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Database: UniProt/TrEMBL
Entry: A0A173KUR1_9SPHN
LinkDB: A0A173KUR1_9SPHN
Original site: A0A173KUR1_9SPHN 
ID   A0A173KUR1_9SPHN        Unreviewed;       396 AA.
AC   A0A173KUR1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-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=EP837_01219 {ECO:0000313|EMBL:ANI77652.1};
OS   Sphingobium sp. EP60837.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1855519 {ECO:0000313|EMBL:ANI77652.1, ECO:0000313|Proteomes:UP000078304};
RN   [1] {ECO:0000313|EMBL:ANI77652.1, ECO:0000313|Proteomes:UP000078304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EP60837 {ECO:0000313|EMBL:ANI77652.1,
RC   ECO:0000313|Proteomes:UP000078304};
RA   Lee C.-M., Yoon S.-H., Kim B.-Y.;
RT   "Complete genome sequence of a organophosphorus pesticides.";
RL   Submitted (JUN-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; CP015986; ANI77652.1; -; Genomic_DNA.
DR   RefSeq; WP_066525434.1; NZ_CP015986.1.
DR   EnsemblBacteria; ANI77652; ANI77652; EP837_01219.
DR   KEGG; sphb:EP837_01219; -.
DR   PATRIC; fig|1855519.3.peg.1241; -.
DR   KO; K02358; -.
DR   Proteomes; UP000078304; 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:UP000078304};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ANI77652.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078304}.
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;  42772 MW;  E66F6646AD6E25C9 CRC64;
     MAKAKFERNK PHCNIGTIGH VDHGKTSLTA AITKVLAETG GATFVDYANI DKAPEERERG
     ITISTAHVEY ETEARHYAHV DCPGHADYVK NMITGAAQMD GAILVVSATD GPMPQTREHI
     LLAKQVGVPQ LVVFMNKVDL VDDPEILELV ELEIRELLSS YDFDGDNIPV IPGSAVKALD
     GSNDEIGKQA VLKLMAAVDS FIPQPERPVD KPFLMPIEDV FSISGRGTVV TGRVETGIVK
     VGEEVEIVGI RDTRKTTVTG VEMFRKLLDQ GEAGDNIGAL VRGVGREDVE RGQVLAKPGS
     VTPHTEFDAE VYVLSKEEGG RHTPFFANYR PQFYFRTTDV TGEVILPEGT EMVMPGDNVK
     LGVKLIAPIA MDAGLRFAIR EGGRTVGAGV VGTISK
//
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