EFG1_BORBU
ID EFG1_BORBU Reviewed; 693 AA.
AC O30913; O51490;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Elongation factor G 1;
DE Short=EF-G 1;
GN Name=fusA; Synonyms=fus1; OrderedLocusNames=BB_0540;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DK1;
RA Sonderbye L., Hindersson P., Pedersen S.;
RT "Putative sequence for Borrelia burgdorferi elongation factor G (EF-G)
RT gene.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF021260; AAB71893.1; -; Genomic_DNA.
DR EMBL; AE000783; AAC66897.1; -; Genomic_DNA.
DR PIR; C70167; C70167.
DR RefSeq; NP_212674.1; NC_001318.1.
DR RefSeq; WP_002557127.1; NC_001318.1.
DR AlphaFoldDB; O30913; -.
DR SMR; O30913; -.
DR STRING; 224326.BB_0540; -.
DR PRIDE; O30913; -.
DR EnsemblBacteria; AAC66897; AAC66897; BB_0540.
DR KEGG; bbu:BB_0540; -.
DR PATRIC; fig|224326.49.peg.931; -.
DR HOGENOM; CLU_002794_4_1_12; -.
DR OMA; AATTCHW; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
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 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; IPR045044; EFG1-like.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/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 PANTHER; PTHR43636; PTHR43636; 1.
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..693
FT /note="Elongation factor G 1"
FT /id="PRO_0000091080"
FT DOMAIN 4..281
FT /note="tr-type G"
FT BINDING 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 80..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 134..137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 201
FT /note="D -> E (in Ref. 1; AAB71893)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="S -> N (in Ref. 1; AAB71893)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="I -> M (in Ref. 1; AAB71893)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="T -> A (in Ref. 1; AAB71893)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="T -> I (in Ref. 1; AAB71893)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="T -> I (in Ref. 1; AAB71893)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="E -> S (in Ref. 1; AAB71893)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="I -> T (in Ref. 1; AAB71893)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="R -> G (in Ref. 1; AAB71893)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="R -> A (in Ref. 1; AAB71893)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="D -> N (in Ref. 1; AAB71893)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="R -> K (in Ref. 1; AAB71893)"
FT /evidence="ECO:0000305"
FT CONFLICT 671
FT /note="R -> K (in Ref. 1; AAB71893)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="T -> A (in Ref. 1; AAB71893)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="D -> R (in Ref. 1; AAB71893)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 693 AA; 77573 MW; F8A44C38D58F9B1E CRC64;
MDYNKLRNIG ISAHIDSGKT TLTERILFYC NKIHAIHEVK GKDGVGATMD SMELERERGI
TIASAATHVE WKDFPINIID TPGHVDFTIE VERSLRVLDG AILVLDSVAG VQSQSITVDR
QLKRYSVPRL AFVNKCDKTG ANPYNVKDQL RSKLDLNSVL MQIPIGLEDK HIGVIDLVLM
KAYYFEGKDG TEIIEKEIPS DLLEEAKSKR EIMLDTLADF NDELMELHME GKEVPTEIIY
NATRTGTLAL KLCPVFMGSA YKNKGVQLLL DAVTRFLPSP HDIKNTALDL NNNEKEIDLK
IDNELPTVAL AFKLEDGQYG QLTYVRIYQG ILKKGQELIN SRTSKKFKVG RLIRMHANNT
EDIEFGGSGD IVALFGIECA SGDTFCDPSI NYSMTSMFIP DPVISLSVKP KDKKSADNMA
KALGRFTKED PTFKTYVDIE SNETIIQGMG ELHLEVYIER MKREFKAEVE TGMPQVAYRE
TITRKAEFNY THKKQSGGAG QFGRVAGFME PLDKEGETYE FVNLIKGGVI PTEYIPSCDK
GFQKAMERGT LIGFPIVDIK ITINDGQYHI VDSSDIAFQL AAIGAFREAY EKAKPTILEP
IMKVTLEGPT EFQGNMFGLL NQRRGIITGS LEDGSFSKVE AEVPLSEMFG FSTVLRSSTQ
GKAEFSMEFL RYGKVPSTIF DELRKKFNDQ NKS
