EFG_PHOV8
ID EFG_PHOV8 Reviewed; 705 AA.
AC A6KYJ7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, 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}; OrderedLocusNames=BVU_0807;
OS Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Phocaeicola.
OX NCBI_TaxID=435590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC 11154;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(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; CP000139; ABR38511.1; -; Genomic_DNA.
DR RefSeq; WP_005844844.1; NC_009614.1.
DR AlphaFoldDB; A6KYJ7; -.
DR SMR; A6KYJ7; -.
DR STRING; 435590.BVU_0807; -.
DR EnsemblBacteria; ABR38511; ABR38511; BVU_0807.
DR GeneID; 66751845; -.
DR KEGG; bvu:BVU_0807; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_10; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 88967at2; -.
DR BioCyc; BVUL435590:G1G59-849-MON; -.
DR Proteomes; UP000002861; 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; Reference proteome.
FT CHAIN 1..705
FT /note="Elongation factor G"
FT /id="PRO_1000008803"
FT DOMAIN 7..287
FT /note="tr-type G"
FT REGION 293..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; 77456 MW; 30D96D1199DE545B CRC64;
MAKHDLHLTR NIGIMAHIDA GKTTTSERIL FYTGLTHKIG EVHDGAATMD WMEQEQERGI
TITSAATTTR WKYAGNTYKI NLIDTPGHVD FTAEVERSLR VLDGAVAAYC AVGGVEPQSE
TVWRQADKYN VPRIGYVNKM DRSGADFFEV VRQMKDVLGA NACPVVIPIG AEESFKGVVD
LIKMKAILWH DETMGADYSV EEIPANLVDE ANEWREKMLE KVAEFDDALM EKFFDDPSTI
TEEEILRALR AGTLKMDIVP MFCGSSFKNK GVQTLLDYVC AFLPSPLDTP AIVGTNPTTG
AEEDRKPSED EKTSALAFKI ATDPYVGRLT FFRVYSGKVE AGSYIYNTRS GKKERVSRLF
QMHSNKQNPV EVIGAGDIGA GVGFKDIRTG DTLCDEDAPI VLESMEFPDP VIGIAVEPKT
QKDLDKLSNG LAKLAEEDPT FTVKTDEQSG QTIISGMGEL HLDIIIDRLK REFKVECNQG
KPQVNYKEAI TKTVELREVY KKQSGGRGKF ADIIVAIGPV DEDFTQGGLQ FIDEVKGGNV
PKEFIPSVQK GFQTAMKNGV LAGYPLDSLK VVLKDGSFHP VDSDQLSFEI CAIQAYKNAC
AKAGPVLTEP IMKLEVVTPE ENMGDVIGDL NKRRGQVEGM ESSRSGARIV KAKVPLAEMF
GYVTALRTIT SGRATSSMTY DHHAQVSSSI AKAVLEEVKG RVDLV
