EFTS_ANAMM
ID EFTS_ANAMM Reviewed; 291 AA.
AC Q5PAF7;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=AM791;
OS Anaplasma marginale (strain St. Maries).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=234826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=St. Maries;
RX PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT "Complete genome sequencing of Anaplasma marginale reveals that the surface
RT is skewed to two superfamilies of outer membrane proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:844-849(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.
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; CP000030; AAV86723.1; -; Genomic_DNA.
DR RefSeq; WP_011114433.1; NZ_AFMU01000051.1.
DR AlphaFoldDB; Q5PAF7; -.
DR SMR; Q5PAF7; -.
DR KEGG; ama:AM791; -.
DR HOGENOM; CLU_047155_0_2_5; -.
DR OMA; DAGMMDC; -.
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.
FT CHAIN 1..291
FT /note="Elongation factor Ts"
FT /id="PRO_0000241459"
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; 30889 MW; 9A9307B98530CD16 CRC64;
MKVGVEAIRE LRQITGAGLG DCKEALETCS GDMEKAKVYL REKGLSKAYK KSHRDAADGL
VAVRVEGDKG AILKLGSETD FVARNEKFRS LAAELVSSLL KHGAEDLSSF SASPYDGGSG
VSVADEVVNA AAVLGEHVVL SGIGFLELGG PGVIGSYIHG AVGEGIGRAG ALVALEATTA
KTEALLEFAR QLAMHIVAAK PESVSVETLS NDLVEREREI VAKQVEALGK PESVASKIVD
GRMQKFFEDM VLLEQTFIMD GSTKIRDLLH NKGQDLGCEV RIVAYRLFSV G