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Database: UniProt/TrEMBL
Entry: A0A126RS43_9SPHN
LinkDB: A0A126RS43_9SPHN
Original site: A0A126RS43_9SPHN 
ID   A0A126RS43_9SPHN        Unreviewed;       396 AA.
AC   A0A126RS43;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-SEP-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   ORFNames=K426_19750 {ECO:0000313|EMBL:AMK24879.1};
OS   Sphingobium sp. TKS.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1315974 {ECO:0000313|EMBL:AMK24879.1, ECO:0000313|Proteomes:UP000060779};
RN   [1] {ECO:0000313|Proteomes:UP000060779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TKS {ECO:0000313|Proteomes:UP000060779};
RA   Tabata M.;
RT   "Whole genome sequence of gamma-HCH degrading bacterium Sphingobium
RT   sp. TKS.";
RL   Submitted (APR-2013) 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; CP005083; AMK24879.1; -; Genomic_DNA.
DR   RefSeq; WP_066560553.1; NZ_CP005083.1.
DR   EnsemblBacteria; AMK24879; AMK24879; K426_19750.
DR   PATRIC; fig|1315974.3.peg.4146; -.
DR   Proteomes; UP000060779; Chromosome 1.
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:UP000060779};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AMK24879.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Hydrolase {ECO:0000313|EMBL:AMK24879.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000060779}.
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;  43000 MW;  943F843D6C2C6C66 CRC64;
     MAKAKFERTK PHCNIGTIGH VDHGKTSLTA AITKVLAETG GATFVDYANI DKAPEERERG
     ITISTAHVEY ETEARHYAHV DCPGHADYVK NMITGAAQMD GAILVVSATD GPMPQTREHI
     LLARQVGVPQ LVVFMNKVDL VDDPEILELV ELEIRELLSS YDFDGDNIPV IPGSAVKALD
     GTNDEIGKQA VLKLMEAVDT FIPQPERPID KPFLMPIEDV FSISGRGTVV TGRVETGIVK
     VGEEVEIVGI KDTRKTTVTG VEMFRKLLDE GRAGDNIGAL IRGVGREEVE RGQVLAKPGT
     ITPHTEFDAE VYVLSKEEGG RHTPFFANYR PQFYFRTTDV TGEVILPEGT EMVMPGDNVK
     LGVKLIAPIA MDQGLRFAIR EGGRTVGAGV VGTISK
//
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