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Database: UniProt/TrEMBL
Entry: A0A170Q036_BRASZ
LinkDB: A0A170Q036_BRASZ
Original site: A0A170Q036_BRASZ 
ID   A0A170Q036_BRASZ        Unreviewed;       396 AA.
AC   A0A170Q036;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
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   ORFNames=BF49_6228 {ECO:0000313|EMBL:CUT15148.1};
OS   Bradyrhizobium sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=376 {ECO:0000313|EMBL:CUT15148.1, ECO:0000313|Proteomes:UP000077107};
RN   [1] {ECO:0000313|EMBL:CUT15148.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BF49_genome1 {ECO:0000313|EMBL:CUT15148.1};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) 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: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; LN901633; CUT15148.1; -; Genomic_DNA.
DR   RefSeq; WP_007603012.1; NZ_LN901633.1.
DR   EnsemblBacteria; CUT15148; CUT15148; BF49_6228.
DR   GeneID; 32226262; -.
DR   KEGG; brad:BF49_6228; -.
DR   PATRIC; fig|376.36.peg.6567; -.
DR   KO; K02358; -.
DR   Proteomes; UP000077107; Chromosome i.
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.
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:UP000077107};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:CUT15148.1};
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    206       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   396 AA;  43272 MW;  D636648A00B34C48 CRC64;
     MAKAKFERNK PHCNIGTIGH VDHGKTSLTA AITKVLAEAG GATFTAYDQI DKAPEEKARG
     ITISTAHVEY ETKNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA LVVFLNKCDM VDDPELLELV ELEVRELLSK YEFPGDTIPI IKGSALAALE
     DSDKTLGHEA ILELMKQVDA YIPQPERPVD LPFLMPVEDV FSISGRGTVV TGRVERGIVK
     VGEEIEIVGL RATQKTTVTG VEMFRKLLDQ GQAGDNIGAL LRGTKREDVE RGQVLCKPGS
     VKPHTKFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGVVHLPEGT EMVMPGDNIA
     MEVHLIVPIA MEEKLRFAIR EGGRTVGAGV VASIIE
//
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