ID B6IRN9_RHOCS Unreviewed; 395 AA. AC B6IRN9; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 27-MAR-2024, entry version 95. 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:ACI98125.1}; GN OrderedLocusNames=RC1_0693 {ECO:0000313|EMBL:ACI98125.1}, RC1_0709 GN {ECO:0000313|EMBL:ACI98140.1}; OS Rhodospirillum centenum (strain ATCC 51521 / SW). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=414684 {ECO:0000313|EMBL:ACI98125.1, ECO:0000313|Proteomes:UP000001591}; RN [1] {ECO:0000313|Proteomes:UP000001591} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591}; RA Touchman J.W., Bauer C., Blankenship R.E.; RT "Genome sequence of Rhodospirillum centenum."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACI98125.1, ECO:0000313|Proteomes:UP000001591} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591}, and SW RC {ECO:0000313|EMBL:ACI98125.1}; RX PubMed=20500872; DOI=10.1186/1471-2164-11-325; RA Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D., Chowdhury S.R., RA Hao J., Helmy T., Kim S., Kurdoglu A.A., Matthies H.J., Rollo D., RA Stothard P., Blankenship R.E., Bauer C.E., Touchman J.W.; RT "Metabolic flexibility revealed in the genome of the cyst-forming alpha-1 RT proteobacterium Rhodospirillum centenum."; RL BMC Genomics 11:325-325(2010). 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; CP000613; ACI98125.1; -; Genomic_DNA. DR EMBL; CP000613; ACI98140.1; -; Genomic_DNA. DR RefSeq; WP_012565917.1; NC_011420.2. DR AlphaFoldDB; B6IRN9; -. DR STRING; 414684.RC1_0693; -. DR KEGG; rce:RC1_0693; -. DR KEGG; rce:RC1_0709; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_5; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000001591; 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: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:UP000001591}. FT DOMAIN 10..205 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 395 AA; 43160 MW; C2A70F6CBB3598CB CRC64; MAKAKFERTK PHCNVGTIGH VDHGKTSLTA AITKVLAKTG GATFTAYDQI DKAPEEKARG ITISTAHVEY ETTNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI LLARQVGVPA LVVFLNKMDM ADPELVELVE LEVRELLSSY GFPGDDIPVV KGSALCALED RNPEIGEQAI LELMRHVDAY IPQPERPKDR PFLMPIEDVF SISGRGTVVT GRVERGVIKV GEEVEIVGMK PTVKTTVTGV EMFRKLLDQG EAGDNIGALL RGTKREDVER GQVLAKPGSI TPHTKFEAET YILTKDEGGR HTPFFTNYRP QFYFRTTDVT GMVTLPEGTE MVMPGDNVRI RVELIAPIAM DEGLRFAIRE GGRTVGAGVV SKIIE //