EFTU_THENN
ID EFTU_THENN Reviewed; 400 AA.
AC B9K884;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=CTN_0991;
OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=309803;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA Kim J.J., Park K.J., Lee S.Y.;
RT "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT neapolitana.";
RL Submitted (NOV-2007) 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}.
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DR EMBL; CP000916; ACM23167.1; -; Genomic_DNA.
DR RefSeq; WP_015919484.1; NC_011978.1.
DR PDB; 5W75; X-ray; 2.30 A; A/B/C/D=9-400.
DR PDBsum; 5W75; -.
DR AlphaFoldDB; B9K884; -.
DR SMR; B9K884; -.
DR STRING; 309803.CTN_0991; -.
DR EnsemblBacteria; ACM23167; ACM23167; CTN_0991.
DR KEGG; tna:CTN_0991; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_0; -.
DR OMA; EGDKEWG; -.
DR Proteomes; UP000000445; 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 Gene3D; 3.40.50.300; -; 1.
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 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00485; EF-Tu; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..400
FT /note="Elongation factor Tu"
FT /id="PRO_1000201420"
FT DOMAIN 10..208
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"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:5W75"
FT HELIX 25..37
FT /evidence="ECO:0007829|PDB:5W75"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:5W75"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:5W75"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:5W75"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:5W75"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:5W75"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:5W75"
FT HELIX 144..160
FT /evidence="ECO:0007829|PDB:5W75"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:5W75"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:5W75"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:5W75"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:5W75"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:5W75"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 257..266
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 306..316
FT /evidence="ECO:0007829|PDB:5W75"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 341..348
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 362..374
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:5W75"
FT STRAND 388..398
FT /evidence="ECO:0007829|PDB:5W75"
SQ SEQUENCE 400 AA; 44555 MW; 9CE18CDAB8A86A50 CRC64;
MAKEKFVRTK PHVNVGTIGH IDHGKSTLTA AITKYLSLKG LAQYVPYDQI DKAPEEKARG
ITINITHVEY ETEKRHYAHI DCPGHADYIK NMITGAAQMD GAILVVAATD GPMPQTREHV
LLARQVEVPY MIVFINKTDM VDDPELIELV EMEVRDLLSQ YEYPGDEVPV IKGSALKALE
APDDPNHEAY KPIQELLDAM DNYIPDPQRD VDKPFLMPIE DVFSITGRGT VVTGRIERGR
IRPGDEVEII GLSYEIRKTV VTSVEMFRKE LDEGIAGDNV GCLLRGIDKD EVERGQVLAA
PGSIKPHKRF KAEVYVLKKE EGGRHTPFTK GYKPQFYIRT ADVTGEIVGL PEGVEMVMPG
DHVEMEIELI YPVAIEKGQR FAIREGGRTV GAGVVTEVIE
