(data stored in ACNUC7421 zone)

SWISSPROT: EFTS_ECO27

ID   EFTS_ECO27              Reviewed;         283 AA.
AC   B7UIL5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 55.
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};
GN   OrderedLocusNames=E2348C_0175;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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}.
DR   EMBL; FM180568; CAS07723.1; -; Genomic_DNA.
DR   RefSeq; WP_000818114.1; NC_011601.1.
DR   SMR; B7UIL5; -.
DR   PRIDE; B7UIL5; -.
DR   EnsemblBacteria; CAS07723; CAS07723; E2348C_0175.
DR   KEGG; ecg:E2348C_0175; -.
DR   KO; K02357; -.
DR   OMA; DAGMMDC; -.
DR   BioCyc; ECOL574521:E2348C_RS00905-MONOMER; -.
DR   Proteomes; UP000008205; 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; -; 1.
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;
DR   PRODOM; B7UIL5.
DR   SWISS-2DPAGE; B7UIL5.
KW   Complete proteome; Cytoplasm; Elongation factor; Protein biosynthesis.
FT   CHAIN         1    283       Elongation factor Ts.
FT                                /FTId=PRO_1000117578.
FT   REGION       80     83       Involved in Mg(2+) ion dislocation from
FT                                EF-Tu. {ECO:0000255|HAMAP-Rule:MF_00050}.
SQ   SEQUENCE   283 AA;  30423 MW;  0B9D21E928A5051C CRC64;
     MAEITASLVK ELRERTGAGM MDCKKALTEA NGDIELAIEN MRKSGAIKAA KKAGNVAADG
     VIKTKIDGNY GIILEVNCQT DFVAKDAGFQ AFADKVLDAA VAGKITDVEV LKAQFEEERV
     ALVAKIGENI NIRRVAALEG DVLGSYQHGA RIGVLVAAKG ADEELVKHIA MHVAASKPEF
     IKPEDVSAEV VEKEYQVQLD IAMQSGKPKE IAEKMVEGRM KKFTGEVSLT GQPFVMEPSK
     TVGQLLKEHN AEVTGFIRFE VGEGIEKVET DFAAEVAAMS KQS
//

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