EFTS_VIBPA
ID EFTS_VIBPA Reviewed; 281 AA.
AC Q87MD9;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=VP2317;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(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 {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; BA000031; BAC60580.1; -; Genomic_DNA.
DR RefSeq; NP_798696.1; NC_004603.1.
DR RefSeq; WP_005456729.1; NC_004603.1.
DR AlphaFoldDB; Q87MD9; -.
DR SMR; Q87MD9; -.
DR STRING; 223926.28807315; -.
DR EnsemblBacteria; BAC60580; BAC60580; BAC60580.
DR GeneID; 1189830; -.
DR KEGG; vpa:VP2317; -.
DR PATRIC; fig|223926.6.peg.2219; -.
DR eggNOG; COG0264; Bacteria.
DR HOGENOM; CLU_047155_0_2_6; -.
DR OMA; DAGMMDC; -.
DR Proteomes; UP000002493; Chromosome 1.
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.
DR PROSITE; PS01127; EF_TS_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..281
FT /note="Elongation factor Ts"
FT /id="PRO_0000161230"
FT REGION 80..83
FT /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ SEQUENCE 281 AA; 29774 MW; FE8C248507D13038 CRC64;
MATVTAALVK ELRERTGAGM MECKKALVEA NADIELAIEN MRKSGAAKAA KKAGNVAAEG
AIIIKEENGS AVLLEVNCQT DFVAKDGNFT AFAQEVAAAA LASKATVEEL QAQFEEARVA
LVAKIGENIN IRRVQYVEGT AIASYRHGEK IGVVVAGEGD AETLKHVAMH VAASKPEYVN
PEDVPADVVA KEKEVQVEIA MNEGKPAEIA EKMVVGRMKK FTGEISLTGQ AFIMEPKKTV
GEMLKEKGAS VATFVRLEVG EGIEKAEGLS FAEEVALAQK G