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Database: UniProt/TrEMBL
Entry: I0G5P9_9BRAD
LinkDB: I0G5P9_9BRAD
Original site: I0G5P9_9BRAD 
ID   I0G5P9_9BRAD            Unreviewed;       396 AA.
AC   I0G5P9;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   22-NOV-2017, entry version 36.
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   ECO:0000313|EMBL:BAL76086.1};
GN   ORFNames=S23_28780 {ECO:0000313|EMBL:BAL76086.1};
OS   Bradyrhizobium sp. S23321.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=335659 {ECO:0000313|EMBL:BAL76086.1, ECO:0000313|Proteomes:UP000007886};
RN   [1] {ECO:0000313|EMBL:BAL76086.1, ECO:0000313|Proteomes:UP000007886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S23321 {ECO:0000313|EMBL:BAL76086.1,
RC   ECO:0000313|Proteomes:UP000007886};
RX   PubMed=22452844; DOI=10.1264/jsme2.ME11321;
RA   Okubo T., Tsukui T., Maita H., Okamoto S., Oshima K., Fujisawa T.,
RA   Saito A., Futamata H., Hattori R., Shimomura Y., Haruta S.,
RA   Morimoto S., Wang Y., Sakai Y., Hattori M., Aizawa S.,
RA   Nagashima K.V.P., Masuda S., Hattori T., Yamashita A., Bao Z.,
RA   Hayatsu M., Kajiya-Kanegae H., Yoshinaga I., Sakamoto K., Toyota K.,
RA   Nakao M., Kohara M., Anda M., Niwa R., Jung-Hwan P.,
RA   Sameshima-Saito R., Tokuda S., Yamamoto S., Yamamoto S., Yokoyama T.,
RA   Akutsu T., Nakamura Y., Nakahira-Yanaka Y., Takada Hoshino Y.,
RA   Hirakawa H., Mitsui H., Terasawa K., Itakura M., Sato S.,
RA   Ikeda-Ohtsubo W., Sakakura N., Kaminuma E., Minamisawa K.;
RT   "Complete genome sequence of Bradyrhizobium sp. S23321: insights into
RT   symbiosis evolution in soil oligotrophs.";
RL   Microbes Environ. 27:306-315(2012).
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; AP012279; BAL76086.1; -; Genomic_DNA.
DR   RefSeq; WP_008136415.1; NC_017082.1.
DR   EnsemblBacteria; BAL76086; BAL76086; S23_28780.
DR   KEGG; brs:S23_28780; -.
DR   PATRIC; fig|335659.3.peg.2893; -.
DR   KO; K02358; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000007886; 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:UP000007886};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:BAL76086.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007886}.
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;  43340 MW;  57A6EF30C9E8D361 CRC64;
     MAKAKFERNK PHCNIGTIGH VDHGKTSLTA AITKVLAEAG GATFTAYDQI DKAPEEKARG
     ITISTAHVEY ETPNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA LVVFLNKCDM VDDPELLELV ELEVRELLSK YDFPGDKIPI IKGSALAALE
     DSDKKLGHDA ILELMKNVDE YIPQPERPID QPFLMPVEDV FSISGRGTVV TGRVERGIVK
     VGEEIEIVGL RATQKTTVTG VEMFRKLLDQ GQAGDNIGAL LRGTKREDVE RGQVLCKPGS
     VKPHTKFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGVVHLPEGT EMVMPGDNIA
     MEVHLIVPIA MEEKLRFAIR EGGRTVGAGV VASIIE
//
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