ID F8E997_FLESM Unreviewed; 396 AA. AC F8E997; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAR-2024, entry version 77. 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=Flexsi_0449 {ECO:0000313|EMBL:AEI14136.1}, GN Flexsi_0462 {ECO:0000313|EMBL:AEI14149.1}; OS Flexistipes sinusarabici (strain ATCC 49648 / DSM 4947 / MAS 10). OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales; OC Flexistipitaceae; Flexistipes. OX NCBI_TaxID=717231 {ECO:0000313|EMBL:AEI14149.1, ECO:0000313|Proteomes:UP000006621}; RN [1] {ECO:0000313|EMBL:AEI14149.1, ECO:0000313|Proteomes:UP000006621} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4947 {ECO:0000313|EMBL:AEI14149.1}, and DSM 4947 / MAS 10 RC {ECO:0000313|Proteomes:UP000006621}; RX PubMed=22180813; DOI=10.4056/sigs.2235024; RA Lapidus A., Chertkov O., Nolan M., Lucas S., Hammon N., Deshpande S., RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K., RA Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M., RA Abt B., Spring S., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Woyke T.; RT "Genome sequence of the moderately thermophilic halophile Flexistipes RT sinusarabici strain (MAS10)."; RL Stand. Genomic Sci. 5:86-96(2011). RN [2] {ECO:0000313|Proteomes:UP000006621} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621}; RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L., RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O., RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Flexistipes sinusarabici DSM 4947."; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. 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; CP002858; AEI14136.1; -; Genomic_DNA. DR EMBL; CP002858; AEI14149.1; -; Genomic_DNA. DR RefSeq; WP_013885646.1; NC_015672.1. DR AlphaFoldDB; F8E997; -. DR SMR; F8E997; -. DR STRING; 717231.Flexsi_0449; -. DR KEGG; fsi:Flexsi_0449; -. DR KEGG; fsi:Flexsi_0462; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_0; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000006621; 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:UP000006621}. FT DOMAIN 10..206 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; 43900 MW; A9732FCE180EA5A7 CRC64; MSKQKYERKK PHVNVGTIGH VDHGKTTLTA AMTHVLSLKG YADYIEFGNI DKAPEEKERG ITIATAHVEY ESDKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI LLARQVGVPS IVVFMNKCDM VDDEELLELV ELEIRDLLNT YEFPGDDIPI IKGSALQALE NAEDEEKTKC IWELLQAMDD YIPAPERDID KPFLMPIEDV FSISGRGTVV TGRVERGKVR VQDEIEIVGL TDTRKTVVTG VEMFRKILDE GEAGDNVGVL LRGIKKDDVE RGQVLAKPGS ITPHRKFKCE AYILTKEEGG RHTPFFSGYR PQFYFRTTDV TGVITLAEGV EMVMPGDNIS CDVDLIQPIA MEQGLRFAIR EGGRTVGAGV VTEIVE //