EFTU_BUCSC
ID EFTU_BUCSC Reviewed; 365 AA.
AC O31301;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 96.
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. Schlechtendalia chinensis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=118110;
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}.
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; Y12311; CAA72978.1; -; Genomic_DNA.
DR AlphaFoldDB; O31301; -.
DR SMR; O31301; -.
DR STRING; 118110.XW81_02415; -.
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_0000091299"
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; 40300 MW; 3EBFC163286BF5FC CRC64;
HVDHGKTTLT AAITTVLAKK YGGSARAFDQ IDNAPEEKAR GITINTSHVE YDTSMRHYAH
VDCPGHADYI KNMITGAAQM DGAILVVAAT DGPMPQTREH ILLGRQVGVP YIVVFLNKCD
MVDDEELLEL VEMEVRDLLT QYDFPGEKTP IIRGSALKAL EGDAVWEEKI VDLANTLDSY
IPTPERSIDQ PFLLPIEDVF SISGRGTVVT GRVERGVIKV GEEVEIVGIK VTSKTICTGV
EMFRKLLDEG RAGENVGVLL RGTKRDDIER GQVLAKPGTI TPHIKFESEV YVLSKEEGGR
HTPFFKGYRP QFYFRTTDVT GYVELPEGVE MVMPGDNIKM VVTLIHPIAM SDGLRFAIRE
GGRTV
