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Database: UniProt/TrEMBL
Entry: A0A1X9YIV6_9SPHN
LinkDB: A0A1X9YIV6_9SPHN
Original site: A0A1X9YIV6_9SPHN 
ID   A0A1X9YIV6_9SPHN        Unreviewed;       396 AA.
AC   A0A1X9YIV6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-SEP-2017, entry version 2.
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=KC8_15470 {ECO:0000313|EMBL:ARS28680.1};
OS   Sphingomonas sp. KC8.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1030157 {ECO:0000313|EMBL:ARS28680.1, ECO:0000313|Proteomes:UP000194475};
RN   [1] {ECO:0000313|EMBL:ARS28680.1, ECO:0000313|Proteomes:UP000194475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KC8 {ECO:0000313|EMBL:ARS28680.1};
RA   Chen Y.-L., Yu C.-P., Hu A., Lee T.-H., Yang F.-C., Ismail W.,
RA   Wang P.-H., Wang C.-H., Goh K.-S., Shih C.-J., Chiang Y.-R.;
RT   "Bacteria use an extradiol dioxygenase-mediated pathway to degrade
RT   natural estrogens in aquatic ecosystems.";
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; CP016306; ARS28680.1; -; Genomic_DNA.
DR   RefSeq; WP_010127205.1; NZ_AFMP01000051.1.
DR   Proteomes; UP000194475; Chromosome.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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:UP000194475};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ARS28680.1};
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;  42905 MW;  D0C9C175757C2D12 CRC64;
     MAKAKFERTK PHCNIGTIGH VDHGKTSLTA AITKVLAETG GATFTSYDNI DKAPEERERG
     ITISTAHVEY ETADRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSATD GPMPQTREHI
     LLARQVGVPQ LVVFLNKVDL VDDPEILELV ELEVRELLSK YDFDGDNIPI IPGSAVAALT
     DKTPEIGHDA VLKLMAAVDS WIPQPERPLD RPFLMPIEDV FSISGRGTVV TGRVETGIVK
     VGEEVEIVGI KDTRKTTVTG VEMFRKLLDQ GQAGDNIGAL IRGVGREEVE RGQVLAKPGT
     ITPHTEFSAE VYVLSKDEGG RHTPFFANYR PQFYFRTTDV TGEVTLPEGT EMVMPGDNVS
     LGIKLIAPIA MDQGLRFAIR EGGRTVGAGV VGTITK
//
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