ID EFTU_COXBU Reviewed; 397 AA. AC Q83ES6; B5QS64; Q83ET7; Q9X6G1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 129. DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118}; GN Name=tufA {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tuf-1; GN OrderedLocusNames=CBU_0221.2; ORFNames=CBU_0221b; GN and GN Name=tufB {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tuf-2; GN OrderedLocusNames=CBU_0236; OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae; OC Coxiella. OX NCBI_TaxID=227377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSA 493 / Nine Mile phase I; RX PubMed=12704232; DOI=10.1073/pnas.0931379100; RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., RA Fraser C.M., Heidelberg J.F.; RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-358, AND DEVELOPMENTAL STAGE. RC STRAIN=RSA 493 / Nine Mile phase I; RX PubMed=10531263; DOI=10.1128/iai.67.11.6026-6033.1999; RA Seshadri R., Hendrix L.R., Samuel J.E.; RT "Differential expression of translational elements by life cycle variants RT of Coxiella burnetii."; RL Infect. Immun. 67:6026-6033(1999). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY, AND DEVELOPMENTAL STAGE. RC STRAIN=Nine Mile Crazy / RSA 514; RX PubMed=17088354; DOI=10.1128/iai.00883-06; RA Coleman S.A., Fischer E.R., Cockrell D.C., Voth D.E., Howe D., Mead D.J., RA Samuel J.E., Heinzen R.A.; RT "Proteome and antigen profiling of Coxiella burnetii developmental forms."; RL Infect. Immun. 75:290-298(2007). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- CC tRNA to the A-site of ribosomes during protein biosynthesis. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DEVELOPMENTAL STAGE: Found in the large cell variant (LCV) stage, CC undetectable in the small cell variant (SCV) stage; at protein level. CC LCVs are more metabolically active than SCVs. CC {ECO:0000269|PubMed:10531263, ECO:0000269|PubMed:17088354}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A CC subfamily. {ECO:0000255|HAMAP-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; AE016828; ACI15245.1; -; Genomic_DNA. DR EMBL; AE016828; AAO89794.1; -; Genomic_DNA. DR EMBL; AF136604; AAD32649.1; -; Genomic_DNA. DR RefSeq; NP_819280.1; NC_002971.3. DR RefSeq; WP_005771609.1; NC_002971.4. DR RefSeq; YP_002332954.1; NC_002971.3. DR AlphaFoldDB; Q83ES6; -. DR SMR; Q83ES6; -. DR STRING; 227377.CBU_0221b; -. DR EnsemblBacteria; AAO89794; AAO89794; CBU_0236. DR EnsemblBacteria; ACI15245; ACI15245; CBU_0221b. DR GeneID; 1208103; -. DR GeneID; 1208117; -. DR KEGG; cbu:CBU_0221b; -. DR KEGG; cbu:CBU_0236; -. DR PATRIC; fig|227377.7.peg.217; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_6; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000002671; 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; IBA:GO_Central. DR GO; GO:0006414; P:translational elongation; IBA:GO_Central. 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 1: Evidence at protein level; KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1..397 FT /note="Elongation factor Tu" FT /id="PRO_1000015645" FT DOMAIN 10..206 FT /note="tr-type G" FT REGION 19..26 FT /note="G1" FT /evidence="ECO:0000250" FT REGION 60..64 FT /note="G2" FT /evidence="ECO:0000250" FT REGION 81..84 FT /note="G3" FT /evidence="ECO:0000250" FT REGION 136..139 FT /note="G4" FT /evidence="ECO:0000250" FT REGION 174..176 FT /note="G5" FT /evidence="ECO:0000250" FT BINDING 19..26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT BINDING 81..85 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT BINDING 136..139 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" SQ SEQUENCE 397 AA; 43526 MW; 8157B2CD749064FF CRC64; MSKEKFVREK PHVNVGTIGH VDHGKTTLTA ALTKVLSEKY GGEKKAFDQI DNAPEERARG ITIATSHVEY QSDKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI VLAKQVGVPN IVVYLNKADM VDDKELLELV EMEVRDLLNS YDFPGDETPI IVGSALKALE GDKSEVGEPS IIKLVETMDT YFPQPERAID KPFLMPIEDV FSISGRGTVV TGRVERGIIK VGDEIEIVGI KDTTKTTCTG VEMFRKLLDE GQAGDNVGIL LRGTKREEVE RGQVLAKPGS ITPHKKFEAE IYVLSKEEGG RHTPFLQGYR PQFYFRTTDV TGQLLSLPEG IEMVMPGDNV KVTVELIAPV AMDEGLRFAV REGGRTVGAG VVTKIIE //