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Database: UniProt/SWISS-PROT
Entry: EFTU_BRUME
LinkDB: EFTU_BRUME
Original site: EFTU_BRUME 
ID   EFTU_BRUME              Reviewed;         391 AA.
AC   P64024; Q8YHP2; Q8YHQ4;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   05-DEC-2018, entry version 88.
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=BMEI0742;
GN   and
GN   Name=tufB {ECO:0000255|HAMAP-Rule:MF_00118};
GN   OrderedLocusNames=BMEI0755;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen
RT   Brucella melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL51923.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE008917; AAL51923.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE008917; AAL51936.1; -; Genomic_DNA.
DR   PIR; AE3346; AE3346.
DR   PIR; AH3344; AH3344.
DR   RefSeq; WP_002970090.1; NZ_GG703785.1.
DR   ProteinModelPortal; P64024; -.
DR   SMR; P64024; -.
DR   STRING; 224914.BAWG_3069; -.
DR   PRIDE; P64024; -.
DR   EnsemblBacteria; AAL51923; AAL51923; BMEI0742.
DR   EnsemblBacteria; AAL51936; AAL51936; BMEI0755.
DR   GeneID; 29593568; -.
DR   KEGG; bme:BMEI0742; -.
DR   KEGG; bme:BMEI0755; -.
DR   KEGG; bmel:DK63_681; -.
DR   PATRIC; fig|224914.52.peg.711; -.
DR   eggNOG; ENOG4105CGV; Bacteria.
DR   eggNOG; COG0050; LUCA.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   BioCyc; BMEL224914:G1FZL-794-MONOMER; -.
DR   BioCyc; BMEL224914:G1FZL-808-MONOMER; -.
DR   Proteomes; UP000000419; 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; 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    391       Elongation factor Tu.
FT                                /FTId=PRO_0000091294.
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;  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
//
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