EFTU_BUCMH
ID EFTU_BUCMH Reviewed; 365 AA.
AC O31300;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Flags: Fragment;
GN Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118};
OS Buchnera aphidicola subsp. Melaphis rhois.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=118103;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9580987; DOI=10.1093/oxfordjournals.molbev.a025958;
RA Brynnel E.U., Kurland C.G., Moran N.A., Andersson S.G.;
RT "Evolutionary rates for tuf genes in endosymbionts of aphids.";
RL Mol. Biol. Evol. 15:574-582(1998).
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; Y12310; CAA72977.1; -; Genomic_DNA.
DR AlphaFoldDB; O31300; -.
DR SMR; O31300; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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; 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 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..>365
FT /note="Elongation factor Tu"
FT /id="PRO_0000091300"
FT DOMAIN <1..185
FT /note="tr-type G"
FT BINDING <1..7
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 117..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT NON_TER 1
FT NON_TER 365
SQ SEQUENCE 365 AA; 40367 MW; 5BB369DE30E44510 CRC64;
HVDHGKTTLT AAITTVLAKK YGGSARAFDQ IDNAPEEKAR GITINTSHVE YDTSLRHYAH
VDCPGHADYI KNMITGAAQM DGAILVVAAT DGPMPQTREH ILLGRQVGVP YIVVFLNKCD
MVDDEELLEL VEMEVRDLLT QYDFPGDKTP IIRGSALKAL EGDCIWESKI IDLANILDTY
IPEPKRSIDQ PFLLPIEDVF SISGRGTVVT GRVERGIIKV GEEVEIVGIK PTSKTICTGV
EMFRKLLDEG RAGENVGVLL RGTKRDDIER GQVLSKPGTI TPHIKFESEV YVLSKEEGGR
HTPFFKGYRP QFYFRTTDVT GYVELPEGIE MVMPGDNVKM VVTLIHPIAM SDGLRFAIRE
GGRTV
