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Database: UniProt/TrEMBL
Entry: G8AEN2_AZOBR
LinkDB: G8AEN2_AZOBR
Original site: G8AEN2_AZOBR 
ID   G8AEN2_AZOBR            Unreviewed;       396 AA.
AC   G8AEN2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-SEP-2017, entry version 37.
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=tufB2 {ECO:0000313|EMBL:CCC98855.1};
GN   Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118}, tufB1
GN   {ECO:0000313|EMBL:CCC98841.1};
GN   ORFNames=AZOBR_160001 {ECO:0000313|EMBL:CCC98841.1}, AZOBR_160015
GN   {ECO:0000313|EMBL:CCC98855.1};
OS   Azospirillum brasilense Sp245.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=1064539 {ECO:0000313|EMBL:CCC98855.1, ECO:0000313|Proteomes:UP000007319};
RN   [1] {ECO:0000313|EMBL:CCC98855.1, ECO:0000313|Proteomes:UP000007319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sp245 {ECO:0000313|EMBL:CCC98855.1,
RC   ECO:0000313|Proteomes:UP000007319};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H.,
RA   Robertson J.S., Barbe V., Calteau A., Rouy Z., Mangenot S.,
RA   Prigent-Combaret C., Normand P., Boyer M., Siguier P., Dessaux Y.,
RA   Elmerich C., Condemine G., Krishnen G., Kennedy I., Paterson A.H.,
RA   Gonzalez V., Mavingui P., Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
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; HE577327; CCC98841.1; -; Genomic_DNA.
DR   EMBL; HE577327; CCC98855.1; -; Genomic_DNA.
DR   RefSeq; WP_014241041.1; NC_016617.1.
DR   STRING; 1064539.AZOBR_160015; -.
DR   EnsemblBacteria; CCC98841; CCC98841; AZOBR_160001.
DR   EnsemblBacteria; CCC98855; CCC98855; AZOBR_160015.
DR   KEGG; abs:AZOBR_160001; -.
DR   KEGG; abs:AZOBR_160015; -.
DR   PATRIC; fig|192.7.peg.1614; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   KO; K02358; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000007319; 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.
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:UP000007319};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:CCC98855.1};
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:UP000007319}.
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;  43176 MW;  CBA50C0F32A15450 CRC64;
     MAKAKFERNK PHCNIGTIGH VDHGKTSLTA AITKVLAESG GATFTAYDQI DKAPEEKARG
     ITISTAHVEY ETTNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA LVVFMNKVDM VDDPELLELV EMEVRELLSS YQFPGDDIPI VKGSALCALE
     DRSPEIGRDA ILKLMAEVDQ YIPQPERPKD RPFLMPIEDV FSISGRGTVV TGRVERGIVK
     VGEEVEIVGL KTTVKTTVTG VEMFRKLLDS GEAGDNIGAL LRGTKREDVE RGQVLAKPGS
     ITPHTTFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGMVKLPEGT EMVMPGDNIS
     MEVELIAPIA MDEGLRFAIR EGGRTVGAGV VASIIK
//
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