GenomeNet

Database: UniProt/SWISS-PROT
Entry: EFTU_BACLD
LinkDB: EFTU_BACLD
Original site: EFTU_BACLD 
ID   EFTU_BACLD              Reviewed;         396 AA.
AC   Q65PA9; Q62ZP8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   05-DEC-2018, entry version 103.
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};
GN   OrderedLocusNames=BLi00131, BL01055;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC
OS   12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL
RC   NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H.,
RA   Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R.,
RA   Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an
RT   organism with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL
RC   NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G.,
RA   Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L.,
RA   Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N.,
RA   Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
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; CP000002; AAU21760.1; -; Genomic_DNA.
DR   EMBL; AE017333; AAU39105.1; -; Genomic_DNA.
DR   RefSeq; WP_003178321.1; NC_006322.1.
DR   ProteinModelPortal; Q65PA9; -.
DR   SMR; Q65PA9; -.
DR   STRING; 279010.BLi00131; -.
DR   PRIDE; Q65PA9; -.
DR   EnsemblBacteria; AAU21760; AAU21760; BL01055.
DR   EnsemblBacteria; AAU39105; AAU39105; BLi00131.
DR   GeneID; 3029278; -.
DR   KEGG; bld:BLi00131; -.
DR   KEGG; bli:BL01055; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   BioCyc; BLIC279010:BLI_RS00660-MONOMER; -.
DR   Proteomes; UP000000606; 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; Cytoplasm; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    396       Elongation factor Tu.
FT                                /FTId=PRO_1000015609.
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;  43653 MW;  F512AC058FB81D2D CRC64;
     MAKEKFDRSK SHANIGTIGH VDHGKTTLTA AITTVLHKKS GKGTAMAYDQ IDGAPEERER
     GITISTAHVE YETDNRHYAH VDCPGHADYV KNMITGAAQM DGAILVVSAA DGPMPQTREH
     ILLSRNVGVP YIVVFLNKCD MVDDEELLEL VEMEVRDLLS EYEFPGDDVP VIKGSALKAL
     EGDAQYEEKI FELMAAVDEY IPTPERETDK PFMMPVEDVF SITGRGTVAT GRVERGQVKV
     GDEVEIIGLQ EENKKTTVTG VEMFRKLLDY AEAGDNIGAL LRGVSREEIQ RGQVLAQPGT
     ITPHKKFKAE VYVLSKEEGG RHTPFFSNYR PQFYFRTTDV TGIIQLPEGV EMVMPGDNIE
     MTVELISTIA IEDGTRFSIR EGGRTVGSGV VSSIIE
//
DBGET integrated database retrieval system