EFG2_BORAP
ID EFG2_BORAP Reviewed; 669 AA.
AC Q0SMG2; G0IRE6;
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 2;
DE Short=EF-G 2;
GN Name=fusA2; OrderedLocusNames=BAPKO_0736, BafPKo_0717;
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 (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:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; CP000395; ABH01966.1; -; Genomic_DNA.
DR EMBL; CP002933; AEL69912.1; -; Genomic_DNA.
DR RefSeq; WP_011601171.1; NC_017238.1.
DR AlphaFoldDB; Q0SMG2; -.
DR SMR; Q0SMG2; -.
DR STRING; 390236.BafPKo_0717; -.
DR EnsemblBacteria; AEL69912; AEL69912; BafPKo_0717.
DR KEGG; baf:BAPKO_0736; -.
DR KEGG; bafz:BafPKo_0717; -.
DR PATRIC; fig|390236.22.peg.684; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_12; -.
DR OMA; AVCQIPW; -.
DR OrthoDB; 88967at2; -.
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; 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.
FT CHAIN 1..669
FT /note="Elongation factor G 2"
FT /id="PRO_0000263431"
FT DOMAIN 1..276
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 74..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 128..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 669 AA; 75265 MW; 5585213A450D270E CRC64;
MGIRNIGIMA HIDAGKTTTT ERIIYYTGKS HKMGDVDSGN TITDWMPQEQ ERGITISSAA
ITCHWKEHQI NIIDTPGHVD FTAEVERSLR VLDGGIVIFS AVDGIQAQTE TVWKQAEKYE
IPRLAYVNKM DRVGANFFKV VEDIENKFKT IPLVLQIPIG NESNFEGVVD IILNKELHFA
MENGIPKLTY SQIREEFIEK TALFKKKLID ILSQFSEEIT QLFLEDKEIS LDVIKSEIRR
GTISRFIIPV LMGTSLKNIG IEPLIDSIVD YLPSPFEKSF TAFSLDTNKK ILVDPNENKK
LSALVFKVQY SSVIAAHLYF VRVYSGEINS NKKIFNASNG KREKFTKIFR VFSNKNEQID
FVKTGDIGAV LGLKFSVTGD TLIEENNNIL LESVMFPEPV VLMSVEPERS SDEVRLKEIF
EIISKEDPTF SYSESKETGQ LIISGMGELH LEIILTRIKD EFNLNVYTGK PQVSYRESAG
KIVKEVFEFN NIFAGKNINF KIGMIIKPLS RGEGNKIDFE CSIDSTIKSA ILRGITTTFV
SGAFGYPIID INVIIFSIVC EISKISESVF ESISGFAFHS IFQKSDPIRL EPIMLLEIRT
PIEHTGEIIS TLNVIGGVIH SVSNIGEYDL IKSEAAFEKL FGYASILRSS TKGRGSFTME
FSYFKEKVS
