ID C0QQK8_PERMH Unreviewed; 396 AA. AC C0QQK8; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 93. 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_1 {ECO:0000313|EMBL:ACO03452.1}; GN Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118}, tuf_2 GN {ECO:0000313|EMBL:ACO03974.1}; GN OrderedLocusNames=PERMA_1180 {ECO:0000313|EMBL:ACO03452.1}, PERMA_1194 GN {ECO:0000313|EMBL:ACO03974.1}; OS Persephonella marina (strain DSM 14350 / EX-H1). OC Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae; OC Persephonella. OX NCBI_TaxID=123214 {ECO:0000313|EMBL:ACO03452.1, ECO:0000313|Proteomes:UP000001366}; RN [1] {ECO:0000313|EMBL:ACO03452.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=EX-H1; RA Heidelberg J.F., Reysenbach A.-L., Nelson W.C.; RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACO03452.1, ECO:0000313|Proteomes:UP000001366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14350 / EX-H1 {ECO:0000313|Proteomes:UP000001366}, and RC EX-H1 {ECO:0000313|EMBL:ACO03452.1}; RX PubMed=19136599; DOI=10.1128/JB.01645-08; RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S., RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.; RT "Complete and draft genome sequences of six members of the Aquificales."; RL J. Bacteriol. 191:1992-1993(2009). 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; CP001230; ACO03452.1; -; Genomic_DNA. DR EMBL; CP001230; ACO03974.1; -; Genomic_DNA. DR RefSeq; WP_012675691.1; NC_012440.1. DR AlphaFoldDB; C0QQK8; -. DR STRING; 123214.PERMA_1180; -. DR PaxDb; 123214-PERMA_1180; -. DR KEGG; pmx:PERMA_1180; -. DR KEGG; pmx:PERMA_1194; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_0; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000001366; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001366}. 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 396 AA; 43887 MW; 6291E48B7E9B54CE CRC64; MAREKFERKK EHVNVGTIGH VDHGKTTLTA AITYVLSKKG LAEFIGYGEI DKAPEERDRG ITINITHVEY ETEKRHYAHV DCPGHADYIK NMITGAAQMD GAILVVSAAD GPMPQTREHV LLARQVNVPY IVVFLNKCDM VDDEELLELV ELEVRELLNK YEFPGDDVPV IRGSALGALN DEEKWVKSIE ELLDAMDNYI PTPERATDKP FLMAIEDVFT ISGRGTVVTG RVERGTLKVG DEVEIVGLSD EIRKTVVTGI EMFRKTLDEA VAGDNVGVLL RGIGKDEVER GQVLAAPGSI TPHKKFKAQV YILSKEEGGR HTPFFLGYRP QFYIRTADIT GTVVELPEGQ EMVMPGDNVE LTVELMEPVA IEEQMRFAIR EGGRTVGAGV VTQIIE //