ID   EFG_STAIN               Reviewed;         693 AA.
AC   Q5U8S9;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 86.
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};
OS   Staphylococcus intermedius.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus; Staphylococcus intermedius group.
OX   NCBI_TaxID=1285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29663 / DSM 20373 / NCTC 11048 / H11;
RX   PubMed=17325218; DOI=10.1128/aac.01542-06;
RA   O'Neill A.J., McLaws F., Kahlmeter G., Henriksen A.S., Chopra I.;
RT   "Genetic basis of resistance to fusidic acid in staphylococci.";
RL   Antimicrob. Agents Chemother. 51:1737-1740(2007).
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; AY776250; AAV39278.1; -; Genomic_DNA.
DR   RefSeq; WP_019169061.1; NZ_MWUY01000001.1.
DR   AlphaFoldDB; Q5U8S9; -.
DR   SMR; Q5U8S9; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..693
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091223"
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   693 AA;  76731 MW;  EAEAA7A4149B3CD3 CRC64;
     MGRDFSLKNT RNIGIMAHID AGKTTTTERI LYYTGRIHKI GETHEGASQM DWMEQEQDRG
     ITITSAATTA EWKNHRVNII DTPGHVDFTV EVERSLRVLD GAVTVLDAQS GVEPQTETVW
     RQATTYGVPR IVFVNKMDKI GANFDYAVST LHDRLQANAA PIQLPIGAED EFSAIIDLVT
     MKCFKYNNDL GTEIEEVEIP EDYRERAEEA REALIEAVAE TNESLMEKIF DEQEITVDEL
     KDAIRQATTD VEFYPVLCGT AFKNKGVQLM LDAVIDYLPS PLDVKPIVGH RADNPDEEVI
     AKADDDAEFA ALAFKVMTDP YVGKLTFFRV YSGTLTSGSY VKNSTKGKRE RVGRILQMHA
     NSREEISSVY SGDIAAAVGL KDTGTGDTLC GEKNDIILES MEFPEPVIHL SVEPKSKADQ
     DKMTQALVKL QEEDPTFKAH TDEETGQVII GGMGELHLDI IVDRMKKEFN VEANVGAPMV
     SYRETFKTSA AVQGKFSRQS GGRGQYGDVH IEFTPNETGA GFEFENAIVG GVVPREYIPS
     VEQGLKDAME NGVLAGYPLI DVKAKLFDGS YHDVDSSEMA FKIAASLALK EAAKKCDPVI
     LEPMMKVTIE MPEEYMGDIM GDVTARRGRV DGMEPRGNAQ VVNAYVPLSE MFGYATSLRS
     NTQGRGTYTM YFDHYAEVPK SISEEIIKKN KGE