EFTU_BRUSU
ID EFTU_BRUSU Reviewed; 391 AA.
AC P64025; Q075P7; Q8YHP2; Q8YHQ4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, 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};
GN Name=tufA {ECO:0000255|HAMAP-Rule:MF_00118};
GN OrderedLocusNames=BR1251, BS1330_I1247;
GN and
GN Name=tufB {ECO:0000255|HAMAP-Rule:MF_00118};
GN OrderedLocusNames=BR1235, BS1330_I1231;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=17014718; DOI=10.1186/1471-2180-6-84;
RA Halling S.M., Jensen A.E.;
RT "Intrinsic and selected resistance to antibiotics binding the ribosome:
RT analyses of Brucella 23S rrn, L4, L22, EF-Tu1, EF-Tu2, efflux and
RT phylogenetic implications.";
RL BMC Microbiol. 6:84-84(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {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}.
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DR EMBL; DQ227935; ABB77373.1; -; Genomic_DNA.
DR EMBL; DQ227956; ABB77352.1; -; Genomic_DNA.
DR EMBL; AE014291; AAN30154.1; -; Genomic_DNA.
DR EMBL; AE014291; AAN30170.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM18572.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM18588.1; -; Genomic_DNA.
DR RefSeq; WP_002970090.1; NZ_KN046804.1.
DR AlphaFoldDB; P64025; -.
DR SMR; P64025; -.
DR PRIDE; P64025; -.
DR EnsemblBacteria; AEM18572; AEM18572; BS1330_I1231.
DR EnsemblBacteria; AEM18588; AEM18588; BS1330_I1247.
DR GeneID; 45124617; -.
DR GeneID; 55590924; -.
DR KEGG; bms:BR1235; -.
DR KEGG; bms:BR1251; -.
DR KEGG; bsi:BS1330_I1231; -.
DR KEGG; bsi:BS1330_I1247; -.
DR PATRIC; fig|204722.22.peg.597; -.
DR HOGENOM; CLU_007265_0_0_5; -.
DR OMA; EGDKEWG; -.
DR PhylomeDB; P64025; -.
DR Proteomes; UP000007104; Chromosome I.
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; cd01884; EF_Tu; 1.
DR CDD; cd03697; EFTU_II; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_B; EF_Tu_B; 1.
DR InterPro; IPR041709; EF-Tu_GTP-bd.
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; T_Tr_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 Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..391
FT /note="Elongation factor Tu"
FT /id="PRO_0000091295"
FT DOMAIN 10..201
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 55..59
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 76..79
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 131..134
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 169..171
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 76..80
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ SEQUENCE 391 AA; 42605 MW; ED4CDF37183A900E CRC64;
MAKSKFERTK PHVNIGTIGH VDHGKTSLTA AITKFFGEFK AYDQIDAAPE ERARGITIST
AHVEYETANR HYAHVDCPGH ADYVKNMITG AAQMDGAILV VSAADGPMPQ TREHILLARQ
VGVPAIVVFL NKCDQVDDAE LLELVELEVR ELLSKYEFPG DEIPIIKGSA LAALEDSSKE
LGEDAIRNLM DAVDSYIPTP ERPIDQPFLM PIEDVFSISG RGTVVTGRVE RGIVKVGEEV
EIVGIKATTK TTVTGVEMFR KLLDQGQAGD NIGALIRGVG REDVERGQVL CKPGSVKPHT
KFKAEAYILT KDEGGRHTPF FTNYRPQFYF RTTDVTGVVT LPAGTEMVMP GDNVAMDVTL
IVPIAMEEKL RFAIREGGRT VGAGIVSSII E
