EFG2_BORBU
ID EFG2_BORBU Reviewed; 669 AA.
AC O51634;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Elongation factor G 2;
DE Short=EF-G 2;
GN Name=fusB; Synonyms=fus2; OrderedLocusNames=BB_0691;
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 [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}.
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DR EMBL; AE000783; AAC67051.1; -; Genomic_DNA.
DR PIR; B70186; B70186.
DR RefSeq; NP_212825.1; NC_001318.1.
DR RefSeq; WP_010889801.1; NC_001318.1.
DR AlphaFoldDB; O51634; -.
DR SMR; O51634; -.
DR STRING; 224326.BB_0691; -.
DR PRIDE; O51634; -.
DR EnsemblBacteria; AAC67051; AAC67051; BB_0691.
DR KEGG; bbu:BB_0691; -.
DR PATRIC; fig|224326.49.peg.1082; -.
DR HOGENOM; CLU_002794_4_1_12; -.
DR OMA; AVCQIPW; -.
DR Proteomes; UP000001807; 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; Reference proteome.
FT CHAIN 1..669
FT /note="Elongation factor G 2"
FT /id="PRO_0000091081"
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: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; 75057 MW; 20BEA5691C8BDAC7 CRC64;
MSIRNIGIMA HIDAGKTTTT ERIIYYTGKS HKMGDVDSGN TITDWMPQEQ ERGITISSAA
ITCHWKDCQI NIIDTPGHVD FTAEVERSLR VLDGGIVIFS AVDGIQAQTE TVWKQAEKYE
IPRLAYVNKM DRIGADFFKV VGDIENKFKT IPLVLQIPIG NESNFEGVVD IILNKELHFS
MENGIPKLTY SQIREEFIEK VILFKKKLID ILSQFSEEIT QLFLEDKEIG LDIIKREIRR
GTISRFIIPV LMGTSLKNIG IEPLIDSIVD YLPSPFEKSF SAFSLDTNKK ILVDPNENKK
LSALVFKVQY SSVIASHLYF VRVYSGEINP NKKIINASNG KREKFTKIFR VFSNKNEQID
FVKTGDIGAV LGLKFSVTGD TLVEENNNVL LEAVMFPEPV VLMSVEPERS SDEVRLKEIF
EIISKEDPTF SYSESKETGQ LIISGMGELH LEIILTRIKD EFNLNVYTGK PQVSYRESAG
KIVKEVFEFN NIFAGKNIDF KIGMIIKPLS RGAGNKIDFE CGIEPVIKSA ILRGITSAFV
SGIFGYPIID INVSIFSIVC GANKISESAF ESISGFAFHS IFQKSDPIRL EPIMLLEIRT
PIEHTGEIIS TLNVMGGVIH SVSNIGEYDL IKSEAAFEKL FGYASILRSS TKGRGSFTME
FSYFKEKLS
