ID   EFTS_NAUPA              Reviewed;         307 AA.
AC   B9L8B2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=NAMH_0452;
OS   Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales; Nautiliaceae;
OC   Nautilia.
OX   NCBI_TaxID=598659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1463 / DSM 18972 / AmH;
RX   PubMed=19197347; DOI=10.1371/journal.pgen.1000362;
RA   Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K.,
RA   Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.;
RT   "Adaptations to submarine hydrothermal environments exemplified by the
RT   genome of Nautilia profundicola.";
RL   PLoS Genet. 5:E1000362-E1000362(2009).
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; CP001279; ACM93497.1; -; Genomic_DNA.
DR   RefSeq; WP_015902549.1; NC_012115.1.
DR   AlphaFoldDB; B9L8B2; -.
DR   SMR; B9L8B2; -.
DR   STRING; 598659.NAMH_0452; -.
DR   EnsemblBacteria; ACM93497; ACM93497; NAMH_0452.
DR   KEGG; nam:NAMH_0452; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_0_7; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000000448; 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..307
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000117593"
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   307 AA;  33093 MW;  FBD499B5249B2CC3 CRC64;
     MANITAAMVK ALREKTGAGM MDCKKALVEA EGNEEKAVEI LRKKGLAKAA KKADRNAAEG
     RVEIYISDDY KKGSIAEVNC ETDFVAKTDE FIEFVSETVK TINVNDIADT EALNKAPFGA
     GTFEEELKVK IAKIGENIVV RRIGTIKAPE NGIVNGYIHA GGKVGVLVAA ACDSEKTCEA
     IKDTLRDIAM HIAAMKPQYL NPEAVPADVI EKEKEIAKAQ LLKEGKPEQV IDKIIPGKIK
     RFYSDVCVTE QEYVKAEKKE TVAEALSKAA KAAGGEAKLV DFIRFEVGEG LVKNACNMAD
     EVAAALS