EFTS_CLOD6
ID EFTS_CLOD6 Reviewed; 303 AA.
AC Q185S9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=CD630_21390;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
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; AM180355; CAJ69024.1; -; Genomic_DNA.
DR RefSeq; WP_003424535.1; NZ_CP010905.2.
DR RefSeq; YP_001088653.1; NC_009089.1.
DR AlphaFoldDB; Q185S9; -.
DR SMR; Q185S9; -.
DR STRING; 272563.CD630_21390; -.
DR EnsemblBacteria; CAJ69024; CAJ69024; CD630_21390.
DR GeneID; 66354534; -.
DR KEGG; cdf:CD630_21390; -.
DR KEGG; pdc:CDIF630_02370; -.
DR PATRIC; fig|272563.120.peg.2259; -.
DR eggNOG; COG0264; Bacteria.
DR OMA; DAGMMDC; -.
DR PhylomeDB; Q185S9; -.
DR BioCyc; PDIF272563:G12WB-2296-MON; -.
DR Proteomes; UP000001978; 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; 2.
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; Reference proteome.
FT CHAIN 1..303
FT /note="Elongation factor Ts"
FT /id="PRO_1000006079"
FT REGION 82..85
FT /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ SEQUENCE 303 AA; 33140 MW; A957376BAF89E8D0 CRC64;
MANITAQMVK ELRESTGAGM MDCKKALQEA EGNMEKAVDL LREKGLSKAA KKAGRVAAEG
LVAIEMNDDN TVASMVEVNS ETDFVAKNED FKVFVKDAAC MALATDKEDI ASLLGETHKE
GITLQEVLNN RVAKIGEKLD FRRFAKVVTN GQVAGYIHGG GKIGVLVEME TEARDAKVLE
LGKDVAMQVA AMNPKYVSRD EVDAEYIAHE TEVLTQQALN EGKPANIVEK MVKGRLEKEL
KEVCLLEQTF VKNPDITVKQ LVADVAKAVG SDIKVVKVVR FEVGEGIQKR EENFAEEVAK
QLK