ID D8ITY3_HERSS Unreviewed; 396 AA. AC D8ITY3; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 04-NOV-2026, entry version 87. 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=tufB {ECO:0000313|EMBL:ADJ61624.1}; GN Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=Hsero_0097 {ECO:0000313|EMBL:ADJ61624.1}, Hsero_0112 GN {ECO:0000313|EMBL:ADJ61638.1}; OS Herbaspirillum seropedicae (strain SmR1). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Oxalobacteraceae; Herbaspirillum. OX NCBI_TaxID=757424 {ECO:0000313|EMBL:ADJ61624.1, ECO:0000313|Proteomes:UP000000329}; RN [1] {ECO:0000313|EMBL:ADJ61624.1, ECO:0000313|Proteomes:UP000000329} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SmR1 {ECO:0000313|EMBL:ADJ61624.1, RC ECO:0000313|Proteomes:UP000000329}; RA Pedrosa F.O., Monteiro R.A., Wassem R., Cruz L.M., Ayub R.A., Colauto N.B., RA Fernandez M.A., Fungaro M.H.P., Grisard E.C., Hungria M., Madeira H.M.F., RA Nodari R.O., Osaku C.A., Petzl-Erler M.L., Terenzi H., Vieira L.G.E., RA Almeida M.I.M., Alves L.R., Arantes O.M.N., Balsanelli E., Barcellos F.G., RA Baura V.A., Binde D.R., Campo R.J., Chubatsu L.S., Chueire L.M.O., RA Ciferri R.R., Correa L.C., da Conceicao Silva J.L., Dabul A.N.G., RA Dambros B.P., Faoro H., Favetti A., Friedermann G., Furlaneto M.C., RA Gasques L.S., Gimenes C.C.T., Gioppo N.M.R., Glienke-Blanco C., Godoy L.P., RA Guerra M.P., Karp S., Kava-Cordeiro V., Margarido V.P., Mathioni S.M., RA Menck-Soares M.A., Murace N.K., Nicolas M.F., Oliveira C.E.C., RA Pagnan N.A.B., Pamphile J.A., Patussi E.V., Pereira L.F.P., RA Pereira-Ferrari L., Pinto F.G.S., Precoma C., Prioli A.J., Prioli S.M.A.P., RA Raittz R.T., Ramos H.J.O., Ribeiro E.M.S.F., Rigo L.U., Rocha C.L.M.S.C., RA Rocha S.N., Santos K., Satori D., Silva A.G., Simao R.C.G., Soares M.A.M., RA Souza E.M., Steffens M.B.R., Steindel M., Tadra-Sfeir M.Z., Takahashi E.K., RA Torres R.A., Valle J.S., Vernal J.I., Vilas-Boas L.A., Watanabe M.A.E., RA Weiss V.A., Yates M.A., Souza E.M.; RT "The genome of Herbaspirillum seropedicae SmR1, an endophytic, nitrogen- RT fixing, plant-growth promoting beta-Proteobacteria."; RL Submitted (APR-2010) 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; CP002039; ADJ61624.1; -; Genomic_DNA. DR EMBL; CP002039; ADJ61638.1; -; Genomic_DNA. DR RefSeq; WP_008334097.1; NC_014323.1. DR AlphaFoldDB; D8ITY3; -. DR STRING; 757424.Hsero_0097; -. DR GeneID; 90162538; -. DR KEGG; hse:Hsero_0097; -. DR KEGG; hse:Hsero_0112; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_4; -. DR OMA; AACIEYQ; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000000329; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00118}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, 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:UP000000329}. FT DOMAIN 10..206 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 60..64 FT /note="G2" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT REGION 81..84 FT /note="G3" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT REGION 136..139 FT /note="G4" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01059" FT REGION 174..176 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 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; 43015 MW; 6D06D4DBDCB2BEF3 CRC64; MAKGKFERTK PHVNVGTIGH VDHGKTTLTA AIATVLSKKF GGEAKAYDQI DAAPEEKARG ITINTAHVEY ETANRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI LLSRQVGVPY IIVFLNKADM VDDAELLELV EMEVRELLSK YEFPGDDLPI VKGSAKLALE GDTGPLGEQA IMALAEALDT YIPTPERAVD GTFLMPVEDV FSISGRGTVV TGRVERGIIK VGEEIEIVGI ADTQKTTCTG VEMFRKLLDQ GQAGDNVGVL LRGTKREDVQ RGQVLAKPGS IKPHKHFTGE IYVLSKDEGG RHTPFFNNYR PQFYFRTTDV TGAIELPKDK EMVMPGDNVS ITVQLINPIA MEEGLRFAIR EGGRTVGAGV VAKIFD //