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EFTS_PHOPR
ID   EFTS_PHOPR              Reviewed;         284 AA.
AC   Q6LN25;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 97.
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=PBPRA2967;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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=CAG21301.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR378672; CAG21301.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011219568.1; NC_006370.1.
DR   AlphaFoldDB; Q6LN25; -.
DR   SMR; Q6LN25; -.
DR   STRING; 298386.PBPRA2967; -.
DR   PRIDE; Q6LN25; -.
DR   EnsemblBacteria; CAG21301; CAG21301; PBPRA2967.
DR   KEGG; ppr:PBPRA2967; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_2_6; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000000593; 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; PS01127; EF_TS_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..284
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161170"
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   284 AA;  30194 MW;  8D21BBD69AFE5072 CRC64;
     MATVTAALVK ELRERTAAGM MDCKKALVEA DGDIELAIDN MRKSGAAKAA KKSGNIAAEG
     TIIIKEVDGI AAILEVNCQT DFVAKDASFL AFANEVADAA LAGRVEVAEL QAAFEEKRIA
     LVTKIGENIS IRRVEFIEGA QIGSYRHGDR IGVVVVVVAS DADQETIKQV AMHVAASKPE
     FVTPEDVPAD VVAKEKQIQI DIAIQSGKPA EIAEKMVVGR MKKFTGEVSL TGQAFIMDPA
     QTVGQMLKAK GATVTNFIRF EVGEGIEKAK EMSFAEEVAA VQKG
 
 
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