ID I3ZL31_TERRK Unreviewed; 395 AA. AC I3ZL31; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 02-SEP-2026, entry version 68. 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}; DE EC=3.6.5.3 {ECO:0000256|HAMAP-Rule:MF_00118}; GN Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=Terro_0908 {ECO:0000313|EMBL:AFL87234.1}, Terro_3738 GN {ECO:0000313|EMBL:AFL89949.1}; OS Terriglobus roseus (strain DSM 18391 / NRRL B-41598 / KBS 63). OC Bacteria; Pseudomonadati; Acidobacteriota; Terriglobia; Terriglobales; OC Acidobacteriaceae; Terriglobus. OX NCBI_TaxID=926566 {ECO:0000313|EMBL:AFL89949.1, ECO:0000313|Proteomes:UP000006056}; RN [1] {ECO:0000313|EMBL:AFL89949.1, ECO:0000313|Proteomes:UP000006056} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18391 {ECO:0000313|EMBL:AFL89949.1}, and DSM 18391 / NRRL RC B-41598 / KBS 63 {ECO:0000313|Proteomes:UP000006056}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Munk A.C.C., RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.; RT "Complete genome of Terriglobus roseus DSM 18391."; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: GTP hydrolase that promotes the GTP-dependent binding of CC aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00118}. CC -!- FUNCTION: May play an important regulatory role in cell growth and in CC the bacterial response to nutrient deprivation. CC {ECO:0000256|ARBA:ARBA00058140}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00118}; CC -!- SUBUNIT: (Microbial infection) Upon infection by bacteriophage Qbeta, CC part of the viral RNA-dependent RNA polymerase complex, the other CC subunits are the viral replicase catalytic subunit (AC P14647), host CC ribosomal protein S1 and EF-Ts. {ECO:0000256|ARBA:ARBA00064283}. CC -!- SUBUNIT: Monomer. Heterotetramer composed of two EF-Ts.EF-Tu dimer CC complexes. {ECO:0000256|ARBA:ARBA00063778}. 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; CP003379; AFL87234.1; -; Genomic_DNA. DR EMBL; CP003379; AFL89949.1; -; Genomic_DNA. DR RefSeq; WP_014784803.1; NC_018014.1. DR AlphaFoldDB; I3ZL31; -. DR STRING; 926566.Terro_0908; -. DR KEGG; trs:Terro_0908; -. DR KEGG; trs:Terro_3738; -. DR PATRIC; fig|926566.3.peg.3684; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_0; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000006056; 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:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. 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 FunFam; 2.40.30.10:FF:000001; Elongation factor Tu; 1. DR FunFam; 3.40.50.300:FF:000003; Elongation factor Tu; 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; IPR050055; EF-Tu_GTPase. 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. 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; NF000766; PRK00049.1; 1. DR NCBIfam; NF009372; PRK12735.1; 1. DR NCBIfam; NF009373; PRK12736.1; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00118}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00118}; KW Metal-binding {ECO:0000256|HAMAP-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:UP000006056}. FT DOMAIN 10..205 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT REGION 19..26 FT /note="G1" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT REGION 61..65 FT /note="G2" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT REGION 82..85 FT /note="G3" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT REGION 137..140 FT /note="G4" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT REGION 175..177 FT /note="G5" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT BINDING 19..26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 26 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 82..86 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 137..140 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" SQ SEQUENCE 395 AA; 43163 MW; CEDBB9B6792589BB CRC64; MGKEKFDRSK PHVNVGTIGH IDHGKTTLTA AITKVLSKHN PKNSFRSFDT IDNAPEERER GITIATSHVE YETANRHYAH VDCPGHADYI KNMITGAAQM DGAILVVAAT DGPMPQTKEH VLLARQVGVP YIVVFLNKCD AVEDEELIDL VEMEVRELLS KYDFPGDDVP VIRGSALGAL NGEAQWEAKI DELMDAVDKN VPQPDRLVDL PFLMPIEDIF SISGRGTVVT GRIERGKIKV GEPAQIVGFR DTQNTTVTGV EMFKKQLDEG LAGDNAGLLL RGTAKDDVER GMVLAKPGSI TPHTTFKGEI YVLSKEEGGR HTPFFDGYRP QFYFRTTDVT GSAKLPAGTE MVMPGDNIAL EITLHTPVAM EKGLRFAIRE GGRTVGAGTI SEIIK //