EFG_BACFR
ID EFG_BACFR Reviewed; 705 AA.
AC Q64NK6;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=BF4183;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD50926.1; -; Genomic_DNA.
DR RefSeq; WP_005791539.1; NZ_UYXF01000007.1.
DR RefSeq; YP_101460.1; NC_006347.1.
DR AlphaFoldDB; Q64NK6; -.
DR SMR; Q64NK6; -.
DR STRING; 295405.BF4183; -.
DR EnsemblBacteria; BAD50926; BAD50926; BF4183.
DR GeneID; 66331194; -.
DR KEGG; bfr:BF4183; -.
DR PATRIC; fig|295405.11.peg.4037; -.
DR HOGENOM; CLU_002794_4_1_10; -.
DR OMA; AATTCHW; -.
DR Proteomes; UP000002197; 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..705
FT /note="Elongation factor G"
FT /id="PRO_0000091065"
FT DOMAIN 7..287
FT /note="tr-type G"
FT REGION 291..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 84..88
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 138..141
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 705 AA; 77508 MW; F61416FD170E1961 CRC64;
MAKNDLHLTR NIGIMAHIDA GKTTTSERIL FYTGLTHKIG EVHDGAATMD WMEQEQERGI
TITSAATTTR WKYAGDTYKI NLIDTPGHVD FTAEVERSLR ILDGAVAAYC AVGGVEPQSE
TVWRQADKYN VPRIAYVNKM DRSGADFFEV VRQMKAVLGA NPCPVVIPIG AEENFKGLVD
LIKMKAIYWH DETMGADYTI EEIPANLVDE ANEWRDKMLE KVAEFDDALM EKYFDDPSTI
TEEEVLRALR NATVQMAVVP MLCGSSFKNK GVQTLLDYVC AFLPSPLDAE NVVGTNPDTG
AEEDRKPSED DKTSALAFKI ATDPYVGRLT FFRVYSGKIE AGSYIYNSRS GKKERVSRLF
QMHSNKQNPV EVIGAGDIGA GVGFKDIHTG DTLCDETAPI VLESMDFPEP VIGIAVEPKT
QKDMDKLSNG LAKLAEEDPT FTVKTDEQTG QTVISGMGEL HLDIIIDRLK REFKVECNQG
KPQVNYKEAI TKTVNLREVY KKQSGGRGKF ADIIVNIGPV DEDFTQGGLQ FVDEVKGGNI
PKEFIPSVQK GFQTAMKNGV LAGYPLDSLK VTLVDGSFHP VDSDQLSFEI CAIQAYKNAC
AKAGPVLMEP IMKLEVVTPE ENMGDVIGDL NKRRGQVEGM ESSRSGARIV KAMVPLAEMF
GYVTALRTIT SGRATSSMVY SHHAQVSSSI AKAVLEEVKG RADLL
