ID   EFGL_THEMA              Reviewed;         683 AA.
AC   Q9X1Y4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Elongation factor G-like protein;
GN   OrderedLocusNames=TM_1651;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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; AE000512; AAD36718.1; -; Genomic_DNA.
DR   PIR; H72227; H72227.
DR   RefSeq; NP_229451.1; NC_000853.1.
DR   RefSeq; WP_004082156.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9X1Y4; -.
DR   SMR; Q9X1Y4; -.
DR   STRING; 243274.THEMA_05990; -.
DR   EnsemblBacteria; AAD36718; AAD36718; TM_1651.
DR   KEGG; tma:TM1651; -.
DR   eggNOG; COG0480; Bacteria.
DR   InParanoid; Q9X1Y4; -.
DR   OMA; KPKIAYR; -.
DR   OrthoDB; 88967at2; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR   GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
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; 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   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; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..683
FT                   /note="Elongation factor G-like protein"
FT                   /id="PRO_0000091278"
FT   DOMAIN          5..267
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         14..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         73..77
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         127..130
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   683 AA;  75903 MW;  E9408FF5A2C6A63C CRC64;
     MGGLQNVRSA ALIGHNGSGK SLLLAQILYK SGLIDKADTK YVDYDPVEEE KGASFSSHVA
     SLEWKGKKVY LIDTPGFSDF ISEVINGIFV SENIISVVNA VAGVEIQTER TWNMADEMKK
     PIIVFVNQMD KERANFENVV AELKERFSRK IVPVVVPIGA AENFEGVVDL LKKKAYRYDG
     DKVQEEDMPE SFNDMRSEIL EDIVEQDEEL MMRYLDGEDI GYDELMRVLK EGYKKGEIVP
     VLSGSALKGI GLDLLLDYLG DIGVSPEEAP SYKALLEDGT EIEVKFSEEE PFCAYIFKSV
     VDQFVGRITF AKVIAGVLRP GDTVVNVQKD VTEKVGHVYV PILKQQKEVE SAGPGEIVVL
     LKLKEGAVGE TLAHRDRRVK IVPPAFPEPM FSRSVHPKSK SDIDKISSGL SRLSDSDPTF
     VWEYDPETGE TVVSGLGAMH LDVMIERLKK IFGVDVEVGK PKIAYRETIT TTAVAEHKHK
     KQTGGHGQYG HVKIQLEPLP RGQGYEFVDK IVGGVIPRNF IPSVDKGIRE AMKKGVLAGY
     PVTDVRVILF DGSYHEVDSS DISFQIAAIQ AFKKGMEAAK PVILEPIMEV EVFVPEENAG
     DVMGEISSRR GRPLGMEPSG KGMVKVKAEV PLAEMLDFSS KLSSITSGRG YFTMRFQRYE
     IVPPNIQEKI IEERRREMQE QEK