ID   EFG2_BORGP              Reviewed;         669 AA.
AC   Q660H9;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Elongation factor G 2 {ECO:0000255|HAMAP-Rule:MF_00054};
DE            Short=EF-G 2 {ECO:0000255|HAMAP-Rule:MF_00054};
GN   Name=fusA2 {ECO:0000255|HAMAP-Rule:MF_00054}; Synonyms=fus-2;
GN   OrderedLocusNames=BG0715;
OS   Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS   PBi) (Borrelia bavariensis).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=290434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX   PubMed=15547252; DOI=10.1093/nar/gkh953;
RA   Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA   Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT   "Comparative analysis of the Borrelia garinii genome.";
RL   Nucleic Acids Res. 32:6038-6046(2004).
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; CP000013; AAU07542.1; -; Genomic_DNA.
DR   RefSeq; WP_011193995.1; NZ_CP028872.1.
DR   AlphaFoldDB; Q660H9; -.
DR   SMR; Q660H9; -.
DR   STRING; 290434.BG0715; -.
DR   EnsemblBacteria; AAU07542; AAU07542; BG0715.
DR   KEGG; bga:BG0715; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_2_12; -.
DR   OMA; AVCQIPW; -.
DR   OrthoDB; 88967at2; -.
DR   Proteomes; UP000002276; 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; 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   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_0000091083"
FT   DOMAIN          1..276
FT                   /note="tr-type G"
FT   BINDING         10..17
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         74..78
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         128..131
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   669 AA;  75081 MW;  A8CD0CDB4F5EC250 CRC64;
     MSIRNIGIMA HIDAGKTTTT ERIIYYTGKS HKIGDVDSGN TITDWMPQEQ ERGITISSAA
     ITCHWKDCQI NIIDTPGHVD FTAEVERSLR VLDGGVVIFS AVDGIQAQTE TVWKQSEKYE
     IPRLAYINKM DRLGANFFKV VGDIENKFKT IPLILQIPIG NESNFEGVVD IILNKELHFA
     MENGIPKLTY SPIREEFAEK VGFFKKKLID ILSQFSEEIT QLFLEDKEIS LDIIKSEIRR
     GTISRFIIPV LMGTSLKNIG IEPLIDSIVD YLPSPFEKNF SAFSLDANKK ILVNPNENKK
     LSALVFKVQY SSVIAAHLYF VRVYSGEINS SKKIFNASNG KREKFTKIFR VFSNKNEQID
     CVKTGDIGAV LGLKFSFTGD TLVEENNNVL LESVTFPEPV VLMSVEPERS SDEVRLREIF
     GIISKEDPTF SYYESKETGQ LIISGMGELH LEIILTRIKD EFNLNVYTGK PQVSYRESAG
     KIVKEVFEFN NIFAGKNIDF KIGMIIKPLP RGEGNKIDFE CDINPTIKSA IFRGITTAFV
     SGVFGYPIID INVGIFSIVS ETSKISESAF ESISGFAFHS IFQKSDPIKL EPIMLLEIRT
     PIEHTGEIIS KFNVMGGVIH SVSNIGEYDL IKSEAAFEKL FGYASILRSS TKGRGSFTME
     FSYFKEKVG