ID B2KEM6_ELUMP Unreviewed; 395 AA. AC B2KEM6; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 27-MAR-2024, entry version 98. 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=Emin_1423 {ECO:0000313|EMBL:ACC98972.1}, Emin_1498 GN {ECO:0000313|EMBL:ACC99046.1}; OS Elusimicrobium minutum (strain Pei191). OC Bacteria; Elusimicrobiota; Elusimicrobia; Elusimicrobiales; OC Elusimicrobiaceae; Elusimicrobium. OX NCBI_TaxID=445932 {ECO:0000313|EMBL:ACC98972.1, ECO:0000313|Proteomes:UP000001029}; RN [1] {ECO:0000313|EMBL:ACC98972.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Pei191 {ECO:0000313|EMBL:ACC98972.1}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Pitluck S., Sun H., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., RA Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., RA Humgenholtz P., Brune A., Richardson P.; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACC98972.1, ECO:0000313|Proteomes:UP000001029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pei191 {ECO:0000313|EMBL:ACC98972.1, RC ECO:0000313|Proteomes:UP000001029}; RX PubMed=19270133; DOI=10.1128/AEM.02698-08; RA Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H., RA Lapidus A., Hugenholtz P., Brune A.; RT "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated RT representative of the phylum 'Elusimicrobia' (formerly termite group 1)."; RL Appl. Environ. Microbiol. 75:2841-2849(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; CP001055; ACC98972.1; -; Genomic_DNA. DR EMBL; CP001055; ACC99046.1; -; Genomic_DNA. DR RefSeq; WP_012415587.1; NC_010644.1. DR AlphaFoldDB; B2KEM6; -. DR STRING; 445932.Emin_1423; -. DR KEGG; emi:Emin_1423; -. DR KEGG; emi:Emin_1498; -. DR HOGENOM; CLU_007265_0_0_0; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000001029; 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; 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; 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:UP000001029}. 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 83..87 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 138..141 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" SQ SEQUENCE 395 AA; 42995 MW; 712371161150BD18 CRC64; MAKEKFVRTK PHVNVGTIGH VDHGKTTLTT ALTKVLAKEG KAKEMGYADI AKGGVVRDAS KIVTVAVSHV EYESDKRHYA HIDCPGHADY IKNMITGAAQ MDGAILVVSA QDGPMPQTRE HVLLAKQVNV PKLVVFLNKV DLADAELLDL VEMEIRDLLS KYEFDGDNTP IIRGSALKAI EGDSSPIGEP SIKALLEALD TWIPEPKRET DKPFLMAVED VFSITGRGTV ATGRIERGVV KVGDTIEIIG FRDTMNTVAT GIEMFRKLLD QGEAGDNVGV LLRGVEKNQI ERGQVLAAPK SIKPHTKFKG QVYILKKDEG GRHTPLTPGY KPQFYFRTTD VTGELKFAGD MIMPGDNAEI EVTLITPVAM EEGLRFAIRE GGRTVGAGVV TKVIE //