ID D4ZE74_SHEVD Unreviewed; 394 AA. AC D4ZE74; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAR-2024, entry version 74. 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=tufA-1 {ECO:0000313|EMBL:BAJ04135.1}; GN Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118}, tufA-2 GN {ECO:0000313|EMBL:BAJ04147.1}; GN OrderedLocusNames=SVI_4164 {ECO:0000313|EMBL:BAJ04135.1}, SVI_4176 GN {ECO:0000313|EMBL:BAJ04147.1}; OS Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ04135.1, ECO:0000313|Proteomes:UP000002350}; RN [1] {ECO:0000313|EMBL:BAJ04135.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSS12 {ECO:0000313|EMBL:BAJ04135.1}; RA Mori H.; RT "Shewanella violocea DSS2 complete genome."; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000002350} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12 RC {ECO:0000313|Proteomes:UP000002350}; RX PubMed=20458400; DOI=10.1039/c000396d; RA Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H., RA Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T., RA Nakasone K., Mori H.; RT "Complete genome sequence and comparative analysis of Shewanella violacea, RT a psychrophilic and piezophilic bacterium from deep sea floor sediments."; RL Mol. Biosyst. 6:1216-1226(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; AP011177; BAJ04135.1; -; Genomic_DNA. DR EMBL; AP011177; BAJ04147.1; -; Genomic_DNA. DR RefSeq; WP_013053420.1; NC_014012.1. DR AlphaFoldDB; D4ZE74; -. DR STRING; 637905.SVI_4164; -. DR KEGG; svo:SVI_4164; -. DR KEGG; svo:SVI_4176; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_6; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000002350; 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:UP000002350}. 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; 43110 MW; D85FDA0A1A2DFDA9 CRC64; MAKEKFERNK PHVNVGTIGH VDHGKTTLTA AISAVLAKTY GGDVKDFSQI DNAPEERERG ITINTSHIEY DTPARHYAHV DCPGHADYVK NMITGAAQMD GAILVVASTD GPMPQTREHI LLSRQVGVPF IIVFMNKCDM VDDEELLELV EMEVRELLSE YDFPGDDLPV IQGSALKALE GEAEWEAKII ELAEALDTYI PEPERAIDGA FLLPIEDVFS ISGRGTVVTG RVERGIIKVG EEVEIVGIKD TTKSTCTGVE MFRKLLDEGR AGENCGVLLR GIKREDVERG QVLAAPASIT PHTTFESEIY VLSKEEGGRH TPFFKGYRPQ FFFRTTDVTG TIELPEGVEM VMPGDNVQMV VTLIAPIAMD EGLRFAIREG GRTVGAGVVA KILA //