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Database: UniProt/TrEMBL
Entry: A0A1C3D820_GEOTH
LinkDB: A0A1C3D820_GEOTH
Original site: A0A1C3D820_GEOTH 
ID   A0A1C3D820_GEOTH        Unreviewed;       395 AA.
AC   A0A1C3D820;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-SEP-2017, entry version 8.
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=A5N86_11160 {ECO:0000313|EMBL:ODA16989.1}, BGM21_00270
GN   {ECO:0000313|EMBL:AOL33122.1};
OS   Geobacillus thermoleovorans (Bacillus thermoleovorans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=33941 {ECO:0000313|EMBL:ODA16989.1, ECO:0000313|Proteomes:UP000094835};
RN   [1] {ECO:0000313|EMBL:ODA16989.1, ECO:0000313|Proteomes:UP000094835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N7 {ECO:0000313|EMBL:ODA16989.1,
RC   ECO:0000313|Proteomes:UP000094835};
RA   Mukhopadhyay S.K.;
RT   "Genome sequence of thermophilic Geobacillus thermoleovorans strain
RT   N7.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AOL33122.1, ECO:0000313|Proteomes:UP000094325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-2391 {ECO:0000313|EMBL:AOL33122.1,
RC   ECO:0000313|Proteomes:UP000094325};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J.,
RA   Ge C., Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   bacillus-like bacteria.";
RL   Submitted (AUG-2016) 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; CP017071; AOL33122.1; -; Genomic_DNA.
DR   EMBL; MDCP01000142; ODA16989.1; -; Genomic_DNA.
DR   RefSeq; WP_011229619.1; NZ_MDCP01000142.1.
DR   GeneID; 32062092; -.
DR   KEGG; gtk:GT3570_00580; -.
DR   KO; K02358; -.
DR   Proteomes; UP000094325; Chromosome.
DR   Proteomes; UP000094835; Unassembled WGS sequence.
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:UP000094325,
KW   ECO:0000313|Proteomes:UP000094835};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ODA16989.1};
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    204       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   395 AA;  43306 MW;  01C05E515C3B29FB CRC64;
     MAKAKFERTK PHVNIGTIGH VDHGKTTLTA AITTVLAKQG KAEAKAYDQI DAAPEERERG
     ITISTAHVEY ETDARHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLSRQVGVPY IVVFLNKCDM VDDEELLELV EMEVRDLLSE YDFPGDEVPV IKGSALKALE
     GDPQWEEKII ELMNAVDEYI PTPQREVDKP FMMPIEDVFS ITGRGTVATG RVERGTLKVG
     DPVEIIGLSD EPKTTTVTGV EMFRKLLDQA EAGDNIGALL RGVSRDEVER GQVLAKPGSI
     TPHTKFKAQV YVLTKEEGGR HTPFFSNYRP QFYFRTTDVT GIITLPEGVE MVMPGDNVEM
     TVELIAPIAI EEGTKFSIRE GGRTVGAGSV SEIIE
//
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