ID B2FQ31_STRMK Unreviewed; 396 AA. AC B2FQ31; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 27-MAR-2024, entry version 100. 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=tufB {ECO:0000313|EMBL:CAQ44461.1}; GN Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118, GN ECO:0000313|EMBL:CAQ44473.1}; GN OrderedLocusNames=Smlt0890 {ECO:0000313|EMBL:CAQ44461.1}, Smlt0904 GN {ECO:0000313|EMBL:CAQ44473.1}; OS Stenotrophomonas maltophilia (strain K279a). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group. OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ44461.1, ECO:0000313|Proteomes:UP000008840}; RN [1] {ECO:0000313|EMBL:CAQ44461.1, ECO:0000313|Proteomes:UP000008840} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K279a {ECO:0000313|EMBL:CAQ44461.1, RC ECO:0000313|Proteomes:UP000008840}; RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74; RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D., RA Parkhill J., Thomson N.R., Avison M.B.; RT "The complete genome, comparative and functional analysis of RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug RT resistance determinants."; RL Genome Biol. 9:R74.1-R74.13(2008). 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; AM743169; CAQ44461.1; -; Genomic_DNA. DR EMBL; AM743169; CAQ44473.1; -; Genomic_DNA. DR RefSeq; WP_004154360.1; NC_010943.1. DR AlphaFoldDB; B2FQ31; -. DR EnsemblBacteria; CAQ44461; CAQ44461; Smlt0890. DR EnsemblBacteria; CAQ44473; CAQ44473; Smlt0904. DR GeneID; 61464813; -. DR KEGG; sml:Smlt0890; -. DR KEGG; sml:Smlt0904; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_6; -. DR Proteomes; UP000008840; 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:UP000008840}. 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; 42961 MW; 59550305D4492C37 CRC64; MAKGKFERTK PHVNVGTIGH VDHGKTTLTA ALTKIGAERF GGEFKDYSSI DAAPEEKARG ITISTAHVEY ESPVRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI LLSRQVGVPY IVVFLNKADM VDDAELLELV EMEVRELLSK YDFPGDDTPI IAGSARLALE GDQSDIGVPA ILKLVDALDS WIPEPERAID KPFLMPVEDV FSISGRGTVV TGRIERGVIK VGDEIEIVGI RPVQKTTVTG VEMFRKLLDQ GQAGDNAGLL LRGTKRDDVE RGQVLAKPGS IKPHTKFEGE VYVLSKDEGG RHTPFFNGYR PQFYFRTTDI TGAAALPEGV EMVMPGDNVK MVVTLINPVA MDEGLRFAIR EGGRTVGAGV VSKIIE //