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Database: UniProt/SWISS-PROT
Entry: EFTU_BACFR
LinkDB: EFTU_BACFR
Original site: EFTU_BACFR 
ID   EFTU_BACFR              Reviewed;         394 AA.
AC   P33165;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   22-NOV-2017, entry version 113.
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}; OrderedLocusNames=BF4199;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2110445; DOI=10.1007/BF00249075;
RA   Ludwig W., Weizenegger M., Betzl D., Leidel E., Lenz T., Ludvigsen A.,
RA   Moellenhoff D., Wenzig P., Schleifer K.H.;
RT   "Complete nucleotide sequences of seven eubacterial genes coding for
RT   the elongation factor Tu: functional, structural and phylogenetic
RT   evaluations.";
RL   Arch. Microbiol. 153:241-247(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA
RT   inversions regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD50942.1; -; Genomic_DNA.
DR   PIR; B60663; B60663.
DR   RefSeq; WP_005782155.1; NC_006347.1.
DR   RefSeq; YP_101476.1; NC_006347.1.
DR   ProteinModelPortal; P33165; -.
DR   SMR; P33165; -.
DR   PRIDE; P33165; -.
DR   EnsemblBacteria; BAD50942; BAD50942; BF4199.
DR   GeneID; 3085281; -.
DR   KEGG; bfr:BF4199; -.
DR   PATRIC; fig|295405.11.peg.4054; -.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; POG091H00LA; -.
DR   Proteomes; UP000002197; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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.
FT   CHAIN         1    394       Elongation factor Tu.
FT                                /FTId=PRO_0000091288.
FT   DOMAIN       10    205       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   394 AA;  43580 MW;  7B4C6FD208323149 CRC64;
     MAKEKFERTK PHVNIGTIGH VDHGKTTLTA AITTVLAKKG LSELRSFDSI DNAPEEKERG
     ITINTSHVEY ETANRHYAHV DCPGHADYVK NMVTGAAQMD GAIIVVAATD GPMPQTREHI
     LLARQVNVPK LVVFMNKCDM VEDAEMLELV EMEMRELLSF YDFDGDNTPI IQGSALGALN
     GVEKWEDKVM ELMEAVDTWI PLPPRDVDKP FLMPVEDVFS ITGRGTVATG RIETGVIHVG
     DEIEILGLGE DKKSVVTGVE MFRKLLDQGE AGDNVGLLLR GVDKNEIKRG MVLCKPGQIK
     PHSKFKAEVY ILKKEEGGRH TPFHNKYRPQ FYLRTMDCTG EITLPEGTEM VMPGDNVTIT
     VELIYPVALN IGLRFAIREG GRTVGAGQIT EIID
//
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