ID   EFTS_MYCA1              Reviewed;         275 AA.
AC   A0QJ27;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   10-JUN-2026, entry version 91.
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=MAV_3743;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) 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; CP000479; ABK67396.1; -; Genomic_DNA.
DR   RefSeq; WP_011725650.1; NC_008595.1.
DR   AlphaFoldDB; A0QJ27; -.
DR   SMR; A0QJ27; -.
DR   GeneID; 75271136; -.
DR   KEGG; mav:MAV_3743; -.
DR   HOGENOM; CLU_047155_0_0_11; -.
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.
FT   CHAIN           1..275
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000006126"
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;  29142 MW;  65566296097EFCEA CRC64;
     MANFTAADVK RLRELTGAGM LDCKNALAES DGDFDKAVEA LRIKGAKDVG KRAERATAEG
     LVAAQGGALI ELNSETDFVA KNAEFQALAD QIVAAAASSK AADVDALKAA KIGDTTVEQA
     IAELSAKIGE KLELRRVAHF DGTVEAYLHR RAADLPPAVG VLVEYQGSGK DSDKEAAHAV
     ALQIAALKAR YLSRDDVPED VVASERRIAE ETAKAEGKPE QALPKIVEGR LNGFFKDAVL
     LEQPSVSDSK KTVKALLDEA GVTVTRFVRF EVGQA
//