ID   EFTS_SULNB              Reviewed;         353 AA.
AC   A6Q716;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-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=SUN_0315;
OS   Sulfurovum sp. (strain NBC37-1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurovaceae; Sulfurovum; unclassified Sulfurovum.
OX   NCBI_TaxID=387093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBC37-1;
RX   PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA   Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA   Horikoshi K.;
RT   "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT   emergence of pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(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; AP009179; BAF71275.1; -; Genomic_DNA.
DR   RefSeq; WP_011980008.1; NC_009663.1.
DR   AlphaFoldDB; A6Q716; -.
DR   SMR; A6Q716; -.
DR   STRING; 387093.SUN_0315; -.
DR   EnsemblBacteria; BAF71275; BAF71275; SUN_0315.
DR   KEGG; sun:SUN_0315; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_1_7; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000006378; 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; 3.
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..353
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000006196"
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   353 AA;  38390 MW;  DCE0F3CB6820D90E CRC64;
     MANFGPKDIK KLREMTDAGM MDCKKALTEA DGDMDKAVEW LRDQGMGAAA KKAGKVAAEG
     AIGIKVEGHK AVIVEINSQT DFVAQNDKFK ALMDTVVNHA FENNLADAEA INNSTINGEP
     FADFLSQQIA IIGEKLVVRR AALIVGDETT AVNGYVHSNA QNGVIIEAKC DSAKTAEAMT
     PVLKEVAMHA AAMAPSTLSF KDFDPKFVED ETKGRIVAIE TENEELRRLG KTEKNVPQYI
     SMSQLTDEVM AAAEEALKAE LAAEGKPEKI WDKILPGKLA RFISDNTTLD QEQCLLDQKF
     VMDDSKTVFE YVQEKAKAAG GSAEIVHFVR LEVGEGIEVE EEDFAAEVAK QMA