ID EFTU_PSYCK Reviewed; 396 AA. AC Q1Q8P2; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 27-MAR-2024, entry version 105. DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118}; GN Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=Pcryo_0425; GN and GN Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=Pcryo_2184; OS Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378 OS / K5). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Psychrobacter. OX NCBI_TaxID=335284; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., RA Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Richardson P.; RT "Complete sequence of chromosome of Psychrobacter cryohalolentis K5."; RL Submitted (MAR-2006) 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:0000255|HAMAP-Rule:MF_00118}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-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; CP000323; ABE74208.1; -; Genomic_DNA. DR EMBL; CP000323; ABE75961.1; -; Genomic_DNA. DR RefSeq; WP_011512793.1; NC_007969.1. DR AlphaFoldDB; Q1Q8P2; -. DR SMR; Q1Q8P2; -. DR STRING; 335284.Pcryo_0425; -. DR KEGG; pcr:Pcryo_0425; -. DR KEGG; pcr:Pcryo_2184; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_6; -. DR Proteomes; UP000002425; 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; Elongation factor; GTP-binding; Nucleotide-binding; KW Protein biosynthesis. FT CHAIN 1..396 FT /note="Elongation factor Tu" FT /id="PRO_0000337480" FT DOMAIN 10..206 FT /note="tr-type G" FT REGION 19..26 FT /note="G1" FT /evidence="ECO:0000250" FT REGION 60..64 FT /note="G2" FT /evidence="ECO:0000250" FT REGION 81..84 FT /note="G3" FT /evidence="ECO:0000250" FT REGION 136..139 FT /note="G4" FT /evidence="ECO:0000250" FT REGION 174..176 FT /note="G5" FT /evidence="ECO:0000250" FT BINDING 19..26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT BINDING 81..85 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT BINDING 136..139 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" SQ SEQUENCE 396 AA; 43076 MW; FEF19998A2389AF1 CRC64; MAKAKFERLK PHVNVGTIGH VDHGKTTLTA AIATVAAITS GGEAKDYASI DSAPEEKARG ITINTSHVEY DTPSRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSATD GPMPQTREHI LLSRQVGVPY IVVFMNKCDV VDDEELLELV EMEVRELLSD YDFPGDDTPI IHGSATEALK GSQEKYGQPA VVELLNVLDT YIPEPERDID KAFLMPIEDV FSISGRGTVV TGRVESGIVR VGDEIEIVGI RDTQKTTCTG VEMFRKLLDE GRAGENCGVL LRGTKREDVQ RGQVLAKPGS ITPHTKFDAE VYVLSKEEGG RHTPFLNGYR PQFYFRTTDV TGAIQLQDGT EMVMPGDNVE MGVELIHPIA MDKGLRFAIR EGGRTVGAGV VANVLN //