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 01-MAY-2013, entry version 63.
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 HSSP; P49410; 1XB2.
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 ProtClustDB; PRK00049; -.
DR BioCyc; MFLO265311:GHIB-640-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:HAMAP.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:HAMAP.
DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC.
DR HAMAP; MF_00118_B; EF_Tu_B; 1; -.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR005225; Small_GTP-bd_dom.
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 InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
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; SSF50465; Elong_init_C; 1.
DR SUPFAM; SSF50447; Translat_factor; 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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