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EFTS_GLAP5
ID   EFTS_GLAP5              Reviewed;         283 AA.
AC   B8F3R8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=HAPS_0282;
OS   Glaesserella parasuis serovar 5 (strain SH0165) (Haemophilus parasuis).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Glaesserella.
OX   NCBI_TaxID=557723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH0165;
RX   PubMed=19074396; DOI=10.1128/jb.01682-08;
RA   Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R.,
RA   Jin M., Jin Q., Chen H.;
RT   "Complete genome sequence of Haemophilus parasuis SH0165.";
RL   J. Bacteriol. 191:1359-1360(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}.
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DR   EMBL; CP001321; ACL31970.1; -; Genomic_DNA.
DR   RefSeq; WP_012621652.1; NC_011852.1.
DR   AlphaFoldDB; B8F3R8; -.
DR   SMR; B8F3R8; -.
DR   STRING; 557723.HAPS_0282; -.
DR   EnsemblBacteria; ACL31970; ACL31970; HAPS_0282.
DR   GeneID; 66618715; -.
DR   KEGG; hap:HAPS_0282; -.
DR   PATRIC; fig|557723.8.peg.289; -.
DR   HOGENOM; CLU_047155_0_2_6; -.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000006743; 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; 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..283
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000117582"
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   283 AA;  30088 MW;  EFFBBB68683B238A CRC64;
     MAEITAALVK ELRERTGAGM MECKKALVEA NGDIELAIDN MRKSGQAKAA KKAGRVAAEG
     VILARIGAGF GVLVEMNCET DFVAKDAGFV GLANEVADYA LANKGTSIEA LQAQFEEKRA
     ALVAKIGENM NIRRVQYLEG QVIAQYLHGA KIGVLVAGQG AEEELKKVAM HVAASKPDFV
     NPEDVSAEVV AKEREIQIEI AMNSGKPKEI AEKMVEGRMA KFTGEVSLTG QPFVMDPSQT
     VGAYLKSVNA SVTNFVRLEV GEGIEKVEED FAAEVAKITG GNA
 
 
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