ID H8K2U1_RICAG Unreviewed; 394 AA. AC H8K2U1; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAR-2024, entry version 65. 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=MCE_06595 {ECO:0000313|EMBL:AFC70133.1}; OS Rickettsia amblyommatis (strain GAT-30V) (Rickettsia amblyommii). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=1105111 {ECO:0000313|EMBL:AFC70133.1, ECO:0000313|Proteomes:UP000008005}; RN [1] {ECO:0000313|Proteomes:UP000008005} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GAT-30V {ECO:0000313|Proteomes:UP000008005}; RA Johnson S.L., Munk A.C., Han S., Bruce D.C., Dasch G.A.; RT "Complete genome sequence of Candidatus Rickettsia amblyommii strain GAT- RT 30V."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AFC70133.1, ECO:0000313|Proteomes:UP000008005} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GAT-30V {ECO:0000313|EMBL:AFC70133.1, RC ECO:0000313|Proteomes:UP000008005}; RX PubMed=27638476; DOI=10.1099/ijsem.0.001502; RA Karpathy S.E., Slater K.S., Goldsmith C.S., Nicholson W.L., Paddock C.D.; RT "Rickettsia amblyommatis sp. nov., a spotted fever group Rickettsia RT associated with multiple species of Amblyomma ticks in North, Central and RT South America."; RL Int. J. Syst. Evol. Microbiol. 66:5236-5243(2016). 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; CP003334; AFC70133.1; -; Genomic_DNA. DR RefSeq; WP_014392637.1; NC_017028.1. DR AlphaFoldDB; H8K2U1; -. DR STRING; 1105111.MCE_06595; -. DR KEGG; ram:MCE_06595; -. DR HOGENOM; CLU_007265_0_0_5; -. DR Proteomes; UP000008005; 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}; Hydrolase {ECO:0000313|EMBL:AFC70133.1}; 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..204 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 394 AA; 42833 MW; BFD94A829B2D0FC2 CRC64; MAKAKFERTK PHVNIGTIGH VDHGKTSLTA AITIVLAKTG GAQATAYDQI DAAPEEKERG ITISTAHVEY ETKNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI LLAKQVGVPA MVVFLNKVDM VDDPDLLELV EMEVRELLSK YGFPGDAIPI IKGSALQALE GKPEGEKAIN ELMDAVDSYI PQPVRATDKP FLMPIEDVFS ISGRGTVVTG RVESGIIKVG EEIEIVGLKD TQKTTCTGVE MFRKLLDEGQ AGDNVGILLR GTKREEVERG QVLAKPGSIK PHDQFEAEVY VLNKEEGGRH TPFTNDYRPQ FYFRTTDVTG TIKLPADKQM VMPGDNATFT VELIKPIAMQ EGLKFSIREG GRTVGAGVVT KINN //