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Database: UniProt/TrEMBL
Entry: A0A0K2D8M2_9RHIZ
LinkDB: A0A0K2D8M2_9RHIZ
Original site: A0A0K2D8M2_9RHIZ 
ID   A0A0K2D8M2_9RHIZ        Unreviewed;       396 AA.
AC   A0A0K2D8M2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   22-NOV-2017, entry version 13.
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:ALA16169.1};
GN   ORFNames=AL346_00575 {ECO:0000313|EMBL:ALA16169.1}, AL346_00655
GN   {ECO:0000313|EMBL:ALA16183.1};
OS   Chelatococcus sp. CO-6.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Chelatococcaceae; Chelatococcus.
OX   NCBI_TaxID=1702325 {ECO:0000313|EMBL:ALA16169.1, ECO:0000313|Proteomes:UP000065824};
RN   [1] {ECO:0000313|EMBL:ALA16169.1, ECO:0000313|Proteomes:UP000065824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-6 {ECO:0000313|EMBL:ALA16169.1,
RC   ECO:0000313|Proteomes:UP000065824};
RA   Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA   Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M.,
RA   Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J.,
RA   Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L.,
RA   Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J.,
RA   Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L.,
RA   Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z.,
RA   Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J.,
RA   Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W.,
RA   Hatfull G.F.;
RL   Submitted (AUG-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; CP012398; ALA16169.1; -; Genomic_DNA.
DR   EMBL; CP012398; ALA16183.1; -; Genomic_DNA.
DR   RefSeq; WP_053193117.1; NZ_CP012398.1.
DR   EnsemblBacteria; ALA16169; ALA16169; AL346_00575.
DR   EnsemblBacteria; ALA16183; ALA16183; AL346_00655.
DR   KEGG; chel:AL346_00575; -.
DR   KEGG; chel:AL346_00655; -.
DR   PATRIC; fig|1702325.3.peg.117; -.
DR   KO; K02358; -.
DR   Proteomes; UP000065824; 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:UP000065824};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ALA16169.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Hydrolase {ECO:0000313|EMBL:ALA16169.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000065824}.
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;  43426 MW;  F25C352BB47D3A0B CRC64;
     MAKEKFERTK PHCNIGTIGH VDHGKTSLTA AITKVLAEKG GASFTAYDQI DKAPEEKARG
     ITISTSHVEY ETDKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSSAD GPMPQTREHI
     LLARQVGVPA LVVFMNKVDM VDDPELLDLV ELEVRELLSK YDFPGDDIPI VKGSALCALE
     DRSPEIGRDA VLQLMDAVDA YIPQPERPKD QPFLMPVEDV FSISGRGTVV TGRVERGVVK
     VGEEVEIVGL RPTQKTTVTG VEMFRKLLDQ GEAGDNIGAL LRGTKREDVE RGQVLCKPGS
     VKPHTKFKAE AYILTKEEGG RHTPFFNNYR PQFYFRTTDV TGMVKLPEGT EMVMPGDNVA
     MEVELIVPIA MEEKLRFAIR EGGRTVGAGV VASIIE
//
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