ID   EFTS_VIBCH              Reviewed;         280 AA.
AC   Q9KPV3;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Elongation factor Ts;
DE            Short=EF-Ts;
GN   Name=tsf; OrderedLocusNames=VC_2259;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000305}.
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DR   EMBL; AE003852; AAF95403.1; -; Genomic_DNA.
DR   PIR; A82100; A82100.
DR   RefSeq; NP_231890.1; NC_002505.1.
DR   RefSeq; WP_000301490.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KPV3; -.
DR   SMR; Q9KPV3; -.
DR   STRING; 243277.VC_2259; -.
DR   DNASU; 2613181; -.
DR   EnsemblBacteria; AAF95403; AAF95403; VC_2259.
DR   GeneID; 57740882; -.
DR   GeneID; 66939891; -.
DR   KEGG; vch:VC_2259; -.
DR   PATRIC; fig|243277.26.peg.2155; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_2_6; -.
DR   OMA; DAGMMDC; -.
DR   BioCyc; VCHO:VC2259-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..280
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161229"
FT   REGION          79..82
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   280 AA;  29847 MW;  5283E1B46E271665 CRC64;
     MAVTAALVKE LRERTGAGMM ECKKALVETN GDIELAIENM RKSGAAKAAK KAGNIAAEGT
     IMIKEGEGIA ALVEVNCQTD FVAKDSNFVA FANQVTDAAL ASKASVEELQ AQFEEARVAL
     VAKIGENINI RRVQYVEGEA LATYRHGDRI GVVVAGSADV ETLKHVAMHV AASRPEFLTP
     DDVPAEVVAK EREVQVGIAM NEGKSKEIAE KMVEGRMKKF TGEVSLTGQP FVMEPKKTVG
     EILAEKGATV SAFIRLEVGE GIEKQEGLSF AEEVALAQKG