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Database: UniProt/SWISS-PROT
Entry: EFTU_HISS2
LinkDB: EFTU_HISS2
Original site: EFTU_HISS2 
ID   EFTU_HISS2              Reviewed;         394 AA.
AC   B0UV21;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   05-DEC-2018, entry version 68.
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=HSM_0063, HSM_1806;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D.,
RA   Gillaspy A.F., Carson M., Gipson J., Gipson M., Bruce D., Detter J.C.,
RA   Han C.S., Land M., Tapia R., Thompson L.S., Orvis J., Zaitshik J.,
RA   Barnes G., Brettin T.S., Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) 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; CP000947; ACA31592.1; -; Genomic_DNA.
DR   EMBL; CP000947; ACA32285.1; -; Genomic_DNA.
DR   RefSeq; WP_011608348.1; NC_010519.1.
DR   ProteinModelPortal; B0UV21; -.
DR   SMR; B0UV21; -.
DR   PRIDE; B0UV21; -.
DR   EnsemblBacteria; ACA31592; ACA31592; HSM_1806.
DR   EnsemblBacteria; ACA32285; ACA32285; HSM_0063.
DR   GeneID; 31488114; -.
DR   KEGG; hsm:HSM_0063; -.
DR   KEGG; hsm:HSM_1806; -.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   BioCyc; HSOM228400:G1GB8-1892-MONOMER; -.
DR   BioCyc; HSOM228400:G1GB8-63-MONOMER; -.
DR   Proteomes; UP000008543; 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    394       Elongation factor Tu.
FT                                /FTId=PRO_1000076100.
FT   DOMAIN       10    204       tr-type G.
FT   NP_BIND      19     26       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND      81     85       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND     136    139       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   REGION       19     26       G1. {ECO:0000250}.
FT   REGION       60     64       G2. {ECO:0000250}.
FT   REGION       81     84       G3. {ECO:0000250}.
FT   REGION      136    139       G4. {ECO:0000250}.
FT   REGION      174    176       G5. {ECO:0000250}.
SQ   SEQUENCE   394 AA;  43386 MW;  066D3F62731942B4 CRC64;
     MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLSKHF GGAARAFDQI DNAPEEKARG
     ITINTSHVEY DTATRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
     LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALQALN
     GVAEWEEKIL ELASHLDNYI PEPERAIDQP FLLPIEDVFS ISGRGTVVTG RVERGIIRTG
     EEVEIVGIKE TTKTTVTGVE MFRKLLDEGR AGENIGALLR GTKREEIERG QVLAKPGSIT
     PHTDFESEVY VLSKEEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMT
     VSLIHPIAMD QGLRFAIREG GRTVGAGVVA KIIK
//
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