EFG_THEMA
ID EFG_THEMA Reviewed; 692 AA.
AC P38525;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Elongation factor G;
DE Short=EF-G;
GN Name=fusA; Synonyms=fus; OrderedLocusNames=TM_1503;
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 [GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=1920450; DOI=10.1007/bf02193628;
RA Tiboni O., Cantoni R., Creti R., Cammarano P., Sanangelantoni A.M.;
RT "Phylogenetic depth of Thermotoga maritima inferred from analysis of the
RT fus gene: amino acid sequence of elongation factor G and organization of
RT the Thermotoga str operon.";
RL J. Mol. Evol. 33:142-151(1991).
RN [2]
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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB19927.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAD36570.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S57688; AAB19927.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE000512; AAD36570.1; ALT_INIT; Genomic_DNA.
DR PIR; H72243; H72243.
DR RefSeq; NP_229303.1; NC_000853.1.
DR AlphaFoldDB; P38525; -.
DR SMR; P38525; -.
DR STRING; 243274.THEMA_06785; -.
DR EnsemblBacteria; AAD36570; AAD36570; TM_1503.
DR KEGG; tma:TM1503; -.
DR eggNOG; COG0480; Bacteria.
DR InParanoid; P38525; -.
DR OMA; AATTCHW; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 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 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..692
FT /note="Elongation factor G"
FT /id="PRO_0000091246"
FT DOMAIN 9..283
FT /note="tr-type G"
FT BINDING 18..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 82..86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 105
FT /note="A -> R (in Ref. 1; AAB19927)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="E -> A (in Ref. 1; AAB19927)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="V -> F (in Ref. 1; AAB19927)"
FT /evidence="ECO:0000305"
FT CONFLICT 390..391
FT /note="CD -> WH (in Ref. 1; AAB19927)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="T -> N (in Ref. 1; AAB19927)"
FT /evidence="ECO:0000305"
FT CONFLICT 527..539
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 692 AA; 77846 MW; 02A4DCCD91547580 CRC64;
MEARYVDLDK LRNIGIMAHI DAGKTTTTER ILYYTGRKHF IGDVDEGNTT TDWMPQEKER
GITIQSAATT CFWKGYRINI IDTPGHVDFT AEVERALRVL DGAIAVFDAT AGVEPQSETV
WRQADKYNVP RIAFMNKMDK VGADFYMAVE TLVTKLRANP IPVQMPIGSE KDFQGVIDLI
KMKAIYWVSE DGSVYEERDI PEELREEAEM RREEMLEKIA ELDEEILEKY LEGEEISEEE
IKRVLRKATI ENKAVPVLCG AAKANKGIQP LLDAVIDYLP SPLDLPPVKG WRVSDGEVVY
RKPDENEPFT ALVFKVQVDP YIGKLVYFRV YSGRLEKGSY VYNSTKGQRE RISRIVFMHA
DKREEVDYVR PGDIAAGVGL KVSQTGDTLC DEKEPIILEK IDFPEPVISL AVEPVTKADE
EKLVKALLAL SEEDPTLQVR VDKETGETII SGMGELHLEI VVDRLKREFG VNVRVGQPQV
AYRETIKKSA EAEGKYIRQT GGRGQYGHVI LRIEPIPEEE GKNFEFIDKT VGGVIPKEFM
PAIEAGIKEA MMAGPLAGYP VVRVRAIVLD GSYHEVDSSE MAFKIAASMA FKEAMKKAQP
VLLEPIMKLE ITTPEEYMGN IISDLNSRRA KVESLETRGH LKVIVAKVPL SETFGYATVL
RSLSQGRASY IMQFSHYQEV PEKIAEKIIK VV
