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Database: UniProt/TrEMBL
Entry: A0A0H3DWS6_EDWTF
LinkDB: A0A0H3DWS6_EDWTF
Original site: A0A0H3DWS6_EDWTF 
ID   A0A0H3DWS6_EDWTF        Unreviewed;       394 AA.
AC   A0A0H3DWS6;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   28-MAR-2018, entry version 16.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|HAMAP-Rule:MF_00118, ECO:0000256|RuleBase:RU004061};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=ETAF_0141 {ECO:0000313|EMBL:ADM40264.1}, ETAF_2923
GN   {ECO:0000313|EMBL:ADM43025.1};
OS   Edwardsiella tarda (strain FL6-60).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=718251 {ECO:0000313|EMBL:ADM43025.1, ECO:0000313|Proteomes:UP000002230};
RN   [1] {ECO:0000313|Proteomes:UP000002230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FL6-60 {ECO:0000313|Proteomes:UP000002230};
RA   van Soest J.J., Henkel C.V., Jansen H.J., van den Hondel C.A.M.J.J.,
RA   Bloemberg G.V., Meijer A.H., Spaink H.P.;
RT   "Genome comparisons of Edwardsiella bacteria analysed using deep
RT   sequencing technology.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADM43025.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FL6-60 {ECO:0000313|EMBL:ADM43025.1};
RX   PubMed=22003892; DOI=10.1186/1471-2172-12-58;
RA   van Soest J.J., Stockhammer O.W., Ordas A., Bloemberg G.V.,
RA   Spaink H.P., Meijer A.H.;
RT   "Comparison of static immersion and intravenous injection systems for
RT   exposure of zebrafish embryos to the natural pathogen Edwardsiella
RT   tarda.";
RL   BMC Immunol. 12:58-58(2011).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00118}.
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DR   EMBL; CP002154; ADM40264.1; -; Genomic_DNA.
DR   EMBL; CP002154; ADM43025.1; -; Genomic_DNA.
DR   RefSeq; WP_012847048.1; NC_017309.1.
DR   ProteinModelPortal; A0A0H3DWS6; -.
DR   EnsemblBacteria; ADM40264; ADM40264; ETAF_0141.
DR   EnsemblBacteria; ADM43025; ADM43025; ETAF_2923.
DR   GeneID; 7961417; -.
DR   KEGG; etd:ETAF_0141; -.
DR   KEGG; etd:ETAF_2923; -.
DR   PATRIC; fig|718251.5.peg.141; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   Proteomes; UP000002230; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd03697; EFTU_II; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; TF_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00485; EF-Tu; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002230};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ADM43025.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   DOMAIN       10    204       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      19     26       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND      81     85       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
FT   NP_BIND     136    139       GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
SQ   SEQUENCE   394 AA;  43289 MW;  55AEC4990BDA0F7B CRC64;
     MSKEKFERSK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGSARAFDQI DNAPEEKARG
     ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
     LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPV IRGSALKALE
     GEAEWEAKII ELAETLDSYI PEPERDIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG
     DEVEIVGIKA TTKTTCTGVE MFRKLLDEGR AGENVGVLLR GTKRDEIERG QVLAKPGSIT
     PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV
     VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVIE
//
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