ID B8FET7_DESAL Unreviewed; 397 AA. AC B8FET7; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, 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=Dalk_1917 {ECO:0000313|EMBL:ACL03614.1}, Dalk_1928 GN {ECO:0000313|EMBL:ACL03625.1}; OS Desulfatibacillum aliphaticivorans. OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales; OC Desulfatibacillaceae; Desulfatibacillum. OX NCBI_TaxID=218208 {ECO:0000313|EMBL:ACL03614.1, ECO:0000313|Proteomes:UP000000739}; RN [1] {ECO:0000313|EMBL:ACL03614.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK-01 {ECO:0000313|EMBL:ACL03614.1}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., RA Wawrik B., Richardson P.; RT "Complete sequence of Desulfatibacillum alkenivorans AK-01."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACL03614.1, ECO:0000313|Proteomes:UP000000739} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AK-01 {ECO:0000313|EMBL:ACL03614.1, RC ECO:0000313|Proteomes:UP000000739}; RX PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x; RA Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N., RA Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.; RT "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint RT for anaerobic alkane oxidation."; RL Environ. Microbiol. 14:101-113(2012). 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; CP001322; ACL03614.1; -; Genomic_DNA. DR EMBL; CP001322; ACL03625.1; -; Genomic_DNA. DR RefSeq; WP_012611045.1; NC_011768.1. DR AlphaFoldDB; B8FET7; -. DR KEGG; dal:Dalk_1917; -. DR KEGG; dal:Dalk_1928; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_7; -. DR Proteomes; UP000000739; 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:UP000000739}. FT DOMAIN 10..207 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 397 AA; 43864 MW; 519FA43F1E443C54 CRC64; MAKAKYERTK PHVNVGTIGH IDHGKTTLTA AITKTLGQKG QANFIPFDQI DKAPEEKARG ITIATAHVEY ETDNRHYAHV DCPGHADYIK NMITGAAQMD GAILVVGADD GPMPQTREHI LLARQVGVPR IVVFLNKCDM VDDEELIELV ELELRELLDK YEFPGDDTPI IRGSALKALE ADSYEDDACK PIFELMDAID SFIPEPVRDT DKPFLMPIED VFSISGRGTV VTGRVERGII RVSEEVEIVG IRPTIKTVCT GVEMFRKILD EGQAGDNIGV LLRGTKREDV ERGQVVTHVG KIKPYTKFKA EVYVLSKEEG GRHTPFFTGY RPQFYFRTTD VTGVVTLPEG VEMVMPGDNV AVEAELITPI AMEKEVRFAI REGGRTVGAG VVSEIIE //