AC MF_00054; DC Protein; auto c? TR HAMAP; MF_00054_B; -; 1; level=0 c? TR HAMAP; MF_00054_A; -; 1; level=0 XX Names: EF_G_EF_2 XX case ID EFG DE RecName: Full=Elongation factor G; DE Short=EF-G; end case case ID EF2 DE RecName: Full=Elongation factor 2; DE Short=EF-2; end case GN Name=fusA; XX 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. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-G/EF-2 CC subfamily. XX DR Pfam; PF00679; EFG_C; 1; trigger=no DR Pfam; PF00009; GTP_EFTU; 1; trigger=no DR Pfam; PF03144; GTP_EFTU_D2; 1; trigger=no DR PRINTS; PR00315; ELONGATNFCT; 1; trigger=no DR NCBIfam; TIGR00231; Small_GTP; 1; trigger=no DR NCBIfam; TIGR00484; EF-G; 1; trigger=no DR NCBIfam; TIGR00490; AEF-2; 1; trigger=no DR PROSITE; PS00301; G_TR_1; 1; trigger=no DR PROSITE; PS51722; G_TR_2; 1; trigger=no XX KW Cytoplasm KW Elongation factor KW Protein biosynthesis KW GTP-binding KW Nucleotide-binding XX GO GO:0005525; F:GTP binding GO GO:0003746; F:translation elongation factor activity GO GO:0006414; P:translational elongation GO GO:0005737; C:cytoplasm XX FT From: EFG_ECOLI (P0A6M8) case FT BINDING 17..24 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: [AS]-H-[IV]-D-[AS]-G-K-T FT BINDING 88..92 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: D-T-P-G-H FT BINDING 142..145 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: N-K-x-D end case FT From: EF2_SACS2 (P30925) case FT BINDING 27..34 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: A-H-[IV]-[DH]-H-G-K-T FT BINDING 93..97 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: D-T-P-G-H FT BINDING 147..150 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: N-K-[IV]-D FT MOD_RES 603 FT /note="Diphthamide" FT Condition: H end case XX case Size: 669-715; end case case Size: 726-743; end case Related: MF_03063!; Template: P0A6M8; P13551; P30925; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in ANADE, BDEBA, BORA1, BORAP, BORBR, BORBU, BORGP, BORPA, BURO1, BURMA, BURPS, BURTA, PARXL, DESPS, GEOMG, GEOSL, HAHCH, METCA, MYXXD, PHOPR, POLSJ, PSEA6, PSEAE, PSEPK, CUPMC, RALN1, SACD2, SHEDO, SHEFN, SHEON, SHESM, SHESR, STRCO, SYNAS, SYNWW, SYNY3, TREDE, TREPA, TRIEI, VIBCH, VIBPA, VIBVY Plasmid: in CUPMC, RALN1 Comments: EFG2_BORBU could be made slightly longer in the N-terminal (MVVVGDL) by frameshifting just before the current initiator Met XX # Revision 1.43 2023/11/28 //