EFG_ENTFA
ID EFG_ENTFA Reviewed; 693 AA.
AC Q839G9;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=EF_0200;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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; AE016830; AAO80070.1; -; Genomic_DNA.
DR RefSeq; NP_813999.1; NC_004668.1.
DR RefSeq; WP_002356192.1; NZ_KE136524.1.
DR PDB; 6BK7; X-ray; 1.83 A; A/B=1-404.
DR PDBsum; 6BK7; -.
DR AlphaFoldDB; Q839G9; -.
DR SMR; Q839G9; -.
DR STRING; 226185.EF_0200; -.
DR PRIDE; Q839G9; -.
DR EnsemblBacteria; AAO80070; AAO80070; EF_0200.
DR GeneID; 60892696; -.
DR KEGG; efa:EF0200; -.
DR PATRIC; fig|226185.45.peg.66; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_9; -.
DR OMA; AATTCHW; -.
DR Proteomes; UP000001415; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..693
FT /note="Elongation factor G"
FT /id="PRO_0000091122"
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 10..16
FT /evidence="ECO:0007829|PDB:6BK7"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:6BK7"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:6BK7"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:6BK7"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:6BK7"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:6BK7"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:6BK7"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:6BK7"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:6BK7"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:6BK7"
FT HELIX 204..219
FT /evidence="ECO:0007829|PDB:6BK7"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:6BK7"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:6BK7"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:6BK7"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:6BK7"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:6BK7"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 309..318
FT /evidence="ECO:0007829|PDB:6BK7"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 322..342
FT /evidence="ECO:0007829|PDB:6BK7"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 362..369
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:6BK7"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:6BK7"
SQ SEQUENCE 693 AA; 76679 MW; E093A25A0E57D88F CRC64;
MAREFSLEKT RNIGIMAHVD AGKTTTTERI LYYTGKIHKI GETHEGASQM DWMEQEQERG
ITITSAATTA QWKGYRVNII DTPGHVDFTI EVQRSLRVLD GAVTVLDSQS GVEPQTETVW
RQATEYKVPR IVFCNKMDKI GADFFYSVES LHDRLQANAH PIQIPIGAEE DFTGIIDLIK
MKAEIYTNDL GTDIQETDIP EDYLEKAQEW REKLVEAVAE TDEDLMMKYL EGEEITEEEL
VAGIRQATIN VEFFPVLAGS AFKNKGVQLM LDAVLDYLPS PLDIDAIKGI DTKTDEETTR
PADDEAPFAS LAFKVMTDPF VGRLTFFRVY SGVLESGSYV LNASKGKKER IGRILQMHAN
TRQEIDKVYS GDIAAAVGLK DTTTGDTLCA LDAPVILESI EFPDPVIQVA VEPKSKADQD
KMGVALQKLA EEDPSFRVET NVETGETVIS GMGELHLDVL VDRMKREFKV EANVGAPQVS
YRETFRAATK AEGKFVRQSG GKGQYGHVWV EFTPNEEGKG FEFENAIVGG VVPREYIPAV
EKGLEDSMNN GVLAGYPLVD IKAKLYDGSY HDVDSNETAF RVAASMALKA AAKNANPVIL
EPMMKVTITV PEDYLGDIMG HVTSRRGRVE GMEAHGNSQI VNAMVPLAEM FGYATTLRSA
TQGRGTFMMV FDHYEDVPKS VQEEIIKKNG GNA
