GenomeNet

Database: UniProt/SWISS-PROT
Entry: EFTU_OLICO
LinkDB: EFTU_OLICO
Original site: EFTU_OLICO 
ID   EFTU_OLICO              Reviewed;         396 AA.
AC   B6JET1; F8BZC9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   10-OCT-2018, entry version 62.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=OCAR_5675, OCA5_c23320;
OS   Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145
OS   / OM5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Oligotropha.
OX   NCBI_TaxID=504832;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=18539730; DOI=10.1128/JB.00614-08;
RA   Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.;
RT   "Genome sequence of the chemolithoautotrophic bacterium Oligotropha
RT   carboxidovorans OM5T.";
RL   J. Bacteriol. 190:5531-5532(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX   PubMed=21742883; DOI=10.1128/JB.05619-11;
RA   Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA   Meyer O.;
RT   "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT   carboxidovorans strains OM4 and OM5.";
RL   J. Bacteriol. 193:5043-5043(2011).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00118}.
DR   EMBL; CP001196; ACI92803.1; -; Genomic_DNA.
DR   EMBL; CP002826; AEI07032.1; -; Genomic_DNA.
DR   RefSeq; WP_012562832.1; NC_015684.1.
DR   ProteinModelPortal; B6JET1; -.
DR   SMR; B6JET1; -.
DR   STRING; 504832.OCA5_c23320; -.
DR   PRIDE; B6JET1; -.
DR   EnsemblBacteria; ACI92803; ACI92803; OCAR_5675.
DR   EnsemblBacteria; AEI07032; AEI07032; OCA5_c23320.
DR   KEGG; oca:OCAR_5675; -.
DR   KEGG; ocg:OCA5_c23320; -.
DR   PATRIC; fig|504832.7.peg.2457; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   BioCyc; OCAR504832:G1GTX-1600-MONOMER; -.
DR   Proteomes; UP000007730; 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; Cytoplasm; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    396       Elongation factor Tu.
FT                                /FTId=PRO_1000095083.
FT   DOMAIN       10    206       tr-type G.
FT   NP_BIND      19     26       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND      81     85       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND     136    139       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   REGION       19     26       G1. {ECO:0000250}.
FT   REGION       60     64       G2. {ECO:0000250}.
FT   REGION       81     84       G3. {ECO:0000250}.
FT   REGION      136    139       G4. {ECO:0000250}.
FT   REGION      174    176       G5. {ECO:0000250}.
SQ   SEQUENCE   396 AA;  43444 MW;  3682AB67670C143D CRC64;
     MAKEKFERKK PHCNIGTIGH VDHGKTSLTA AITKVLAEAG GATFTAYDQI DKAPEEKARG
     ITISTSHVEY ETPNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA IVVFLNKCDM VDDPELLELV ELEVRELLSK YNFPGDKIPI IKGSALAALE
     NSDEKLGRDA VLELMKNVDE YIPQPERPVD QPFLMPVEDV FSISGRGTVV TGRVERGIVK
     VGEEIEIVGI RPTQKTTVTG VEMFRKLLDQ GQAGDNIGAL LRGTKREDVE RGQVLCKPGS
     VKPHTKFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGVVHLPEGT EMVMPGDNIA
     MEVHLIVPIA MEEKLRFAIR EGGRTVGAGV VASIIE
//
DBGET integrated database retrieval system