ID E6NSX5_HELPQ Unreviewed; 399 AA. AC E6NSX5; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAR-2024, entry version 65. 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 ECO:0000313|EMBL:BAJ60241.1}; GN OrderedLocusNames=HPF57_1167 {ECO:0000313|EMBL:BAJ60241.1}; OS Helicobacter pylori (strain F57). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=866346 {ECO:0000313|EMBL:BAJ60241.1, ECO:0000313|Proteomes:UP000008082}; RN [1] {ECO:0000313|EMBL:BAJ60241.1, ECO:0000313|Proteomes:UP000008082} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F57 {ECO:0000313|EMBL:BAJ60241.1, RC ECO:0000313|Proteomes:UP000008082}; RX PubMed=21575176; DOI=10.1186/1471-2180-11-104; RA Kawai M., Furuta Y., Yahara K., Tsuru T., Oshima K., Handa N., RA Takahashi N., Yoshida M., Azuma T., Hattori M., Uchiyama I., Kobayashi I.; RT "Evolution in an oncogenic bacterial species with extreme genome RT plasticity: Helicobacter pylori East Asian genomes."; RL BMC Microbiol. 11:104-104(2011). RN [2] {ECO:0000313|EMBL:BAJ60241.1, ECO:0000313|Proteomes:UP000008082} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F57 {ECO:0000313|EMBL:BAJ60241.1, RC ECO:0000313|Proteomes:UP000008082}; RX PubMed=21212362; DOI=10.1073/pnas.1012579108; RA Furuta Y., Kawai M., Yahara K., Takahashi N., Handa N., Tsuru T., RA Oshima K., Yoshida M., Azuma T., Hattori M., Uchiyama I., Kobayashi I.; RT "Birth and death of genes linked to chromosomal inversion."; RL Proc. Natl. Acad. Sci. U.S.A. 108:1501-1506(2011). 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; AP011945; BAJ60241.1; -; Genomic_DNA. DR RefSeq; WP_001040578.1; NC_017367.1. DR AlphaFoldDB; E6NSX5; -. DR SMR; E6NSX5; -. DR KEGG; hex:HPF57_1167; -. DR PATRIC; fig|866346.4.peg.1253; -. DR HOGENOM; CLU_007265_0_1_7; -. DR Proteomes; UP000008082; 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}. FT DOMAIN 10..209 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 399 AA; 43622 MW; 1D5A3C0F0BDA3B6B CRC64; MAKEKFNRTK PHVNIGTIGH VDHGKTTLSA AISAVLSLKG LAEMKDYDNI DNAPEEKERG ITIATSHIEY ETENRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI LLSRQVGVPH IVVFLNKQDM VDDQELLELV EMEVRELLSA YEFPGDDTPI VAGSALRALE EAKAGNVGEW GEKVLKLMAE VDAYIPTPER DTEKTFLMPV EDVFSIAGRG TVVTGRIERG VVKVGDEVEI VGIRATQKTT VTGVEMFRKE LEKGEAGDNV GVLLRGTKKE EVERGMVLCK PGSITPHKKF EGEIYVLSKE EGGRHTPFFT NYRPQFYVRT TDVTGSITLP EGVEMVMPGD NVKITVELIS PVALELGTKF AIREGGRTVG AGVVSNIIE //