GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0E0T7N3_GEOS2
LinkDB: A0A0E0T7N3_GEOS2
Original site: A0A0E0T7N3_GEOS2 
ID   A0A0E0T7N3_GEOS2        Unreviewed;       395 AA.
AC   A0A0E0T7N3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-SEP-2017, entry version 15.
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   OrderedLocusNames=GYMC52_0106 {ECO:0000313|EMBL:ADU92621.1};
OS   Geobacillus sp. (strain Y412MC52).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=550542 {ECO:0000313|EMBL:ADU92621.1, ECO:0000313|Proteomes:UP000002223};
RN   [1] {ECO:0000313|EMBL:ADU92621.1, ECO:0000313|Proteomes:UP000002223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y412MC52 {ECO:0000313|EMBL:ADU92621.1,
RC   ECO:0000313|Proteomes:UP000002223};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Chertkov O., Munk C., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y412MC52.";
RL   Submitted (JAN-2011) 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002442; ADU92621.1; -; Genomic_DNA.
DR   RefSeq; WP_011229619.1; NC_014915.1.
DR   ProteinModelPortal; A0A0E0T7N3; -.
DR   SMR; A0A0E0T7N3; -.
DR   EnsemblBacteria; ADU92621; ADU92621; GYMC52_0106.
DR   GeneID; 32062092; -.
DR   KEGG; gya:GYMC52_0106; -.
DR   KO; K02358; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000002223; 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:UP000002223};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ADU92621.1};
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
//
DBGET integrated database retrieval system