ID E3GZN1_ROTDC Unreviewed; 396 AA. AC E3GZN1; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAR-2024, entry version 76. 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:ADP39766.1}; GN OrderedLocusNames=HMPREF0733_10308 {ECO:0000313|EMBL:ADP39766.1}; OS Rothia dentocariosa (strain ATCC 17931 / CDC X599 / XDIA). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC Rothia. OX NCBI_TaxID=762948 {ECO:0000313|EMBL:ADP39766.1, ECO:0000313|Proteomes:UP000000387}; RN [1] {ECO:0000313|Proteomes:UP000000387} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17931 / CDC X599 / XDIA RC {ECO:0000313|Proteomes:UP000000387}; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A., RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X., RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J., RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A., RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B., RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J., RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M., RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G., RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M., RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L., RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.; RT "The complete genome of Rothia dentocariosa ATCC 17931."; RL Submitted (OCT-2010) 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; CP002280; ADP39766.1; -; Genomic_DNA. DR RefSeq; WP_013397618.1; NC_014643.1. DR AlphaFoldDB; E3GZN1; -. DR GeneID; 29742623; -. DR KEGG; rdn:HMPREF0733_10308; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_11; -. DR Proteomes; UP000000387; 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..206 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 83..87 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 138..141 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" SQ SEQUENCE 396 AA; 43744 MW; 0E6A5B19F44F5309 CRC64; MAKAKFERSK PHVNVGTIGH VDHGKTTLTA AISKVLADKY PDLNEQRDFG MIDSAPEERQ RGITINIAHI EYQTEKRHYA HVDAPGHADY VKNMITGAAQ MDGAILVVAA TDGPMAQTRE HVLLARQVGV PTLLVALNKA DMVDDEELLD LVEMEVRDLL SSQEFDGDDA PVIRVSALKA LEGDPEWVAK VEELMEAVDT YIPDPVRETD KPFLMPIEDV FTITGRGTVV TGRAERGTLK INSEVEIVGI RPIQKTTVTG IEMFHKQLDE AWAGENCGLL LRGLKRDDVE RGQVVVEPGS ITPHTEFEAN VYILSKDEGG RHNPFYSNYR PQFYFRTTDV TGVIKLPEGT EMVMPGDNTE MSVELIQPIA MEEGLGFAIR EGGRTVGSGR VTKIIK //