ID EFTU_DEIRA Reviewed; 405 AA.
AC Q9R342;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 138.
DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tufA {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=DR_0309;
GN and
GN Name=tufB {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=DR_2050;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC
RC 15346 / NCIMB 9279 / VKM B-1422 / R1;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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; AE000513; AAF09890.1; -; Genomic_DNA.
DR EMBL; AE000513; AAF11600.1; -; Genomic_DNA.
DR PIR; E75533; E75533.
DR RefSeq; NP_294032.1; NC_001263.1.
DR RefSeq; NP_295773.1; NC_001263.1.
DR RefSeq; WP_010886954.1; NZ_JMLF01000031.1.
DR AlphaFoldDB; Q9R342; -.
DR SMR; Q9R342; -.
DR STRING; 243230.DR_0309; -.
DR PaxDb; 243230-DR_0309; -.
DR EnsemblBacteria; AAF09890; AAF09890; DR_0309.
DR EnsemblBacteria; AAF11600; AAF11600; DR_2050.
DR GeneID; 69516541; -.
DR KEGG; dra:DR_0309; -.
DR KEGG; dra:DR_2050; -.
DR PATRIC; fig|243230.17.peg.2277; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_0; -.
DR InParanoid; Q9R342; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000002524; Chromosome I.
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; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..405
FT /note="Elongation factor Tu"
FT /id="PRO_0000091318"
FT DOMAIN 10..215
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 61..65
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 82..85
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 137..140
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 175..177
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 82..86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 137..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ SEQUENCE 405 AA; 44453 MW; AD27C0F1931F79B2 CRC64;
MAKGTFERTK PHVNIGTIGH VDHGKTTLTA AITFTAASAD PTIETLAYDQ IDKAPEEKAR
GITINTAHVE YQTETRHYSH VDCPGHADYV KNMITGAAQM DGAILVVSSA DGPMPQTREH
ILLARQVGVP YIVVFMNKVD MVDDEELLEL VEMEVRELLS KYEFPGDDLP VVKGSALRAL
EALQSNPKMA RGTDKWVDYI WELLDAVDSY IPTPERDTDK TFLMPVEDVF TITGRGTVAT
GRVERGTVKV QDEVEIVGLT DTRKTTVTGI EMHRKLLDSG MAGDNVGVLL RGVARDDVER
GQVLAKPGSI KPHTKFEASV YVLSKDEGGR HSAFFGGYRP QFYFRTTDVT GVVELQEGVE
MVMPGDNVTF TVELIKPIAM EEGLRFAIRE GGRTVGAGVV SKVLE
//
