EFTS_CLOBM
ID EFTS_CLOBM Reviewed; 307 AA.
AC B1KWM4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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}; OrderedLocusNames=CLK_1811;
OS Clostridium botulinum (strain Loch Maree / Type A3).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498214;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Loch Maree / Type A3;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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; CP000962; ACA54384.1; -; Genomic_DNA.
DR RefSeq; WP_012342498.1; NC_010520.1.
DR AlphaFoldDB; B1KWM4; -.
DR SMR; B1KWM4; -.
DR EnsemblBacteria; ACA54384; ACA54384; CLK_1811.
DR KEGG; cbl:CLK_1811; -.
DR HOGENOM; CLU_047155_0_0_9; -.
DR OMA; DAGMMDC; -.
DR Proteomes; UP000000722; 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; 3.
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.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; Protein biosynthesis.
FT CHAIN 1..307
FT /note="Elongation factor Ts"
FT /id="PRO_1000116717"
FT REGION 80..83
FT /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ SEQUENCE 307 AA; 34226 MW; C70CD2018A3FE333 CRC64;
MISAKMVKDL REKTGAGMMD CKKALTECDG DLEKAVEVLR EKGLAAAAKK SGRVAAEGIV
STYISEDMKN GSIVEFNCET DFVSVNELFV ELANNLSKQA AFSNVSTAEE LLEEKYIADE
SKLVKDVITE LIAKLGENMN LRRIAKLSVD KGVIKSYIHG GGRIGVLVKL ACEKEDAKLA
EIAKDVAMQV AATNPLFLNR DGVDTDTLEK EKEIYRVQAL NEGKPEKVVE KMVMGRINKY
YKENCLVEQL WVKNGDYTIT KYLQEQSKEI GADITVEAFV RYEKGEGIEK KEEDFAEEVQ
RQMNQGK