EFG_BACTN
ID EFG_BACTN Reviewed; 705 AA.
AC Q8A474;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=BT_2729;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(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; AE015928; AAO77835.1; -; Genomic_DNA.
DR RefSeq; NP_811641.1; NC_004663.1.
DR RefSeq; WP_008762033.1; NZ_UYXG01000001.1.
DR AlphaFoldDB; Q8A474; -.
DR SMR; Q8A474; -.
DR STRING; 226186.BT_2729; -.
DR PaxDb; Q8A474; -.
DR PRIDE; Q8A474; -.
DR EnsemblBacteria; AAO77835; AAO77835; BT_2729.
DR GeneID; 45362445; -.
DR GeneID; 60923900; -.
DR KEGG; bth:BT_2729; -.
DR PATRIC; fig|226186.12.peg.2772; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_10; -.
DR InParanoid; Q8A474; -.
DR OMA; AATTCHW; -.
DR Proteomes; UP000001414; 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 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..705
FT /note="Elongation factor G"
FT /id="PRO_0000091072"
FT DOMAIN 7..287
FT /note="tr-type G"
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; 77587 MW; 5168F514AF2C7876 CRC64;
MAKTDLHLTR NIGIMAHIDA GKTTTSERIL FYTGLTHKIG EVHDGAATMD WMEQEQERGI
TITSAATTTR WKYAGDTYKI NLIDTPGHVD FTAEVERSLR ILDGAVAAYC AVGGVEPQSE
TVWRQADKYN VPRIAYVNKM DRSGADFFEV VRQMKAVLGA NPCPIVVPIG AEETFKGLVD
LIKMKAIYWH DETMGADYTV EEIPADLVDE ANEWRDKMLE KVAEFDDALM EKYFDDPSTI
TEEEVLRALR NATVQMAVVP MLCGSSFKNK GVQTLLDYVC AFLPSPLDTE NVIGTNPNTG
AEEDRKPSDD EKTSALAFKI ATDPYVGRLT FFRVYSGKIE AGSYIYNSRS GKKERVSRLF
QMHSNKQNPV EVIGAGDIGA GVGFKDIHTG DTLCDETAPI VLESMDFPEP VIGIAVEPKT
QKDMDKLSNG LAKLAEEDPT FTVKTDEQTG QTVISGMGEL HLDIIIDRLK REFKVECNQG
KPQVNYKEAI TKTVDLREVY KKQSGGRGKF ADIIVKIGPV DEDFKEGGLQ FIDEVKGGNI
PKEFIPSVQK GFTSAMKNGV LAGYPLDSMK VTLIDGSFHP VDSDQLSFEI CAIQAYKNAC
AKAGPVLMEP IMKLEVVTPE ENMGDVIGDL NKRRGQVEGM ESSRSGARIV KAMVPLAEMF
GYVTALRTIT SGRATSSMVY SHHAQVSNSI AKAVLEEVKG RADLL
