EFTS_COXBU
ID EFTS_COXBU Reviewed; 296 AA.
AC Q9X5U9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Elongation factor Ts;
DE Short=EF-Ts;
GN Name=tsf; OrderedLocusNames=CBU_1385;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION OF PROTEIN LEVELS.
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=10531263; DOI=10.1128/iai.67.11.6026-6033.1999;
RA Seshadri R., Hendrix L.R., Samuel J.E.;
RT "Differential expression of translational elements by life cycle variants
RT of Coxiella burnetii.";
RL Infect. Immun. 67:6026-6033(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(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 -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Up-regulated more than 4 fold in the large cell
CC variant (LCV) stage compared to the small cell variant (SCV) stage; at
CC protein level. LCVs are thought to be more metabolically active than
CC SCVs.
CC -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000305}.
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DR EMBL; AF127534; AAD33343.1; -; Genomic_DNA.
DR EMBL; AE016828; AAO90888.1; -; Genomic_DNA.
DR RefSeq; NP_820374.1; NC_002971.3.
DR RefSeq; WP_005772548.1; NZ_CDBG01000001.1.
DR AlphaFoldDB; Q9X5U9; -.
DR SMR; Q9X5U9; -.
DR STRING; 227377.CBU_1385; -.
DR DNASU; 1209291; -.
DR EnsemblBacteria; AAO90888; AAO90888; CBU_1385.
DR GeneID; 1209291; -.
DR KEGG; cbu:CBU_1385; -.
DR PATRIC; fig|227377.7.peg.1381; -.
DR eggNOG; COG0264; Bacteria.
DR HOGENOM; CLU_047155_0_2_6; -.
DR OMA; DAGMMDC; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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.
DR PROSITE; PS01127; EF_TS_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..296
FT /note="Elongation factor Ts"
FT /id="PRO_0000161113"
FT REGION 82..85
FT /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT /evidence="ECO:0000250"
SQ SEQUENCE 296 AA; 31820 MW; 52FB20668DED665A CRC64;
MTTITPIMVK ELRERTGAAV MACKKALQET NGDMEAAIDL LRKAGDAKAA KRAGKTAAEG
VIVIAISKDQ KKGFMAEVNS ETDFVARDTN FMAFASKVAE RGLAEGVSDV AATLALPIEP
NSSSTIEDER KALVNRIGEN IQIRRVASLS SDGVVGHYSH GGRIGVLLAL DVPNPELAKG
LAMHVAAFNP QAVSANQVST EFVEKEKEIF LARAQETGKP ANIIEKMVKG QVEKLLKEVS
LEGQSFVKDP EKLVGDLLKA EKAKVLAFLR FEVGEGVEKE SQNFADEVMA QVQGNR