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Database: UniProt/SWISS-PROT
Entry: EFTU_CAUVC
LinkDB: EFTU_CAUVC
Original site: EFTU_CAUVC 
ID   EFTU_CAUVC              Reviewed;         396 AA.
AC   Q99QM0;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   10-OCT-2018, entry version 102.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tufA {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=CC_1240;
GN   and
GN   Name=tufB {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=CC_3199;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter
OS   crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J.,
RA   Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J.,
RA   Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L.,
RA   Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK23221.1; -; Genomic_DNA.
DR   EMBL; AE005673; AAK25161.1; -; Genomic_DNA.
DR   PIR; A87403; A87403.
DR   RefSeq; NP_420053.1; NC_002696.2.
DR   RefSeq; NP_421993.1; NC_002696.2.
DR   RefSeq; WP_010919120.1; NC_002696.2.
DR   ProteinModelPortal; Q99QM0; -.
DR   SMR; Q99QM0; -.
DR   STRING; 190650.CC_3199; -.
DR   PRIDE; Q99QM0; -.
DR   EnsemblBacteria; AAK23221; AAK23221; CC_1240.
DR   EnsemblBacteria; AAK25161; AAK25161; CC_3199.
DR   GeneID; 940971; -.
DR   GeneID; 941607; -.
DR   KEGG; ccr:CC_1240; -.
DR   KEGG; ccr:CC_3199; -.
DR   PATRIC; fig|190650.5.peg.1266; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   BioCyc; CAULO:CC1240-MONOMER; -.
DR   BioCyc; CAULO:CC3199-MONOMER; -.
DR   Proteomes; UP000001816; 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_0000091304.
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;  43340 MW;  1F58829078B624D2 CRC64;
     MAKEKFERTK PHCNIGTIGH VDHGKTTLTA AITMTLAKSG GATAKKYDEI DAAPEEKARG
     ITINTAHVEY ETANRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPA LVVFMNKVDM VDDEELLELV EMEVRELLSS YQFPGDDIPI TKGSALAAVE
     GRDPQIGEEK ILELMASVDA YIPQPERPVD MPFLMPVEDV FSISGRGTVV TGRVERGIVK
     VGEEVEIVGI RPVQKTTCTG VEMFRKLLDQ GQAGDNVGVL LRGTKREDVE RGQVLCKPGS
     ITPHTKFVAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGIIKLREGV EMIMPGDNAE
     LDVELITPIA MEEKLRFAIR EGGRTVGAGV VAKIVE
//
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