ID   EFG_RHIRD               Reviewed;         699 AA.
AC   P70782;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
GN   Name=fusA;
OS   Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS   radiobacter).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8892818; DOI=10.1128/jb.178.21.6192-6199.1996;
RA   Syvaenen A.-C., Amiri H., Jamal A., Andersson S.G.E., Kurland C.G.;
RT   "A chimeric disposition of the elongation factor genes in Rickettsia
RT   prowazekii.";
RL   J. Bacteriol. 178:6192-6199(1996).
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}.
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DR   EMBL; X99673; CAA67990.1; -; Genomic_DNA.
DR   AlphaFoldDB; P70782; -.
DR   SMR; P70782; -.
DR   STRING; 1082932.ATCR1_17692; -.
DR   eggNOG; COG0480; Bacteria.
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.
FT   CHAIN           1..699
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091054"
FT   DOMAIN          8..288
FT                   /note="tr-type G"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         86..90
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         140..143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   699 AA;  78045 MW;  E72A1081DEC28E2B CRC64;
     MAREYKIEDY RNFGIMAHID AGKTTTTERI LYYTGKSHKI GEVHDGAATM DWMEQEQERG
     ITITTAATTT FWKGRDGKMR RFNIIDTPGH VDFTIEVERS LRVLDGAIAL LDANAGVEPQ
     TETVWRQAEK YNVPRMIFCN KMDKTGADFY RSVEMIKTRL GATAVVMQLP IGAETEFKGV
     IDLIEMNALI WRDESLGAQW DVVEIPDDLK AKADEYREKL IETVVEIDEE AMEDYLNGIM
     PDNDKIRALV RRGTIDVKFL PMFCGTAFKN KGVQPLLDAV VDYLPSPLDI PAIKGIDFKT
     EAEIERHADD SEPLSMLAFK IMNDPFVGSL TFARIYSGKL EKGTSVINTV KDKREAVGRM
     LQMHSNSRED IEEAFAGDIV ALAGHKETTT GDTLCDPLKP VILERMEFPE PVIQIAIEPK
     TKGDQEKMGL ALNRRAAEDP SFRVKTDEES GQTYYAGMGE LHLDILVDRM RREFKVEATV
     GAPQVAYRET ITRHDEEDYT HKKQSGGTGQ FARVKIIFEP NPEGEDFKFE SKIVGGAVPK
     EYIPGVQKGI ESVLSSGPLA GFPMLGVKAT LIDGAYHDVD SSVLAFEIAS RACFREAAKK
     AGAQLLEPMM KVEVVTPEDY VGDVIGDLNS RRGQIQGQES RGITIVISAH VPLANMFKYV
     DNLRSMSQGR AQYSMTFDHY SPVPSNVAQE IQAKYSGQK