ID   EFTS_ZYMMO              Reviewed;         307 AA.
AC   Q9X5E8; Q5NND1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Elongation factor Ts;
DE            Short=EF-Ts;
GN   Name=tsf; OrderedLocusNames=ZMO1155;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RA   Lee H.J., Kang H.S.;
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
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; AF124757; AAD29655.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV89779.1; -; Genomic_DNA.
DR   RefSeq; WP_011240982.1; NZ_CP035711.1.
DR   AlphaFoldDB; Q9X5E8; -.
DR   SMR; Q9X5E8; -.
DR   STRING; 264203.ZMO1155; -.
DR   EnsemblBacteria; AAV89779; AAV89779; ZMO1155.
DR   GeneID; 58026930; -.
DR   KEGG; zmo:ZMO1155; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_2_0_5; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000001173; 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; 1.
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_0000161242"
FT   REGION          80..83
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        91
FT                   /note="D -> A (in Ref. 1; AAD29655)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        134
FT                   /note="E -> K (in Ref. 1; AAD29655)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        156
FT                   /note="H -> Y (in Ref. 1; AAD29655)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   307 AA;  32142 MW;  1C99C51C1F884B2F CRC64;
     MAEITAAAVK ALRERTGAGM MDCKKALNEA NGEMEAAVDW LRAKGLAAAA KKSGRQAAEG
     LVGVMIDGTK GAVLEVNSET DFVAKNEKFQ DFVKGVTALV LEHGSDIDTL SKAPHPAGGS
     VNDVLTANIA TIGENQALRR AALLEVENGV VVPYIHNQVA PGVGKIGVLV ALESEAPSDF
     LESLGKQIAM HVAAATPLAL DEDSLDDAAV ERERAIAQEK AAESGKPAEI VTRMVEGAVA
     KYRKENALLS QIFVVDGKTR VSDVVSKAAK ETGKPITLKQ FVRFQLGEGI EKQETDFAAE
     VAAAAGV