ID H2IVV6_RAHAC Unreviewed; 394 AA. AC H2IVV6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, 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=Rahaq2_0341 {ECO:0000313|EMBL:AEX50287.1}, GN Rahaq2_4250 {ECO:0000313|EMBL:AEX54011.1}; OS Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / OS NCIMB 13365 / CIP 78.65). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Rahnella. OX NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX54011.1, ECO:0000313|Proteomes:UP000009010}; RN [1] {ECO:0000313|EMBL:AEX54011.1, ECO:0000313|Proteomes:UP000009010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010}, and CIP 78.65 RC {ECO:0000313|EMBL:AEX54011.1}; RX PubMed=22582378; DOI=10.1128/JB.00380-12; RA Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S., RA Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S., RA Tapia R., Woyke T., Sobecky P.A.; RT "Complete Genome Sequence of Rahnella aquatilis CIP 78.65."; RL J. Bacteriol. 194:3020-3021(2012). RN [2] {ECO:0000313|Proteomes:UP000009010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P., RA Martinez R., Woyke T.; RT "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65."; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AEX54011.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP 78.65 {ECO:0000313|EMBL:AEX54011.1}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P., RA Martinez R., Woyke T.; RL Submitted (JAN-2012) 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; CP003244; AEX50287.1; -; Genomic_DNA. DR EMBL; CP003244; AEX54011.1; -; Genomic_DNA. DR RefSeq; WP_013573670.1; NC_016818.1. DR AlphaFoldDB; H2IVV6; -. DR STRING; 745277.Rahaq2_0341; -. DR GeneID; 61514190; -. DR KEGG; raq:Rahaq2_0341; -. DR KEGG; raq:Rahaq2_4250; -. DR PATRIC; fig|745277.3.peg.333; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_6; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000009010; 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:UP000009010}. 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; 43128 MW; 369C6B4107BEB361 CRC64; MSKEKFERNK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGSARAFDQI DNAPEEKARG ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI LLGRQVGVPY MIVFMNKCDM VDDEELLELV EMEVRELLSA YEFPGDDIPV IKGSALKALE GDATWEAKII ELAEALDSYI PLPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIVKVG EEVEIVGIKD TVKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREDIERG QVLAKPGSIK PHTKFDSEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNVNMV VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVIA //