ID F2LXU4_HIPMA Unreviewed; 394 AA. AC F2LXU4; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-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 OrderedLocusNames=Hipma_1379 {ECO:0000313|EMBL:AEA34335.1}, Hipma_1392 GN {ECO:0000313|EMBL:AEA34348.1}; OS Hippea maritima (strain ATCC 700847 / DSM 10411 / MH2). OC Bacteria; Campylobacterota; Desulfurellia; Desulfurellales; Hippeaceae; OC Hippea. OX NCBI_TaxID=760142 {ECO:0000313|EMBL:AEA34335.1, ECO:0000313|Proteomes:UP000008139}; RN [1] {ECO:0000313|EMBL:AEA34335.1, ECO:0000313|Proteomes:UP000008139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700847 / DSM 10411 / MH2 RC {ECO:0000313|Proteomes:UP000008139}, and DSM 10411 RC {ECO:0000313|EMBL:AEA34335.1}; RX PubMed=21886857; RA Huntemann M., Lu M., Nolan M., Lapidus A., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., RA Liolios K., Pagani I., Ivanova N., Ovchinikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C., RA Brambilla E.M., Rohde M., Spring S., Goker M., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., RA Mavromatis K.; RT "Complete genome sequence of the thermophilic sulfur-reducer Hippea RT maritima type strain (MH(2))."; RL Stand. Genomic Sci. 4:303-311(2011). RN [2] {ECO:0000313|Proteomes:UP000008139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700847 / DSM 10411 / MH2 RC {ECO:0000313|Proteomes:UP000008139}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., RA Mikhailova N., Lu M., Detter J.C., Tapia R., Han C., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Hippea maritima DSM 10411."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. 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; CP002606; AEA34335.1; -; Genomic_DNA. DR EMBL; CP002606; AEA34348.1; -; Genomic_DNA. DR RefSeq; WP_013682367.1; NC_015318.1. DR AlphaFoldDB; F2LXU4; -. DR STRING; 760142.Hipma_1379; -. DR KEGG; hmr:Hipma_1379; -. DR KEGG; hmr:Hipma_1392; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_7; -. DR InParanoid; F2LXU4; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000008139; 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:UP000008139}. FT DOMAIN 10..204 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 394 AA; 43542 MW; A7999C34D48A9388 CRC64; MAKEKYVRSK PHVNIGTIGH VDHGKTTLTA AITKVLAEKG KAEFKDYNEI DNAPEERERG VTINTAHVEY ETDKRHYAHV DCPGHADYIK NMITGAAQMD GAILVVSAAD GPMPQTREHI LLARQVNVPY IVVFLNKTDM VDDPELIDLV EMEVRELLSK YDFPGDDVPV IRGSALKALE GDPEAKKAIE ELMDAVDEYI PTPQREADKP FLMPIEDIFS ISGRGTVVTG RVERGVLKPG EEIEIVGFGE TRKTVATSLE MFRKILDEAI AGDNVGVLLR GIKKEEVERG MVLAKPGSIT PHKKFKAQVY VLTKDEGGRH TPFFEGYRPQ FYIRTTDVTG TVHLPEGVEM VMPGDNVELT VELIAPVALE KETRFAIREG GKTVGAGVIT EILE //