EFTS_ANAPZ
ID EFTS_ANAPZ Reviewed; 287 AA.
AC Q2GKU8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, 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}; OrderedLocusNames=APH_0398;
OS Anaplasma phagocytophilum (strain HZ).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma; phagocytophilum group.
OX NCBI_TaxID=212042;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ;
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
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; CP000235; ABD44036.1; -; Genomic_DNA.
DR RefSeq; WP_011450526.1; NC_007797.1.
DR AlphaFoldDB; Q2GKU8; -.
DR SMR; Q2GKU8; -.
DR STRING; 212042.APH_0398; -.
DR PRIDE; Q2GKU8; -.
DR EnsemblBacteria; ABD44036; ABD44036; APH_0398.
DR GeneID; 56368526; -.
DR KEGG; aph:APH_0398; -.
DR eggNOG; COG0264; Bacteria.
DR HOGENOM; CLU_047155_2_0_5; -.
DR OMA; DAGMMDC; -.
DR OrthoDB; 1405357at2; -.
DR Proteomes; UP000001943; 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; 1.
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..287
FT /note="Elongation factor Ts"
FT /id="PRO_0000241460"
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 287 AA; 30802 MW; 8F7B2BD683299C87 CRC64;
MKIDVEVIKE LRQITGAGIG DCKEALESCS GDMDKAREYL REKGLSKAYK KSHRDVADGL
VAVFAEGDVG AILKLGSETD FVARNEKFRS LALGLVRGLY GYGVEDLEGF SASSYDGSRV
ADEIVAAAAV LGENVVLSGV GFVKLSGPGV IGSYVHGMVS EGLGKAAALV VLEGGPHSDE
LASFAKQLAM HIVAAKPEAL SIDTLSSDVV DRERELVARQ VEALGKPDSV AQKIIEGRMQ
KFFEEMVLLE QVFVMDGQTK IRDLLVQKGQ SLKHEIRIAA YRLFAIA