ID G4QBT1_TAYAM Unreviewed; 396 AA. AC G4QBT1; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 24-JAN-2024, entry version 63. 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=TASI_1538 {ECO:0000313|EMBL:AEP37276.1}, TASI_1568 GN {ECO:0000313|EMBL:AEP37305.1}; OS Taylorella asinigenitalis (strain MCE3). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Taylorella. OX NCBI_TaxID=1008459 {ECO:0000313|EMBL:AEP37276.1, ECO:0000313|Proteomes:UP000009284}; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MCE3; RA Hebert L., Moumen B., Pons N., Duquesne F., Breuil M.-F., Goux D., RA Batto J.-M., Renault P., Laugier C., Petry S.; RT "Genomic characterization of the Taylorella genus."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AEP37276.1, ECO:0000313|Proteomes:UP000009284} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCE3 {ECO:0000313|EMBL:AEP37276.1, RC ECO:0000313|Proteomes:UP000009284}; RX PubMed=22235352; DOI=10.1371/journal.pone.0029953; RA Hebert L., Moumen B., Pons N., Duquesne F., Breuil M.F., Goux D., RA Batto J.M., Laugier C., Renault P., Petry S.; RT "Genomic characterization of the taylorella genus."; RL PLoS ONE 7:E29953-E29953(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; CP003059; AEP37276.1; -; Genomic_DNA. DR EMBL; CP003059; AEP37305.1; -; Genomic_DNA. DR RefSeq; WP_013521790.1; NC_016043.1. DR AlphaFoldDB; G4QBT1; -. DR STRING; 1008459.TASI_1538; -. DR GeneID; 79939810; -. DR KEGG; tas:TASI_1538; -. DR KEGG; tas:TASI_1568; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_4; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000009284; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt. 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:UP000009284}. 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 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; 43086 MW; 227B3E0184DED902 CRC64; MAKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLSKMY GGEAKDYSAI DAAPEERARG ITINTAHVEY ETATRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI LLSRQVGVPY IIVFLNKADM VDDEELLELV EMEVRELLSK YDFPGDDTPI IKGSAKLALE GDEGPLGKEA ILKLAEALDT YIPTPERAVD GTFLMPVEDV FSISGRGTVV TGRIERGVIK VGEEIEIVGI RETAKTTCTG VEMFRKLLDE GQAGDNVGLL LRGTKREDVE RGQVLAKPGT IKPHTNFSAE VYILSKEEGG RHTPFFQGYR PQFYFRTTDV TGAITLPADK EMVLPGDNVS MDVELISPIA MEEGLRFAIR EGGRTVGAGV VAKITK //