EFTU_MYCLE
ID EFTU_MYCLE Reviewed; 396 AA.
AC P30768;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 138.
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=ML1877;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8341612; DOI=10.1093/nar/21.14.3327;
RA Silbak F., Bercovier H.;
RT "Nucleotide sequence of Mycobacterium leprae elongation factor (EF-Tu)
RT gene.";
RL Nucleic Acids Res. 21:3327-3327(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8446028; DOI=10.1111/j.1365-2958.1993.tb01112.x;
RA Honore N.T., Bergh S., Chanteau S., Doucet-Populaire F., Eiglmeier K.,
RA Garnier T., Georges C., Launois P., Limpaiboon T., Newton S., Niang K.,
RA del Portillo P., Ramesh G.R., Reddi P., Ridel P.R., Sittisombut N.,
RA Wu-Hunter S., Cole S.T.;
RT "Nucleotide sequence of the first cosmid from the Mycobacterium leprae
RT genome project: structure and function of the Rif-Str regions.";
RL Mol. Microbiol. 7:207-214(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8089081; DOI=10.1093/oxfordjournals.jbchem.a124393;
RA Dhandayuthapani S., Banu J.M., Kashiwabara Y.;
RT "Cloning and sequence determination of the gene coding for the elongation
RT factor Tu of Mycobacterium leprae.";
RL J. Biochem. 115:664-669(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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; L13276; AAA71969.1; -; Unassigned_DNA.
DR EMBL; Z14314; CAA78674.1; -; Genomic_DNA.
DR EMBL; D13869; BAA02982.2; -; Genomic_DNA.
DR EMBL; AL583923; CAC30831.1; -; Genomic_DNA.
DR PIR; G87143; G87143.
DR PIR; S31151; S31151.
DR RefSeq; NP_302267.1; NC_002677.1.
DR RefSeq; WP_010908588.1; NC_002677.1.
DR AlphaFoldDB; P30768; -.
DR SMR; P30768; -.
DR STRING; 272631.ML1877; -.
DR EnsemblBacteria; CAC30831; CAC30831; CAC30831.
DR KEGG; mle:ML1877; -.
DR PATRIC; fig|272631.5.peg.3551; -.
DR Leproma; ML1877; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_11; -.
DR OMA; EGDKEWG; -.
DR Proteomes; UP000000806; 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; 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; Reference proteome.
FT CHAIN 1..396
FT /note="Elongation factor Tu"
FT /id="PRO_0000091348"
FT DOMAIN 10..205
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 62..66
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 83..86
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 138..141
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 175..177
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 83..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 138..141
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT CONFLICT 129..152
FT /note="GVPYILVALNKSDAVDDEELLELV -> VYLTSWSHLTSPTPWTTRNYSSLS
FT (in Ref. 2; CAA78674)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="L -> V (in Ref. 2; CAA78674)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="G -> A (in Ref. 2; CAA78674)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="R -> P (in Ref. 3; BAA02982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 43668 MW; D9CB88343C642778 CRC64;
MAKAKFERTK PHVNIGTIGH VDHGKTTLTA AITKVLHDKF PNLNESRAFD QIDNAPEERQ
RGITINISHV EYQTEKRHYA HVDAPGHADY IKNMITGAAQ MDGAILVVAA TDGPMPQTRE
HVLLARQVGV PYILVALNKS DAVDDEELLE LVEMEVRELL AAQEFDEDAP VVRVSALKAL
EGDAKWVESV TQLMDAVDES IPAPVRETDK PFLMPVEDVF TITGRGTVVT GRVERGVVNV
NEEVEIVGIR QTTTKTTVTG VEMFRKLLDQ GQAGDNVGLL LRGIKREDVE RGQVVIKPGT
TTPHTEFEGQ VYILSKDEGG RHTPFFNNYR PQFYFRTTDV TGVVTLPEGT EMVMPGDNTN
ISVTLIQPVA MDEGLRFAIR EGGRTVGAGR VVKIIK
