EFTS_BRUME
ID EFTS_BRUME Reviewed; 305 AA.
AC P64048; Q8YHH5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=BMEI0824;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL52005.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008917; AAL52005.1; ALT_INIT; Genomic_DNA.
DR PIR; AB3355; AB3355.
DR RefSeq; WP_002964288.1; NZ_GG703780.1.
DR AlphaFoldDB; P64048; -.
DR SMR; P64048; -.
DR STRING; 224914.BMEI0824; -.
DR EnsemblBacteria; AAL52005; AAL52005; BMEI0824.
DR GeneID; 45124535; -.
DR GeneID; 55590842; -.
DR KEGG; bme:BMEI0824; -.
DR PATRIC; fig|224914.52.peg.621; -.
DR eggNOG; COG0264; Bacteria.
DR OMA; DAGMMDC; -.
DR PhylomeDB; P64048; -.
DR Proteomes; UP000000419; Chromosome I.
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; PS01127; EF_TS_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; Protein biosynthesis.
FT CHAIN 1..305
FT /note="Elongation factor Ts"
FT /id="PRO_0000161090"
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 305 AA; 31491 MW; 6E7660A97411A242 CRC64;
MSISASLVKE LRDLTGAGMM DCKAALAATE GKIEAAVDWL RAKGIAKADK KAGRTAAEGL
VGVAASGNKA VVVEVNSETD FVARNDAFQE LVRKIAQAAL STDGSSEAVA NANVDGKTVT
EAAKDAVATI GENISFRRSA ALSVPQGVVA TYIHNGVADG LGKLGVLVAI ETAGDAEAAQ
AFGRQVAMHV AAVNPLALTS ADVNPEAAER EKAIFIDQAR QSGKPDNIIE KMVEGRMRKF
YEEVVLLSQA FVINPDLTVE AALKDAEKAI GAPAKITGFA RIALGEGIEK EESDFAAEVA
AAAKG