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Database: UniProt/TrEMBL
Entry: A0A1B3N1S3_9SPHN
LinkDB: A0A1B3N1S3_9SPHN
Original site: A0A1B3N1S3_9SPHN 
ID   A0A1B3N1S3_9SPHN        Unreviewed;       396 AA.
AC   A0A1B3N1S3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   22-NOV-2017, entry version 10.
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:AOF99308.1};
GN   ORFNames=BSY18_1921 {ECO:0000313|EMBL:AOF99308.1};
OS   Blastomonas sp. RAC04.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Blastomonas.
OX   NCBI_TaxID=1842535 {ECO:0000313|EMBL:AOF99308.1, ECO:0000313|Proteomes:UP000094988};
RN   [1] {ECO:0000313|EMBL:AOF99308.1, ECO:0000313|Proteomes:UP000094988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAC04 {ECO:0000313|EMBL:AOF99308.1,
RC   ECO:0000313|Proteomes:UP000094988};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-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; CP016460; AOF99308.1; -; Genomic_DNA.
DR   RefSeq; WP_054134239.1; NZ_CP016460.1.
DR   EnsemblBacteria; AOF99308; AOF99308; BSY18_1921.
DR   KEGG; blas:BSY18_1921; -.
DR   PATRIC; fig|1842535.3.peg.1929; -.
DR   KO; K02358; -.
DR   Proteomes; UP000094988; 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:UP000094988};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AOF99308.1};
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    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;  42902 MW;  97CE1F6BBCD35B83 CRC64;
     MAKAKFERTK PHCNIGTIGH VDHGKTTLTA AITKVLAETG GATFTDYANI DKAPEERERG
     ITISTAHVEY ETEARHYAHV DCPGHADYVK NMITGAAQMD GAILVVNAAD GPMPQTREHI
     LLARQVGVPA LVVYMNKVDQ VDDEEILELV ELEVRELLSS YDFPGDDIPI VKGSALAALE
     GRDDAIGKES IYALMKAVDE FIPQPARPID RPFLMPVEDV FSISGRGTVV TGRVESGIVK
     VGEEVEIVGL KDTRKTVVTG VEMFRKLLDQ GMAGDNIGAL VRGVAREDVE RGQVLCKPGS
     VTPHTEFNAE VYVLSKDEGG RHTPFFANYR PQFYFRTTDV TGEVVLPEGT EMVMPGDNVT
     IGVKLIAPIA MDPGLRFAIR EGGRTVGSGV VSTISK
//
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