ID A9BR91_DELAS Unreviewed; 396 AA. AC A9BR91; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAR-2024, entry version 97. 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=Daci_0503 {ECO:0000313|EMBL:ABX33149.1}; OS Delftia acidovorans (strain DSM 14801 / SPH-1). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Delftia. OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX33149.1, ECO:0000313|Proteomes:UP000000784}; RN [1] {ECO:0000313|EMBL:ABX33149.1, ECO:0000313|Proteomes:UP000000784} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784}; RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004; RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.; RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by RT defined pairs of heterotrophic bacteria."; RL Appl. Environ. Microbiol. 70:4053-4063(2004). RN [2] {ECO:0000313|Proteomes:UP000000784} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784}; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.; RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1."; RL Submitted (NOV-2007) 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; CP000884; ABX33149.1; -; Genomic_DNA. DR RefSeq; WP_012202435.1; NC_010002.1. DR AlphaFoldDB; A9BR91; -. DR STRING; 398578.Daci_0503; -. DR GeneID; 24113735; -. DR KEGG; dac:Daci_0503; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_4; -. DR Proteomes; UP000000784; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. 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}; Nucleotidyltransferase {ECO:0000313|EMBL:ABX33149.1}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00118}; Reference proteome {ECO:0000313|Proteomes:UP000000784}; KW Transferase {ECO:0000313|EMBL:ABX33149.1}. 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 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 396 AA; 43025 MW; 5A81B1E11E487A29 CRC64; MAKAKFERTK PHVNVGTIGH VDHGKTTLTA AIATVLSKKF GGEAKAYDQI DAAPEEKARG ITINTAHVEY ETAGRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI LLARQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLAK YDFPGDDTPI IRGSAKLALE GDQSDKGEAA ILRLAEALDS YIPTPERAVD GAFAMPVEDV FSISGRGTVV TGRIERGIIK VGEEIEIVGI RDTQKTIVTG VEMFRKLLDQ GQAGDNVGLL LRGTKREDVE RGQVLCKPGS IKPHTHFTAE VYVLSKDEGG RHTPFFNNYR PQFYFRTTDV TGSIELPADK EMVMPGDNVS ITVKLIAPIA MEEGLRFAIR EGGRTVGAGV VAKIIA //