ID   EFTS_ANAMF              Reviewed;         291 AA.
AC   B9KIW9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=AMF_586;
OS   Anaplasma marginale (strain Florida).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=320483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Florida;
RX   PubMed=19134224; DOI=10.1186/1471-2164-10-16;
RA   Dark M.J., Herndon D.R., Kappmeyer L.S., Gonzales M.P., Nordeen E.,
RA   Palmer G.H., Knowles D.P. Jr., Brayton K.A.;
RT   "Conservation in the face of diversity: multistrain analysis of an
RT   intracellular bacterium.";
RL   BMC Genomics 10:16-16(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; CP001079; ACM49431.1; -; Genomic_DNA.
DR   RefSeq; WP_010267861.1; NZ_AFMS01000102.1.
DR   AlphaFoldDB; B9KIW9; -.
DR   SMR; B9KIW9; -.
DR   STRING; 320483.AMF_586; -.
DR   EnsemblBacteria; ACM49431; ACM49431; AMF_586.
DR   GeneID; 7398029; -.
DR   KEGG; amf:AMF_586; -.
DR   PATRIC; fig|320483.3.peg.679; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_2_5; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000007307; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..291
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000117555"
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   291 AA;  30903 MW;  74136E7554DFC95D CRC64;
     MKVGVEAIRE LRQITGAGLG DCKEALETCS GDMEKAKVYL REKGLSKAYK KSHRDAADGL
     VAVRVEGDKG AILKLGSETD FVARNEKFRS LAAELVSSLL KHGAEDLSSF SASPYDGGSG
     VSVADEVVNA AAVLGEHIVL SGIGFLELGG PGVIGSYIHG AVGEGIGRAG ALVALEATTA
     KTEALLEFAR QLAMHIVAAK PESVSVETLS NDIVEREREI VAKQVEALGK PESVASKIVD
     GRMQKFFEDM VLLEQTFIMD GSTKIRDLLH NKGQDLGCEV RIVAYRLFSV G