ID   EFG_DESAP               Reviewed;         689 AA.
AC   B1I1I5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Elongation factor G {ECO:0000255|HAMAP-Rule:MF_00054};
DE            Short=EF-G {ECO:0000255|HAMAP-Rule:MF_00054};
GN   Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=Daud_0222;
OS   Desulforudis audaxviator (strain MP104C).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC   Candidatus Desulforudis.
OX   NCBI_TaxID=477974;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP104C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA   Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT   "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00054}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00054}.
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|HAMAP-Rule:MF_00054}.
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DR   EMBL; CP000860; ACA58783.1; -; Genomic_DNA.
DR   RefSeq; WP_012301375.1; NC_010424.1.
DR   AlphaFoldDB; B1I1I5; -.
DR   SMR; B1I1I5; -.
DR   STRING; 477974.Daud_0222; -.
DR   EnsemblBacteria; ACA58783; ACA58783; Daud_0222.
DR   KEGG; dau:Daud_0222; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_9; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 88967at2; -.
DR   Proteomes; UP000008544; 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..689
FT                   /note="Elongation factor G"
FT                   /id="PRO_1000091706"
FT   DOMAIN          8..282
FT                   /note="tr-type G"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         135..138
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   689 AA;  76485 MW;  8E52E1106508E68D CRC64;
     MARVFPLERT RNIGIMAHID AGKTTTTERI LFYTGRVHRI GEVDDGAATM DWMVQEQERG
     ITITSAATTC YWRDYRINII DTPGHVDFTV EVERSLRVLD GAIAVFDAVA GVEPQSETVW
     RQADKYRVPR IVYLNKMDRV GADFFKSMQS IKTKLGSDPV AVQIPLGAED RFVGMIDLVT
     RKAFIYTDDL GTKIKEIPIP ADLTGVVAEY REKLLEMVAE TDEELMIKYL NGEELTVEDI
     KIGIRKATLA VKKFPVLCGS SYRNKGVQPL LDAVVDYLPA PTDVPAVCGI DQRTGREDRR
     VARDDEPFSA LAFKVMVDPY VGKLTFFRVY SGTVNSGSHV YNSTKQKKER IGRLLQMHAN
     HREEIEAAHA GDIIGAVGLK FTSTGDTLSD EEHPIILEAM EFPEPVISIA IEPKTKGDQD
     KMGVALQRLA EEDPTFKIQS NEETGQTLIS GMGELHLEII VDRLLREFKV QANIGRPQVA
     YKETIKGIAQ AEGRFIRQTG GRGQYGHVVI VVEPLDRGKG FAFSNQIVGG VVPKEFIPAV
     ETGVREALTS GVLFGYPVAD VKVSLVDGSY HPVDSSEVAF KIAASMAVKK AVANASPVLL
     EPIMRVEVVL PEDYVGDVIS DLNSRRGHIT QMEHQGKTQI VRADVPLAEM FGYATELRSR
     TQGRGNHTMQ FDHYAEVPQN IADKMIRKY