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Database: UniProt/SWISS-PROT
Entry: EFTU_BACSK
LinkDB: EFTU_BACSK
Original site: EFTU_BACSK 
ID   EFTU_BACSK              Reviewed;         396 AA.
AC   Q5WLR4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   28-FEB-2018, entry version 93.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=ABC0148;
OS   Bacillus clausii (strain KSM-K16).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii
RT   KSM-K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00118}.
DR   EMBL; AP006627; BAD62691.1; -; Genomic_DNA.
DR   RefSeq; WP_011245012.1; NC_006582.1.
DR   ProteinModelPortal; Q5WLR4; -.
DR   SMR; Q5WLR4; -.
DR   STRING; 66692.ABC0148; -.
DR   PRIDE; Q5WLR4; -.
DR   EnsemblBacteria; BAD62691; BAD62691; ABC0148.
DR   GeneID; 34046821; -.
DR   KEGG; bcl:ABC0148; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   BioCyc; BCLA66692:G1G25-173-MONOMER; -.
DR   Proteomes; UP000001168; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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; Cytoplasm; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    396       Elongation factor Tu.
FT                                /FTId=PRO_1000015610.
FT   DOMAIN       10    205       tr-type G.
FT   NP_BIND      19     26       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND      82     86       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND     137    140       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   REGION       19     26       G1. {ECO:0000250}.
FT   REGION       61     65       G2. {ECO:0000250}.
FT   REGION       82     85       G3. {ECO:0000250}.
FT   REGION      137    140       G4. {ECO:0000250}.
FT   REGION      175    177       G5. {ECO:0000250}.
SQ   SEQUENCE   396 AA;  43433 MW;  1E0E4707785502AC CRC64;
     MAKEKFDRSK THANIGTIGH VDHGKTTLTA AITTVLAKRS GKGQAMAYDA IDGAPEERER
     GITISTAHVE YETDSRHYAH VDCPGHADYV KNMITGAAQM DGGILVVSAA DGPMPQTREH
     ILLSRNVGVP YLVVFLNKCD MVDDEELLEL VEMEVRDLLS EYDFPGDDVP VIQGSALKAL
     QGEAEWEEKI IELMNAVDEY IPTPERDKDK PFMMPVEDVF SITGRGTVAT GRVERGQLNV
     GDTVEILGIN EEKKSTTVTG VEMFRKLLDY AEAGDNIGAL LRGVSREEIQ RGQVLAKPGT
     ITPHTKFTAE VYVLSKDEGG RHTPFFSNYR PQFYFRTTDV TGVVHLPEGT EMVMPGDNTE
     MTVELIAPIA IEEGTRFSIR EGGRTVGSGV VSTITE
//
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