GenomeNet

Database: UniProt/SWISS-PROT
Entry: EFTU_ECO57
LinkDB: EFTU_ECO57
Original site: EFTU_ECO57 
ID   EFTU_ECO57              Reviewed;         394 AA.
AC   P0A6N3; O68929; P02990; Q8X4S9; Q8XED3;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-APR-2018, entry version 100.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE   AltName: Full=P-43;
GN   Name=tufA {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=Z4697, ECs4190;
GN   and
GN   Name=tufB {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=Z5553, ECs4903;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TUFA AND TUFB).
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (TUFA AND TUFB).
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(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   -!- FUNCTION: May play an important regulatory role in cell growth and
CC       in the bacterial response to nutrient deprivation. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- MISCELLANEOUS: The antibiotic kirromycin inhibits protein
CC       biosynthesis by inhibiting the release of EF-Tu from the ribosome.
CC       {ECO:0000250|UniProtKB:P0CE47}.
CC   -!- MISCELLANEOUS: The antibiotic pulvomycin inhibits protein
CC       biosynthesis by disrupting the allosteric control mechanism of EF-
CC       Tu. {ECO:0000250|UniProtKB:P0CE47}.
CC   -!- MISCELLANEOUS: The sequence of the tufB gene is shown. TufA
CC       differs in a single position (By similarity). {ECO:0000250}.
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; AE005174; AAG58446.1; -; Genomic_DNA.
DR   EMBL; AE005174; AAG59176.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37613.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38326.1; -; Genomic_DNA.
DR   PIR; B85998; B85998.
DR   PIR; G91241; G91241.
DR   RefSeq; NP_312217.1; NC_002695.1.
DR   RefSeq; NP_312930.1; NC_002695.1.
DR   RefSeq; WP_000031784.1; NZ_NOKN01000002.1.
DR   ProteinModelPortal; P0A6N3; -.
DR   SMR; P0A6N3; -.
DR   STRING; 155864.Z4697; -.
DR   PRIDE; P0A6N3; -.
DR   EnsemblBacteria; AAG58446; AAG58446; Z4697.
DR   EnsemblBacteria; AAG59176; AAG59176; Z5553.
DR   EnsemblBacteria; BAB37613; BAB37613; BAB37613.
DR   EnsemblBacteria; BAB38326; BAB38326; BAB38326.
DR   GeneID; 914959; -.
DR   GeneID; 915957; -.
DR   KEGG; ece:Z4697; -.
DR   KEGG; ece:Z5553; -.
DR   KEGG; ecs:ECs4190; -.
DR   KEGG; ecs:ECs4903; -.
DR   PATRIC; fig|386585.9.peg.4373; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   EvolutionaryTrace; P0A6N3; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; 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   GO; GO:0046677; P:response to antibiotic; 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   Acetylation; Antibiotic resistance; Cell inner membrane;
KW   Cell membrane; Complete proteome; Cytoplasm; Elongation factor;
KW   GTP-binding; Membrane; Methylation; Nucleotide-binding;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    394       Elongation factor Tu.
FT                                /FTId=PRO_0000091321.
FT   DOMAIN       10    204       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}.
FT   MOD_RES       2      2       N-acetylserine. {ECO:0000250}.
FT   MOD_RES      57     57       N6-methylated lysine. {ECO:0000250}.
FT   MOD_RES     314    314       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     383    383       Phosphothreonine. {ECO:0000250}.
FT   VARIANT     394    394       S -> G (in tufA).
SQ   SEQUENCE   394 AA;  43314 MW;  6EDA60255F43358F CRC64;
     MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI DNAPEEKARG
     ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
     LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE
     GDAEWEAKIL ELAGFLDSYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG
     EEVEIVGIKE TQKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGTIK
     PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV
     VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLS
//
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