EFG_MYCLE
ID EFG_MYCLE Reviewed; 701 AA.
AC P30767;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Elongation factor G;
DE Short=EF-G;
GN Name=fusA; Synonyms=efg; OrderedLocusNames=ML1878;
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=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 [2]
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: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000305}.
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DR EMBL; Z14314; CAA78673.1; -; Genomic_DNA.
DR EMBL; AL583923; CAC30832.1; -; Genomic_DNA.
DR PIR; H87143; H87143.
DR PIR; S31150; S31150.
DR RefSeq; NP_302268.1; NC_002677.1.
DR RefSeq; WP_010908589.1; NC_002677.1.
DR AlphaFoldDB; P30767; -.
DR SMR; P30767; -.
DR STRING; 272631.ML1878; -.
DR EnsemblBacteria; CAC30832; CAC30832; CAC30832.
DR KEGG; mle:ML1878; -.
DR PATRIC; fig|272631.5.peg.3552; -.
DR Leproma; ML1878; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_11; -.
DR OMA; AATTCHW; -.
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; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR035649; EFG_V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR004540; Transl_elong_EFG/EF2.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00484; EF-G; 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..701
FT /note="Elongation factor G"
FT /id="PRO_0000091158"
FT DOMAIN 11..287
FT /note="tr-type G"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 84..88
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 138..141
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 564
FT /note="G -> A (in Ref. 1; CAA78673)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 701 AA; 77161 MW; F18B724F35F3181E CRC64;
MAQKDVLTDL TKVRNIGIMA HIDAGKTTTT ERILYYTGIS YKIGEVHDGA ATMDWMEQEQ
ERGITITSAA TTCFWNDNQI NIIDTPGHVD FTVEVERSLR VLDGAVAVFD GKEGVEPQSE
QVWRQADKYE VPRICFVNKM DKIGADFYFS VRTMQERLGA NVIPIQLPVG SEGDFEGVVD
LVEMKAKVWS TEAKLGEKYD VVGIPTDLQE KAEEYRTNLL ETVAETDEAL LEKYFSGEEL
TVAEIKGAIR KLTISSEAYP VLCGSAFKNK GVQPMLDAVI DYLPSPLDVP AAIGHVPGKE
DEEIVRKPST DEPLSALAFK VATHPFFGKL TYVRVYSGKV DSGSQVINAT KGKKERLGKL
FQMHSNKENP VETASAGHIY AVIGLKDTTT GDTLADPNNQ IVLESMTFPD PVIEVAIEPK
TKSDQEKLSL SIQKLAEEDP TFKVHLDSET GQTVIGGMGE LHLDILVDRM RREFKVEANV
GKPQVAYKET IRRVVETVEY THKKQTGGSG QFAKVIIKLE PFSGENGATY EFENKVTGGR
IPREYIPSVE AGARDAMQYG VLAGYPLVNL KVTLLDGAYH DVDSSEIAFK IAGSQVLKKA
AAQAQPVILE PIMAVEVTTP EDYMGDVIGD LHSRRGQIQA MKERAGTRVV RAHVPLSEMF
GYVGDLRSKT QGRANYSMVF NSYSEVPANV SKEIIAKATG E
