0000313|Proteomes:UP000013026}; RN [1] {ECO:0000313|EMBL:ADD29371.1, ECO:0000313|Proteomes:UP000006655} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21 RC {ECO:0000313|Proteomes:UP000006655}, and DSM 1279 RC {ECO:0000313|EMBL:ADD29371.1}; RX PubMed=21304689; DOI=10.4056/sigs.1032748; RA Tindall B.J., Sikorski J., Lucas S., Goltsman E., Copeland A., RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., RA Fahnrich R., Goodwin L., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Lapidus A.; RT "Complete genome sequence of Meiothermus ruber type strain (21)."; RL Stand. Genomic Sci. 3:26-36(2010). RN [2] {ECO:0000313|EMBL:AGK05179.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1279 {ECO:0000313|EMBL:AGK05179.1}; RA Klammer A., Drake J., Heiner C., Clum A., Copeland A., Huddleston J., RA Eichler E., Turner S.W.; RT "Non-Hybrid, Finished Microbial Genome Assemblies from Long-Read SMRT RT Sequencing Data."; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AGK05179.1, ECO:0000313|Proteomes:UP000013026} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21 RC {ECO:0000313|Proteomes:UP000013026}, and DSM 1279 RC {ECO:0000313|EMBL:AGK05179.1}; RA Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.; RL Submitted (APR-2013) 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; CP001743; ADD29371.1; -; Genomic_DNA. DR EMBL; CP005385; AGK05179.1; -; Genomic_DNA. DR RefSeq; WP_013014869.1; NC_021081.1. DR AlphaFoldDB; D3PN44; -. DR STRING; 504728.K649_09430; -. DR KEGG; mrb:Mrub_2621; -. DR KEGG; mre:K649_09430; -. DR PATRIC; fig|504728.9.peg.1946; -. DR eggNOG; COG0050; Bacteria. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000006655; Chromosome. DR Proteomes; UP000013026; 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..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; 44722 MW; AED239172CFC92D0 CRC64; MAKGVFERTK PHVNVGTIGH VDHGKTTLTA AITFVAAAAN PNVEVQAYDQ IDKAPEEKAR GITINTAHVE YETEKRHYSH VDCPGHADYV KNMITGAAQM DGAILVVSGT DGPMPQTREH ILLSRQVGVP YIIVFLNKID MVDDPELLDL VEMEIRDLLN QYEFPGDDTP IIRGSGLKAL EHMMAHPKTQ RGENEWVDKI WELLDAIDSY IPTPQRDVDK PFLMPVEDVF TITGRGTVAT GRIERGKIKT GDEVEIVGLR ETQKTVVTGV EMHRKTLSEG IAGDNVGLLL RGVSREDVER GQVLAKPGSV TPHTKFEASV YILKKEEGGR HTGFFTNYRP QFYFRTTDVT GVVELPKGVE MVMPGDNVTF TVELIKPIAM EEGLRFAIRE GGRTVGAGVV AKIIE //