ID E0UU51_SULAO Unreviewed; 399 AA. AC E0UU51; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 27-MAR-2024, entry version 71. 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=Saut_0311 {ECO:0000313|EMBL:ADN08360.1}; OS Sulfurimonas autotrophica (strain ATCC BAA-671 / DSM 16294 / JCM 11897 / OS OK10). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Sulfurimonadaceae; Sulfurimonas. OX NCBI_TaxID=563040 {ECO:0000313|EMBL:ADN08360.1, ECO:0000313|Proteomes:UP000007803}; RN [1] {ECO:0000313|EMBL:ADN08360.1, ECO:0000313|Proteomes:UP000007803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10 RC {ECO:0000313|Proteomes:UP000007803}; RX PubMed=21304749; RA Sikorski J., Munk C., Lapidus A., Ngatchou Djao O.D., Lucas S., RA Glavina Del Rio T., Nolan M., Tice H., Han C., Cheng J.F., Tapia R., RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., RA Mikhailova N., Pati A., Sims D., Meincke L., Brettin T., Detter J.C., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Rohde M., Lang E., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Sulfurimonas autotrophica type strain RT (OK10)."; RL Stand. Genomic Sci. 3:194-202(2010). RN [2] {ECO:0000313|Proteomes:UP000007803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10 RC {ECO:0000313|Proteomes:UP000007803}; RX DOI=10.4056/sigs.1173118; RA Sikorski J., Munk C., Lapidus A., Djao O., Lucas S., Glavina Del Rio T., RA Nolan M., Tice H., Han C., Cheng J., Tapia R., Goodwin L., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Sims D., RA Meincke L., Brettin T., Detter J., Chen A., Palaniappan K., Land M., RA Hauser L., Chang Y., Jeffries C., Rohde M., Lang E., Spring S., Goker M., RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., RA Klenk H.; RT "Complete genome sequence of Sulfurimonas autotrophica type strain RT (OK10T)."; RL Stand. Genomic Sci. 3:194-202(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; CP002205; ADN08360.1; -; Genomic_DNA. DR RefSeq; WP_013326116.1; NC_014506.1. DR AlphaFoldDB; E0UU51; -. DR STRING; 563040.Saut_0311; -. DR KEGG; sua:Saut_0311; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_7; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000007803; 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:UP000007803}. FT DOMAIN 10..209 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 399 AA; 43671 MW; EEC23534E7AD268D CRC64; MAKEKFERNK PHVNIGTIGH VDHGKTTLTA AITAVLAVKN GAKFMDYDAI DNAPEERERG ITIATSHVEY ETDTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI LLSKQVGVPY IVVFMNKEDM VDDEELLELV EMEIRELLDM YEFPGDDTPI TAGSALKALE EAKTGTLGEW SEKIVALMDT VDEYIPEPVR ETDKDFLMPV EDVFSISGRG TVVTGRIERG VVKVGEEVEI VGIKDTQKTT VTGVEMFRKE MEQGEAGDNC GILVRGIAKD EVERGQVLCK PGTITPHTKF TAEIYVLSKD EGGRHTPFFN GYRPQFYVRT TDVTGAITLP EGTEMVMPGD NVSITAELIH PIAMEQGTKF AIREGGRTVG AGVVAEILA //