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 27-MAR-2024, entry version 108.
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; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC 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 AlphaFoldDB; Q0SMX0; -.
DR SMR; Q0SMX0; -.
DR STRING; 29518.BLA32_01570; -.
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 OrthoDB; 9804431at2; -.
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; cd01886; EF-G; 1.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd04091; mtEFG1_II_like; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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; IPR047872; EFG_IV.
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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_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 NCBIfam; TIGR00484; EF-G; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43636; ELONGATION FACTOR G, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43636:SF2; ELONGATION FACTOR G, MITOCHONDRIAL; 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; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 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
//
