ID   EFTS_CERS4              Reviewed;         298 AA.
AC   Q3J2N5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=RHOS4_13810;
GN   ORFNames=RSP_2861;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000143; ABA78949.1; -; Genomic_DNA.
DR   RefSeq; WP_002719943.1; NZ_CP030271.1.
DR   RefSeq; YP_352850.1; NC_007493.2.
DR   AlphaFoldDB; Q3J2N5; -.
DR   SMR; Q3J2N5; -.
DR   STRING; 272943.RSP_2861; -.
DR   EnsemblBacteria; ABA78949; ABA78949; RSP_2861.
DR   GeneID; 57470108; -.
DR   GeneID; 67446526; -.
DR   KEGG; rsp:RSP_2861; -.
DR   PATRIC; fig|272943.9.peg.1715; -.
DR   eggNOG; COG0264; Bacteria.
DR   OMA; DAGMMDC; -.
DR   PhylomeDB; Q3J2N5; -.
DR   Proteomes; UP000002703; Chromosome 1.
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..298
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000241516"
FT   REGION          79..82
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   298 AA;  31120 MW;  43588EB32B19BC70 CRC64;
     MAITAQMVKE LRESTGAGMM DAKKALTETD GDMEAAVDWL RTKGLAKAAK KAGRTAAEGL
     VGVCVDGGTG VAVEVNSETD FVAKNADFQS MVTGFTKAAL TVDDIEALKA ADMGGKTVET
     TLQETIAVIG ENMTLRRMAK ISGDSVAAYV HNAAADGLGK IGVLVAVKGA DNGIAKQVAM
     HIAATNPMAL SEADLDPTVV ERERTVQTQK ALEENAASAK PKPDAVIENN IIPGRMKKFL
     EENTLLGQKF VINPDLTVAE AAKQAGVEIV GFVRMAVGEG IEKEKEDFAA EVAKTLAG