EFTS_BACC7
ID EFTS_BACC7 Reviewed; 295 AA.
AC B7HLF9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Elongation factor Ts {ECO:0000255|HAMAP-Rule:MF_00050};
DE Short=EF-Ts {ECO:0000255|HAMAP-Rule:MF_00050};
GN Name=tsf {ECO:0000255|HAMAP-Rule:MF_00050};
GN OrderedLocusNames=BCAH187_A3873;
OS Bacillus cereus (strain AH187).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Associates with the EF-Tu.GDP complex and induces the
CC exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-
CC Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_00050}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00050}.
CC -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC Rule:MF_00050}.
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DR EMBL; CP001177; ACJ82163.1; -; Genomic_DNA.
DR RefSeq; WP_001018580.1; NC_011658.1.
DR AlphaFoldDB; B7HLF9; -.
DR SMR; B7HLF9; -.
DR EnsemblBacteria; ACJ82163; ACJ82163; BCAH187_A3873.
DR GeneID; 59155677; -.
DR KEGG; bcr:BCAH187_A3873; -.
DR HOGENOM; CLU_047155_0_2_9; -.
DR OMA; DAGMMDC; -.
DR OrthoDB; 1405357at2; -.
DR Proteomes; UP000002214; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.479.20; -; 2.
DR HAMAP; MF_00050; EF_Ts; 1.
DR InterPro; IPR036402; EF-Ts_dimer_sf.
DR InterPro; IPR001816; Transl_elong_EFTs/EF1B.
DR InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer.
DR InterPro; IPR018101; Transl_elong_Ts_CS.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11741; PTHR11741; 1.
DR Pfam; PF00889; EF_TS; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54713; SSF54713; 2.
DR TIGRFAMs; TIGR00116; tsf; 1.
DR PROSITE; PS01126; EF_TS_1; 1.
DR PROSITE; PS01127; EF_TS_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; Protein biosynthesis.
FT CHAIN 1..295
FT /note="Elongation factor Ts"
FT /id="PRO_1000116691"
FT REGION 79..82
FT /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ SEQUENCE 295 AA; 32463 MW; 558A2197A0AE4A85 CRC64;
MAITAQMVKE LREKTGAGMM DCKKALTETN GDMEKAIDFL REKGIAKAAK KADRIAAEGL
TFIETNGNDG LILELNSETD FVAKNEGFQT LIKELAAHLL AKKPANVEEA MAQTMENGKK
VEEHINEAIA KIGEKLTLRR FEIVSKTDAD AFGAYLHMGG RIGVLTVLEG STDEAAAKDV
AMHIAAVNPK YIDRDAVTAE EVEHERQVLT QQALNEGKPE KIVAKMVEGR LGKFFEEICL
LDQAFVKNPD MKVRQFVESK GATLKGFVRY AVGEGIEKRE DNFAEEVMNQ VKGSN