ID   EFG3_MYXXD              Reviewed;         702 AA.
AC   Q1D513;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Elongation factor G 3 {ECO:0000255|HAMAP-Rule:MF_00054};
DE            Short=EF-G 3 {ECO:0000255|HAMAP-Rule:MF_00054};
GN   Name=fusA3 {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=MXAN_4082;
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622;
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA   Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA   Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA   Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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; CP000113; ABF90131.1; -; Genomic_DNA.
DR   RefSeq; WP_011554089.1; NC_008095.1.
DR   AlphaFoldDB; Q1D513; -.
DR   SMR; Q1D513; -.
DR   STRING; 246197.MXAN_4082; -.
DR   PRIDE; Q1D513; -.
DR   EnsemblBacteria; ABF90131; ABF90131; MXAN_4082.
DR   GeneID; 41361412; -.
DR   KEGG; mxa:MXAN_4082; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_7; -.
DR   OMA; AVCQIPW; -.
DR   OrthoDB; 88967at2; -.
DR   Proteomes; UP000002402; 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; 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..702
FT                   /note="Elongation factor G 3"
FT                   /id="PRO_0000263475"
FT   DOMAIN          8..293
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         90..94
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         144..147
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   702 AA;  75746 MW;  35F231766265F29E CRC64;
     MSRHTRIERY RNIGIMAHID AGKTTLTERV LFFTGRIHSV GEVHDGATEM DWLPQEKQRG
     ITITSAATTA FWQPRQGMGA GVPHRINVLD TPGHVDFTIE VERSLRVLDG AVAVFDASQG
     VEPQSEAVWR QADRYNVPRI AFINKMDKVG ADFAMSVASI QARLGARPVA VQWPLGAGSE
     FRGLVDLVRM RAVMFDGEDG SFVDGQAVPE AVRAEVEAQR LRLIEACADE DATVLEKFVD
     GRLEDITAED LERALRSGAL ARTLVPVLCG SAFKKKGVQM LLDAIVNYLP APSDMPAVEG
     FVPGKEERVS RPVSDSGPPC ALAFKLMSDK AVGGIVFLRV YSGTLRAGTV LLNPATGRRE
     RVGRLMFMHA NRREEVAEVH AGDICAALGL KGVRTGDTLC DPAEPVVLES LGVMEPVVQL
     AVEARSPAEL TKLEDGLHRL AAEDPSLRVG VDPESGQVLL SGMGELHLEV VVDRLRTEHG
     VEARVGQPKV AWRDTLRRQV RQEYRHVRQS GGPGQYAYVV LDVGPAPRGA GLVFTDDTRG
     GTIPKELVPA IEKGVAGAMA RGVRDGVPLV DVEVRLLDGD THVRDSTPQA FAVAGSLALQ
     AAAHRAGVQQ LEPVMEVEVT TPEEYLGEVL GDLAARRGRV LGMEARGVVR LVSARVPMAS
     LFGYVTGLRG RTQGRAQASM RLGAYEPVPE ALQASYAAEA RA