ID   EFG_LYSSC               Reviewed;         692 AA.
AC   B1HMZ1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=Bsph_4625;
OS   Lysinibacillus sphaericus (strain C3-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=444177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3-41;
RX   PubMed=18296527; DOI=10.1128/jb.01652-07;
RA   Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA   Berry C., Yuan Z.;
RT   "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT   sphaericus C3-41 and comparison with those of closely related Bacillus
RT   species.";
RL   J. Bacteriol. 190:2892-2902(2008).
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; CP000817; ACA42069.1; -; Genomic_DNA.
DR   RefSeq; WP_012296073.1; NC_010382.1.
DR   AlphaFoldDB; B1HMZ1; -.
DR   SMR; B1HMZ1; -.
DR   PRIDE; B1HMZ1; -.
DR   EnsemblBacteria; ACA42069; ACA42069; Bsph_4625.
DR   KEGG; lsp:Bsph_4625; -.
DR   HOGENOM; CLU_002794_4_1_9; -.
DR   OMA; AATTCHW; -.
DR   Proteomes; UP000002164; 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.
FT   CHAIN           1..692
FT                   /note="Elongation factor G"
FT                   /id="PRO_1000091729"
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   692 AA;  76432 MW;  966A5F59769DB602 CRC64;
     MKREFSLENT RNIGIMAHID AGKTTTTERI LYYTGKIHKI GETHEGASQM DWMEQEQERG
     ITITSAATTA QWAGHRVNII DTPGHVDFTV EVERSLRVLD GAVTVLDAQS GVEPQTETVW
     RQATTYGVPR IVFINKMDKT GADFLYSVGT LHDRLQANAH PIQLPIGAED QFSAIIDLVE
     MKATFYGDEK GTAVTEGEIP EEYRAQAEEY REKLIDAVAS VDEDIMEKYL EGEEITVAEL
     KAAIRRATIA VEFYPVICGT AFKHKGVRPM LNAVIDYLPS PVDVPAIKGT SVDGDEELER
     KSSDDEPFSA LAFKVMTDPF VGKLTFFRVY SGTLDSGSYV QNSSKGKRER VGRILQMHAN
     SREEISKVFA GDIAAAVGLK DTTTGDTLCD EKNLVILESM EFPEPVISLS VEPKSKADQD
     KMGQALQKLQ EEDPTFRAHT DTETGQTIIS GMGELHLDIL VDRMRREFKV EANVGAPMVS
     YRETFRSSAK VQGKFTRQSG GRGQYGDVTI EFSPNEEGKG FEFENAIVGG VIPREYIPAV
     EAGLRDSLDR GVVAGYPLID IKAKLVFGSY HDVDSNEMAF KIAASMALKE ASKQCDAVIL
     EPMMKVEVVI PEEYLGDIMG NITSRRGRVE GMDARGNSQV VRAMVPLAEM FGYATTLRSA
     TQGRGVFSMT FDHYEEVPKS IAAEIIKKNK GE