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Database: UniProt/TrEMBL
Entry: B6IRN9_RHOCS
LinkDB: B6IRN9_RHOCS
Original site: B6IRN9_RHOCS 
ID   B6IRN9_RHOCS            Unreviewed;       395 AA.
AC   B6IRN9;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   22-NOV-2017, entry version 72.
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:ACI98125.1};
GN   OrderedLocusNames=RC1_0693 {ECO:0000313|EMBL:ACI98125.1}, RC1_0709
GN   {ECO:0000313|EMBL:ACI98140.1};
OS   Rhodospirillum centenum (strain ATCC 51521 / SW).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=414684 {ECO:0000313|EMBL:ACI98125.1, ECO:0000313|Proteomes:UP000001591};
RN   [1] {ECO:0000313|Proteomes:UP000001591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RA   Touchman J.W., Bauer C., Blankenship R.E.;
RT   "Genome sequence of Rhodospirillum centenum.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACI98125.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SW {ECO:0000313|EMBL:ACI98125.1};
RX   PubMed=20500872; DOI=10.1186/1471-2164-11-325;
RA   Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D.,
RA   Chowdhury S.R., Hao J., Helmy T., Kim S., Kurdoglu A.A.,
RA   Matthies H.J., Rollo D., Stothard P., Blankenship R.E., Bauer C.E.,
RA   Touchman J.W.;
RT   "Metabolic flexibility revealed in the genome of the cyst-forming
RT   alpha-1 proteobacterium Rhodospirillum centenum.";
RL   BMC Genomics 11:325-325(2010).
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; CP000613; ACI98125.1; -; Genomic_DNA.
DR   EMBL; CP000613; ACI98140.1; -; Genomic_DNA.
DR   RefSeq; WP_012565917.1; NC_011420.2.
DR   STRING; 414684.RC1_0709; -.
DR   EnsemblBacteria; ACI98125; ACI98125; RC1_0693.
DR   EnsemblBacteria; ACI98140; ACI98140; RC1_0709.
DR   KEGG; rce:RC1_0693; -.
DR   KEGG; rce:RC1_0709; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000001591; 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:UP000001591};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00118,
KW   ECO:0000313|EMBL:ACI98125.1};
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:UP000001591}.
FT   DOMAIN       10    205       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   395 AA;  43160 MW;  C2A70F6CBB3598CB CRC64;
     MAKAKFERTK PHCNVGTIGH VDHGKTSLTA AITKVLAKTG GATFTAYDQI DKAPEEKARG
     ITISTAHVEY ETTNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA LVVFLNKMDM ADPELVELVE LEVRELLSSY GFPGDDIPVV KGSALCALED
     RNPEIGEQAI LELMRHVDAY IPQPERPKDR PFLMPIEDVF SISGRGTVVT GRVERGVIKV
     GEEVEIVGMK PTVKTTVTGV EMFRKLLDQG EAGDNIGALL RGTKREDVER GQVLAKPGSI
     TPHTKFEAET YILTKDEGGR HTPFFTNYRP QFYFRTTDVT GMVTLPEGTE MVMPGDNVRI
     RVELIAPIAM DEGLRFAIRE GGRTVGAGVV SKIIE
//
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