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Database: UniProt/SWISS-PROT
Entry: EFTU_CHESB
LinkDB: EFTU_CHESB
Original site: EFTU_CHESB 
ID   EFTU_CHESB              Reviewed;         391 AA.
AC   Q11HA6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JAN-2019, entry version 87.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=Meso_1680;
GN   and
GN   Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=Meso_1826;
OS   Chelativorans sp. (strain BNC1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Chelativorans.
OX   NCBI_TaxID=266779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BNC1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL   Submitted (JUN-2006) 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: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; CP000390; ABG63075.1; -; Genomic_DNA.
DR   EMBL; CP000390; ABG63219.1; -; Genomic_DNA.
DR   RefSeq; WP_011581018.1; NC_008254.1.
DR   ProteinModelPortal; Q11HA6; -.
DR   SMR; Q11HA6; -.
DR   STRING; 266779.Meso_1826; -.
DR   PRIDE; Q11HA6; -.
DR   EnsemblBacteria; ABG63075; ABG63075; Meso_1680.
DR   EnsemblBacteria; ABG63219; ABG63219; Meso_1826.
DR   KEGG; mes:Meso_1680; -.
DR   KEGG; mes:Meso_1826; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; 621774at2; -.
DR   Proteomes; UP000001820; 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    391       Elongation factor Tu.
FT                                /FTId=PRO_0000337430.
FT   DOMAIN       10    201       tr-type G.
FT   NP_BIND      19     26       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND      76     80       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   NP_BIND     131    134       GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
FT   REGION       19     26       G1. {ECO:0000250}.
FT   REGION       55     59       G2. {ECO:0000250}.
FT   REGION       76     79       G3. {ECO:0000250}.
FT   REGION      131    134       G4. {ECO:0000250}.
FT   REGION      169    171       G5. {ECO:0000250}.
SQ   SEQUENCE   391 AA;  42794 MW;  E6B41737CCD77AA6 CRC64;
     MAKGKFERTK PHVNIGTIGH VDHGKTSLTA AITKYFGEFK AYDQIDAAPE EKARGITIST
     AHVEYETENR HYAHVDCPGH ADYVKNMITG AAQMDGAILV VSAADGPMPQ TREHILLARQ
     VGVPAIVVFL NKVDQVDDPE LLELVELEIR ELLSKYEFPG DDIPIVKGSA LAALEDSNKE
     IGEDAVRQLM AEVDKYIPTP ERPIDQPFLM PIEDVFSISG RGTVVTGRVE RGVVKVGEEV
     EIVGIRPTSK TTVTGVEMFR KLLDQGQAGD NIGALLRGID REGVERGQVL AKPGSVTPHT
     KFKAEAYILT KEEGGRHTPF FTNYRPQFYF RTTDVTGVVT LPEGTEMVMP GDNVTMDVTL
     IVPIAMEERL RFAIREGGRT VGAGIVASIT E
//
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