EFG_STAA8
ID EFG_STAA8 Reviewed; 693 AA.
AC Q2G0N1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 106.
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};
GN OrderedLocusNames=SAOUHSC_00529;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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 -!- INTERACTION:
CC Q2G0N1; Q8GNY5: far1; Xeno; NbExp=3; IntAct=EBI-16223558, EBI-16223542;
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; CP000253; ABD29677.1; -; Genomic_DNA.
DR RefSeq; WP_000090315.1; NZ_LS483365.1.
DR RefSeq; YP_499101.1; NC_007795.1.
DR PDB; 2MZW; NMR; -; A=401-693.
DR PDBsum; 2MZW; -.
DR AlphaFoldDB; Q2G0N1; -.
DR SMR; Q2G0N1; -.
DR DIP; DIP-60012N; -.
DR IntAct; Q2G0N1; 1.
DR STRING; 1280.SAXN108_0601; -.
DR EnsemblBacteria; ABD29677; ABD29677; SAOUHSC_00529.
DR GeneID; 3920382; -.
DR KEGG; sao:SAOUHSC_00529; -.
DR PATRIC; fig|93061.5.peg.475; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_9; -.
DR OMA; AATTCHW; -.
DR PRO; PR:Q2G0N1; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..693
FT /note="Elongation factor G"
FT /id="PRO_0000263515"
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"
FT STRAND 407..416
FT /evidence="ECO:0007829|PDB:2MZW"
FT HELIX 417..433
FT /evidence="ECO:0007829|PDB:2MZW"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:2MZW"
FT STRAND 447..454
FT /evidence="ECO:0007829|PDB:2MZW"
FT HELIX 455..468
FT /evidence="ECO:0007829|PDB:2MZW"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:2MZW"
FT STRAND 490..498
FT /evidence="ECO:0007829|PDB:2MZW"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:2MZW"
FT STRAND 505..514
FT /evidence="ECO:0007829|PDB:2MZW"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:2MZW"
FT HELIX 535..537
FT /evidence="ECO:0007829|PDB:2MZW"
FT HELIX 538..549
FT /evidence="ECO:0007829|PDB:2MZW"
FT TURN 550..552
FT /evidence="ECO:0007829|PDB:2MZW"
FT STRAND 563..570
FT /evidence="ECO:0007829|PDB:2MZW"
FT HELIX 578..596
FT /evidence="ECO:0007829|PDB:2MZW"
FT STRAND 604..612
FT /evidence="ECO:0007829|PDB:2MZW"
FT HELIX 616..624
FT /evidence="ECO:0007829|PDB:2MZW"
FT TURN 625..627
FT /evidence="ECO:0007829|PDB:2MZW"
FT STRAND 634..636
FT /evidence="ECO:0007829|PDB:2MZW"
FT STRAND 639..647
FT /evidence="ECO:0007829|PDB:2MZW"
FT HELIX 654..661
FT /evidence="ECO:0007829|PDB:2MZW"
FT STRAND 670..675
FT /evidence="ECO:0007829|PDB:2MZW"
FT HELIX 680..689
FT /evidence="ECO:0007829|PDB:2MZW"
SQ SEQUENCE 693 AA; 76612 MW; BAE273E3A33EEED9 CRC64;
MAREFSLEKT RNIGIMAHID AGKTTTTERI LYYTGRIHKI GETHEGASQM DWMEQEQDRG
ITITSAATTA AWEGHRVNII DTPGHVDFTV EVERSLRVLD GAVTVLDAQS GVEPQTETVW
RQATTYGVPR IVFVNKMDKL GANFEYSVST LHDRLQANAA PIQLPIGAED EFEAIIDLVE
MKCFKYTNDL GTEIEEIEIP EDHLDRAEEA RASLIEAVAE TSDELMEKYL GDEEISVSEL
KEAIRQATTN VEFYPVLCGT AFKNKGVQLM LDAVIDYLPS PLDVKPIIGH RASNPEEEVI
AKADDSAEFA ALAFKVMTDP YVGKLTFFRV YSGTMTSGSY VKNSTKGKRE RVGRLLQMHA
NSRQEIDTVY SGDIAAAVGL KDTGTGDTLC GEKNDIILES MEFPEPVIHL SVEPKSKADQ
DKMTQALVKL QEEDPTFHAH TDEETGQVII GGMGELHLDI LVDRMKKEFN VECNVGAPMV
SYRETFKSSA QVQGKFSRQS GGRGQYGDVH IEFTPNETGA GFEFENAIVG GVVPREYIPS
VEAGLKDAME NGVLAGYPLI DVKAKLYDGS YHDVDSSEMA FKIAASLALK EAAKKCDPVI
LEPMMKVTIE MPEEYMGDIM GDVTSRRGRV DGMEPRGNAQ VVNAYVPLSE MFGYATSLRS
NTQGRGTYTM YFDHYAEVPK SIAEDIIKKN KGE
