ID   EFTS_CORGL              Reviewed;         275 AA.
AC   Q8NP02;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   04-NOV-2026, entry version 127.
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};
GN   OrderedLocusNames=Cgl2025, cg2221;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC
OS   11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 /
OS   534).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 /
RC   LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 /
RC   LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
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; BA000036; BAB99418.1; -; Genomic_DNA.
DR   EMBL; BX927154; CAF20365.1; -; Genomic_DNA.
DR   RefSeq; WP_011014830.1; NC_003450.3.
DR   AlphaFoldDB; Q8NP02; -.
DR   SMR; Q8NP02; -.
DR   STRING; 196627.cg2221; -.
DR   PaxDb; 196627-cg2221; -.
DR   GeneID; 1019981; -.
DR   KEGG; cgb:cg2221; -.
DR   KEGG; cgl:Cgl2025; -.
DR   PATRIC; fig|196627.13.peg.1963; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_0_11; -.
DR   OMA; AACPYVN; -.
DR   OrthoDB; 9808348at2; -.
DR   BioCyc; CORYNE:G18NG-11617-MONOMER; -.
DR   Proteomes; UP000000582; Chromosome.
DR   AbasyAtlas; Q8NP02; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd14275; UBA_EF-Ts; 1.
DR   FunFam; 1.10.286.20:FF:000001; Elongation factor Ts; 1.
DR   FunFam; 1.10.8.10:FF:000001; Elongation factor Ts; 1.
DR   Gene3D; 1.10.286.20; -; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.479.20; Elongation factor Ts, dimerisation domain; 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   NCBIfam; TIGR00116; tsf; 1.
DR   PANTHER; PTHR11741; ELONGATION FACTOR TS; 1.
DR   PANTHER; PTHR11741:SF0; ELONGATION FACTOR TS, MITOCHONDRIAL; 1.
DR   Pfam; PF00889; EF_TS; 1.
DR   SUPFAM; SSF54713; Elongation factor Ts (EF-Ts), dimerisation domain; 1.
DR   SUPFAM; SSF46934; UBA-like; 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..275
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161112"
FT   REGION          76..79
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   275 AA;  29280 MW;  2BED6A737374B1FA CRC64;
     MANYTAADVK KLRELTGSGM LDCKKALEES AGDFDKAVEI LRVKGAKDVG KRAERNATEG
     LVAVSGNTMV EVNSETDFVA KNSDFKEFAA KVADAAAAAK ANSQEELAAV DVDGQTADAA
     LQEFSAKIGE KLELRRAVTL EGDKTAVYLH QRSADLPPAV GVLVAFTGEG EAAEAAARQA
     AMQIAALKAS YLTREDVPAE IIEKERSIAE QITREEGKPE QAIPKIVEGR LNGFYKENVL
     LEQSSVADSK KTVKALLDEA GVTVTSFARF EVGQA
//