ID   EFGL_MYCTO              Reviewed;         714 AA.
AC   P9WNM8; L0T2N7; O07170;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Elongation factor G-like protein;
GN   OrderedLocusNames=MT0128;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR   EMBL; AE000516; AAK44352.1; -; Genomic_DNA.
DR   PIR; A70983; A70983.
DR   RefSeq; WP_003400860.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNM8; -.
DR   SMR; P9WNM8; -.
DR   PRIDE; P9WNM8; -.
DR   EnsemblBacteria; AAK44352; AAK44352; MT0128.
DR   GeneID; 45424086; -.
DR   KEGG; mtc:MT0128; -.
DR   PATRIC; fig|83331.31.peg.137; -.
DR   HOGENOM; CLU_002794_4_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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   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; 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; 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   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; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding.
FT   CHAIN           1..714
FT                   /note="Elongation factor G-like protein"
FT                   /id="PRO_0000427099"
FT   DOMAIN          21..289
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          30..37
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          73..77
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          94..97
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          148..151
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          267..269
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         30..37
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         94..98
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         148..151
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   714 AA;  75603 MW;  16314E920929115A CRC64;
     MADRVNASQG AAAAPTANGP GGVRNVVLVG PSGGGKTTLI EALLVAAKVL SRPGSVTEGT
     TVCDFDEAEI RQQRSVGLAV ASLAYDGIKV NLVDTPGYAD FVGELRAGLR AADCALFVIA
     ANEGVDEPTK SLWQECSQVG MPRAVVITKL DHARANYREA LTAAQDAFGD KVLPLYLPSG
     DGLIGLLSQA LYEYADGKRT TRTPAESDTE RIEEARGALI EGIIEESEDE SLMERYLGGE
     TIDESVLIQD LEKAVARGSF FPVIPVCSST GVGTLELLEV ATRGFPSPME HPLPEVFTPQ
     GVPHAELACD NDAPLLAEVV KTTSDPYVGR VSLVRVFSGT IRPDTTVHVS GHFSSFFGGG
     TSNTHPDHDE DERIGVLSFP LGKQQRPAAA VVAGDICAIG KLSRAETGDT LSDKAEPLVL
     KPWTMPEPLL PIAIAAHAKT DEDKLSVGLG RLAAEDPTLR IEQNQETHQV VLWCMGEAHA
     GVVLDTLANR YGVSVDTIEL RVPLRETFAG NAKGHGRHIK QSGGHGQYGV CDIEVEPLPE
     GSGFEFLDKV VGGAVPRQFI PSVEKGVRAQ MDKGVHAGYP VVDIRVTLLD GKAHSVDSSD
     FAFQMAGALA LREAAAATKV ILLEPIDEIS VLVPDDFVGA VLGDLSSRRG RVLGTETAGH
     DRTVIKAEVP QVELTRYAID LRSLAHGAAS FTRSFARYEP MPESAAARVK AGAG