ID   EFTS_CAUVN              Reviewed;         312 AA.
AC   B8GWS2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=CCNA_01999;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
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; CP001340; ACL95464.1; -; Genomic_DNA.
DR   RefSeq; WP_010919788.1; NC_011916.1.
DR   RefSeq; YP_002517372.1; NC_011916.1.
DR   AlphaFoldDB; B8GWS2; -.
DR   SMR; B8GWS2; -.
DR   PRIDE; B8GWS2; -.
DR   EnsemblBacteria; ACL95464; ACL95464; CCNA_01999.
DR   GeneID; 7333327; -.
DR   KEGG; ccs:CCNA_01999; -.
DR   PATRIC; fig|565050.3.peg.1958; -.
DR   HOGENOM; CLU_047155_2_0_5; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   PhylomeDB; B8GWS2; -.
DR   Proteomes; UP000001364; 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; Reference proteome.
FT   CHAIN           1..312
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000189868"
FT   REGION          84..87
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   312 AA;  32621 MW;  E8B07BB77448BD15 CRC64;
     MAEITAALVK ELREKSGVGM MDCKKALAEN NGDIEASIDW LRAKGLSKAA KKADRAAAEG
     LVAIATAEQG AGETATAVEV NAETDFVSRN DLFQGAARQI AGAALGTDGS VDAITAAKLA
     GGETVQDHLT NLIATIGENM MVRRAAKWTV ENGVVASYIH NATAPDLGRI GVLVAVESTG
     DKAALRELGR KIAMHVAATS PLSLSPDDLD PAAIEREKAV FTEQALESGK PAAVVEKMIE
     GRIRKFLEEV VLLKQAFVMN PDQTVEQLVA ETAKTLGAPV AVKGFTRLAL GEGVEKKQDD
     FAAEVASMTG QA