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Database: UniProt/TrEMBL
Entry: A0A1D7NN63_9SPHN
LinkDB: A0A1D7NN63_9SPHN
Original site: A0A1D7NN63_9SPHN 
ID   A0A1D7NN63_9SPHN        Unreviewed;       396 AA.
AC   A0A1D7NN63;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-SEP-2017, entry version 8.
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=BG023_112307 {ECO:0000313|EMBL:AOL95221.1};
OS   Porphyrobacter sp. LM 6.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Porphyrobacter.
OX   NCBI_TaxID=1896196 {ECO:0000313|EMBL:AOL95221.1, ECO:0000313|Proteomes:UP000094080};
RN   [1] {ECO:0000313|EMBL:AOL95221.1, ECO:0000313|Proteomes:UP000094080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LM 6 {ECO:0000313|EMBL:AOL95221.1,
RC   ECO:0000313|Proteomes:UP000094080};
RA   Hentchel K., Vargas G., Fiebig A., Coleman M., Crosson S.;
RT   "Genome sequences of bacteria isolated from the littoral zone of
RT   southern Lake Michigan.";
RL   Submitted (AUG-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; CP017113; AOL95221.1; -; Genomic_DNA.
DR   RefSeq; WP_069310556.1; NZ_CP017113.1.
DR   EnsemblBacteria; AOL95221; AOL95221; BG023_112307.
DR   KEGG; porl:BG023_112307; -.
DR   PATRIC; fig|1896196.3.peg.2286; -.
DR   KO; K02358; -.
DR   Proteomes; UP000094080; 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:UP000094080};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:AOL95221.1};
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    209       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;  42911 MW;  92D5535467394AD1 CRC64;
     MAKEKFQRNK PHCNIGTIGH VDHGKTTLTA AITKVMAETY GGSAVDFANI DKAPEERERG
     ITISTAHVEY ESAARHYAHV DCPGHADYVK NMITGAAQMD GAILVVNAAD GPMPQTREHI
     LLARQVGVPA LVVYMNKVDQ VDDEEILELV ELEVRELLSS YDFDGDNIPI VKGSALAALE
     GRDDNIGKDS VIALIEAVDS YIPQPDRPVD KPFLMPIEDV FSISGRGTVV TGRIETGIVN
     VGDEVEIVGI KDTRKTTVTG VEMFRKLLDR GEAGDNVGAL IRGVAREEVE RGQVLAKPGS
     VTPHTEFSAE VYVLSKDEGG RHTPFFANYR PQFYFRTTDV TGEVILPEGT EMVMPGDNVT
     IGVKLIAPIA MDEGLRFAIR EGGRTVGSGV VAKITK
//
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