ID   EFTU_STAWA              Reviewed;         270 AA.
AC   Q93PU8;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Elongation factor Tu;
DE            Short=EF-Tu;
DE   Flags: Fragment;
GN   Name=tuf;
OS   Staphylococcus warneri.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27836 / DSM 20316 / LMG 13354 / NCTC 11044 / AW 25 / CCM 2730;
RX   PubMed=11427566; DOI=10.1128/jcm.39.7.2541-2547.2001;
RA   Martineau F., Picard F.J., Ke D., Paradis S., Roy P.H., Ouellette M.,
RA   Bergeron M.G.;
RT   "Development of a PCR assay for identification of Staphylococci at genus
RT   and species levels.";
RL   J. Clin. Microbiol. 39:2541-2547(2001).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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|PROSITE-ProRule:PRU01059}.
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DR   EMBL; AF298806; AAK70337.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93PU8; -.
DR   SMR; Q93PU8; -.
DR   STRING; 1194526.A284_10605; -.
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; cd03697; EFTU_II; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
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; 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   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 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..>270
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000091397"
FT   DOMAIN          <1..103
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         35..38
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         270
SQ   SEQUENCE   270 AA;  29727 MW;  FA12AAD4C291284E CRC64;
     GILVVSAADG PMPQTREHIL LSRNVGVPAL VVFLNKVDMV DDEELLELVE MEVRDLLSEY
     DFPGDDVPVI AGSALKALEG DEKYEEKILE LMQAVDDYIP TPERDSDKPF MMPVEDVFSI
     TGRGTVATGR VERGQIKVGE EVEIIGLHDT SKTTVTGVEM FRKLLDYAEA GDNIGALLRG
     VAREDVQRGQ VLAAPGSITP HTKFKAEVYV LSKDEGGRHT PFFSNYRPQF YFRTTDVTGV
     VQLPEGTEMV MPGDNVEMTV ELIAPIAIED