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EFG1_BORAP
ID   EFG1_BORAP              Reviewed;         693 AA.
AC   Q0SMX0; G0IQ90;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Elongation factor G 1 {ECO:0000255|HAMAP-Rule:MF_00054};
DE            Short=EF-G 1 {ECO:0000255|HAMAP-Rule:MF_00054};
GN   Name=fusA1 {ECO:0000255|HAMAP-Rule:MF_00054};
GN   OrderedLocusNames=BAPKO_0568, BafPKo_0555;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
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; CP000395; ABH01808.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL69760.1; -; Genomic_DNA.
DR   RefSeq; WP_011601076.1; NC_008277.1.
DR   AlphaFoldDB; Q0SMX0; -.
DR   SMR; Q0SMX0; -.
DR   STRING; 390236.BafPKo_0555; -.
DR   PRIDE; Q0SMX0; -.
DR   EnsemblBacteria; AEL69760; AEL69760; BafPKo_0555.
DR   KEGG; baf:BAPKO_0568; -.
DR   KEGG; bafz:BafPKo_0555; -.
DR   PATRIC; fig|390236.22.peg.533; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_12; -.
DR   OMA; AATTCHW; -.
DR   Proteomes; UP000005216; 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   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.
FT   CHAIN           1..693
FT                   /note="Elongation factor G 1"
FT                   /id="PRO_0000263430"
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:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         80..84
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         134..137
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   CONFLICT        455
FT                   /note="G -> E (in Ref. 2; AEL69760)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   693 AA;  77341 MW;  1D4C7A2BFD206FA2 CRC64;
     MDYNKLRNIG ISAHIDSGKT TLTERILFYC NKIHAIHEVK GKDGVGATMD SMELERERGI
     TIASAATHVE WKDFPINIID TPGHVDFTIE VERSLRVLDG AILVLDSVAG VQSQSITVDR
     QLKRYSVPRL AFVNKCDKTG ANPYNVKDQL RSKLDLNSVL MQIPIGLEDK HIGVIDLVLM
     KAYYFEGKDG TEIIEKEIPS ELLEEAKNKR EMMLDALADF NDELMELHME GKEVPIEIIY
     NAIRTGTLAL KLCPVFMGSA YKNKGVQLLL DAVTRFLPSP HDIKNTALDL NNNEKEIDLK
     IDNNLPTVAL AFKLEDGQYG QLTYVRIYQG TLKKGQELIN SRTSKKFKVG RLIRMHANNT
     EDIEFGGSGD IVALFGIECA SGDTFCDPSI NYSMTSMFIP DPVISLSVKP KDKKSADNMA
     KALGRFTKED PTFKTYVDIE SNETIIQGMG ELHLGVYIER MKREFKAEVE TGMPQVAYRE
     TITGKAEFNY THKKQSGGAG QFGRVAGFME PLNKEGETYE FVNLIKGGVI PTEYIPSCDK
     GFQKAMEKGT LIGFPIVDIK ITINDGQYHI VDSSDIAFQL AAIGAFREAY EKAKPTILEP
     IMKVTLEGPT EFQGNMFGLL NQRRGIITGS LEDGSFSKVE AEVPLSEMFG FSTVLRSSTQ
     GKAEFSMEFL KYGKVPSAIF DELRKKFNDQ NKS
 
 
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