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Database: UniProt/TrEMBL
Entry: A0A060DK82_AZOBR
LinkDB: A0A060DK82_AZOBR
Original site: A0A060DK82_AZOBR 
ID   A0A060DK82_AZOBR        Unreviewed;       396 AA.
AC   A0A060DK82;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-SEP-2017, entry version 20.
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:AIB11119.1};
GN   ORFNames=ABAZ39_03620 {ECO:0000313|EMBL:AIB11119.1}, AMK58_10395
GN   {ECO:0000313|EMBL:ALJ35796.1}, AMK58_10465
GN   {ECO:0000313|EMBL:ALJ35809.1};
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192 {ECO:0000313|EMBL:AIB11119.1, ECO:0000313|Proteomes:UP000027186};
RN   [1] {ECO:0000313|EMBL:AIB11119.1, ECO:0000313|Proteomes:UP000027186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Az39 {ECO:0000313|EMBL:AIB11119.1,
RC   ECO:0000313|Proteomes:UP000027186};
RX   PubMed=25059863;
RA   Rivera D., Revale S., Molina R., Gualpa J., Puente M., Maroniche G.,
RA   Paris G., Baker D., Clavijo B., McLay K., Spaepen S., Perticari A.,
RA   Vazquez M., Wisniewski-Dye F., Watkins C., Martinez-Abarca F.,
RA   Vanderleyden J., Cassan F.;
RT   "Complete Genome Sequence of the Model Rhizosphere Strain Azospirillum
RT   brasilense Az39, Successfully Applied in Agriculture.";
RL   Genome Announc. 2:e00683-14(2014).
RN   [2] {ECO:0000313|EMBL:ALJ35796.1, ECO:0000313|Proteomes:UP000065707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sp 7 {ECO:0000313|EMBL:ALJ35796.1,
RC   ECO:0000313|Proteomes:UP000065707};
RA   Millard Andrew;
RL   Submitted (OCT-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; CP007793; AIB11119.1; -; Genomic_DNA.
DR   EMBL; CP012914; ALJ35796.1; -; Genomic_DNA.
DR   EMBL; CP012914; ALJ35809.1; -; Genomic_DNA.
DR   RefSeq; WP_035675071.1; NZ_CP012914.1.
DR   EnsemblBacteria; AIB11119; AIB11119; ABAZ39_03620.
DR   EnsemblBacteria; ALJ35796; ALJ35796; AMK58_10395.
DR   EnsemblBacteria; ALJ35809; ALJ35809; AMK58_10465.
DR   KEGG; abf:AMK58_10395; -.
DR   KEGG; abf:AMK58_10465; -.
DR   KEGG; abq:ABAZ39_03620; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   KO; K02358; -.
DR   Proteomes; UP000027186; Chromosome.
DR   Proteomes; UP000065707; 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:UP000027186,
KW   ECO:0000313|Proteomes:UP000065707};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AIB11119.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Hydrolase {ECO:0000313|EMBL:AIB11119.1};
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;  43145 MW;  31F5E20E82A14F51 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 KATVKTTVTG VEMFRKLLDS GEAGDNIGAL LRGTKREDVE RGQVLAKPGS
     ITPHTTFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGMVKLPEGT EMVMPGDNIS
     MEVELIAPIA MDEGLRFAIR EGGRTVGAGV VASIIK
//
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