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Database: UniProt
Entry: Q6F0J5
LinkDB: Q6F0J5
Original site: Q6F0J5 
ID   EFTU_MESFL              Reviewed;         394 AA.
AC   Q6F0J5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   14-MAY-2014, entry version 69.
DE   RecName: Full=Elongation factor Tu;
DE            Short=EF-Tu;
GN   Name=tuf; OrderedLocusNames=Mfl621;
OS   Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS   (Acholeplasma florum).
OC   Bacteria; Tenericutes; Mollicutes; Entomoplasmatales;
OC   Entomoplasmataceae; Mesoplasma.
OX   NCBI_TaxID=265311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA   Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA   Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R.,
RA   Nusbaum C.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC       EF-Tu/EF-1A subfamily.
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DR   EMBL; AE017263; AAT75978.1; -; Genomic_DNA.
DR   RefSeq; YP_053862.1; NC_006055.1.
DR   ProteinModelPortal; Q6F0J5; -.
DR   SMR; Q6F0J5; 3-393.
DR   STRING; 265311.Mfl621; -.
DR   PRIDE; Q6F0J5; -.
DR   EnsemblBacteria; AAT75978; AAT75978; Mfl621.
DR   GeneID; 2898215; -.
DR   KEGG; mfl:Mfl621; -.
DR   PATRIC; 22474023; VBIMesFlo3168_0624.
DR   eggNOG; COG0050; -.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; SSYSISH; -.
DR   OrthoDB; EOG6R5C6X; -.
DR   BioCyc; MFLO265311:GHIB-640-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR000795; EF_GTP-bd_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
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; EFACTOR_GTP; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    394       Elongation factor Tu.
FT                                /FTId=PRO_1000015684.
FT   NP_BIND      19     26       GTP (By similarity).
FT   NP_BIND      81     85       GTP (By similarity).
FT   NP_BIND     136    139       GTP (By similarity).
SQ   SEQUENCE   394 AA;  42905 MW;  9749119D24B05B58 CRC64;
     MAKEAFDRSL PHVNIGTIGH VDHGKTTLTA AITKVLADKG GAEFKDYANI DNAPEERERG
     ITINTSHVEY KTENRHYAHV DCPGHADYVK NMITGAAQMD GGILVVAATD GPMPQTREHI
     LLSRQVGVPK IVVFLNKCDM VDDEEMIDLV EMEVRDLLSA YDFDGDGAPV IRGSALGALN
     GEAKWVAAIE ELMAAVDEYI PTPTRDSDKT FLMPVEDVFT ITGRGTVATG RVERGTIKVN
     EEVEIVGLVE EAKKTVVTGL EMFRKLLDFA EAGDNVGALL RGVDRESIER GQVLAKPGTI
     KPHTKLQASV YALTTEEGGR QKPFFNKYRP QFYFRTTDVT GEVILPAGTD MVMPGDNVEM
     TVELIKPIAV EDGTKFSIRE GGRTIGAGTV ISVQ
//
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