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 08-NOV-2023, entry version 91.
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; Bacillota; 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; cd01886; EF-G; 1.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR CDD; cd04088; EFG_mtEFG_II; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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; IPR047872; EFG_IV.
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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_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 NCBIfam; TIGR00484; EF-G; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
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; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 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
//
