ID K0AZP3_GOTA9 Unreviewed; 397 AA. AC K0AZP3; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 27-MAR-2024, entry version 55. 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=tuf1 {ECO:0000313|EMBL:AFS79268.1}; GN Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118}, tuf2 GN {ECO:0000313|EMBL:AFS79282.1}; GN OrderedLocusNames=Curi_c22650 {ECO:0000313|EMBL:AFS79268.1}, GN Curi_c22790 {ECO:0000313|EMBL:AFS79282.1}; OS Gottschalkia acidurici (strain ATCC 7906 / DSM 604 / BCRC 14475 / CIP OS 104303 / KCTC 5404 / NCIMB 10678 / 9a) (Clostridium acidurici). OC Bacteria; Bacillota; Tissierellia; Tissierellales; Gottschalkiaceae; OC Gottschalkia. OX NCBI_TaxID=1128398 {ECO:0000313|EMBL:AFS79268.1, ECO:0000313|Proteomes:UP000006094}; RN [1] {ECO:0000313|EMBL:AFS79268.1, ECO:0000313|Proteomes:UP000006094} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9a {ECO:0000313|EMBL:AFS79268.1}, and ATCC 7906 / DSM 604 / RC BCRC 14475 / CIP 104303 / KCTC 5404 / NCIMB 10678 / 9a RC {ECO:0000313|Proteomes:UP000006094}; RX PubMed=23240052; DOI=10.1371/journal.pone.0051662; RA Hartwich K., Poehlein A., Daniel R.; RT "The purine-utilizing bacterium Clostridium acidurici 9a: a genome-guided RT metabolic reconsideration."; RL PLoS ONE 7:E51662-E51662(2012). 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; CP003326; AFS79268.1; -; Genomic_DNA. DR EMBL; CP003326; AFS79282.1; -; Genomic_DNA. DR RefSeq; WP_014968404.1; NC_018664.1. DR AlphaFoldDB; K0AZP3; -. DR STRING; 1128398.Curi_c22650; -. DR KEGG; cad:Curi_c22650; -. DR KEGG; cad:Curi_c22790; -. DR PATRIC; fig|1128398.3.peg.2344; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_9; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000006094; 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:UP000006094}. 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 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 397 AA; 43486 MW; 868B3C7DA3BCE40D CRC64; MGKAKFERSK PHVNIGTIGH VDHGKTTLTA AITTVLHARL GTGEGIAYDN IDKAPEERER GITISTSHVE YETENRHYAH VDCPGHADYV KNMITGAAQM DGAILVCSAA DGPMPQTREH ILLSRQVGVP TIVVFLNKAD MVNDEELIEL VEMEVRELLS EYEFDGDNTP IVVGSALKAL EDPSSEWGDK ILELMAAVDE TIPTPERDTD KAFLMPVEDI FSITGRGTVA TGKVERGVLK VQDNVEIVGI AEESRTVVCT GIEMFRKLLD DAQAGDNIGA LLRGVQREDI QRGQVLAKPG SITPHTHFEA EVYVLNKEEG GRHTPFFDGY RPQFYFRTTD VTGSIKLEEG VEMVMPGDNA KFTIELISPI AMEEGLRFAV REGGRTVGSG VISKILK //