ID I0AI15_IGNAJ Unreviewed; 401 AA. AC I0AI15; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 02-SEP-2026, entry version 66. 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=tufA {ECO:0000313|EMBL:AFH48622.1}; GN Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=IALB_0910 {ECO:0000313|EMBL:AFH48622.1}; OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 / OS Mat9-16). OC Bacteria; Pseudomonadati; Ignavibacteriota; Ignavibacteria; OC Ignavibacteriales; Ignavibacteriaceae; Ignavibacterium. OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH48622.1, ECO:0000313|Proteomes:UP000007394}; RN [1] {ECO:0000313|EMBL:AFH48622.1, ECO:0000313|Proteomes:UP000007394} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16 RC {ECO:0000313|Proteomes:UP000007394}; RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185; RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J., RA Bryant D.A.; RT "Complete genome of Ignavibacterium album, a metabolically versatile, RT flagellated, facultative anaerobe from the phylum Chlorobi."; RL Front. Microbiol. 3:185-185(2012). 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; CP003418; AFH48622.1; -; Genomic_DNA. DR RefSeq; WP_014559777.1; NC_017464.1. DR AlphaFoldDB; I0AI15; -. DR STRING; 945713.IALB_0910; -. DR KEGG; ial:IALB_0910; -. DR PATRIC; fig|945713.3.peg.915; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_10; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000007394; 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|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:UP000007394}. FT DOMAIN 10..211 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 401 AA; 44255 MW; A02F161ADB0C1339 CRC64; MAKEKFDRSK PHVNVGTIGH VDHGKTTLTA AITMALAKKG LSQVRTFDSI DNAPEERERG ITIATAHVEY STEKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI LLARQVGVPR IVVFMNKIDM VDDPELIELV EVELRDLLSK YEFPGDEIPI IKGSALKALE AGQENAPVDD PRYQCIWDLM DAVDSYIPLP ERDIDKPFLM PVEDVFSITG RGTVATGRVE RGRVKLNEEV ELIGLGVHKK TVVTGIEMFR KELDEAIAGD NAGLLLRGVD KKEIERGMVL AKPGSITPHK KFEGEVYILS KDEGGRHTPF FNGYRPQFYF RTTDVTGVAQ LPEGTEMVMP GDNVRLTVEL ISEIAMEEGL RFAIREGGRT VGAGVVTKII E //