EFTS_CLOB6
ID EFTS_CLOB6 Reviewed; 307 AA.
AC C3L0D2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 65.
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=CLJ_B2659;
OS Clostridium botulinum (strain 657 / Type Ba4).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=515621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=657 / Type Ba4;
RA Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum Ba4 strain 657.";
RL Submitted (MAY-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001083; ACQ54774.1; -; Genomic_DNA.
DR RefSeq; WP_003362577.1; NC_012658.1.
DR AlphaFoldDB; C3L0D2; -.
DR SMR; C3L0D2; -.
DR EnsemblBacteria; ACQ54774; ACQ54774; CLJ_B2659.
DR KEGG; cbi:CLJ_B2659; -.
DR HOGENOM; CLU_047155_0_0_9; -.
DR OMA; DAGMMDC; -.
DR Proteomes; UP000002333; 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_1000202233"
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; 34213 MW; 3ABE999EA3512C05 CRC64;
MISAKMVKDL REKTGAGMMD CKKALTECDG DLEKAVEVLR EKGLAAAAKK SGRVAAEGIV
STYISEDMKN GSIIEFNCET DFVSVNELFV ELANNLSKQA AFSNVSTAEE LLEEKYIADE
SKLVKDVITE LIAKLGENMN LRRIAKLSVD KGVITSYIHG GGRIGVIVKL ACEKEDAKLA
EIAKDVAMQV AATNPLFLNR DGVDTDTLEK EKEIYRVQAL NEGKPEKVVE KMVMGRINKY
YKENCLVEQL WVKNGDYTIT KYLQEQSKEI GADITVEAFV RYEKGEGIEK KEEDFAEEVQ
RQMNQGK