EFG2_TREPA
ID EFG2_TREPA Reviewed; 683 AA.
AC O83464;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Elongation factor G 2;
DE Short=EF-G 2;
GN Name=fusB; Synonyms=fusA-1; OrderedLocusNames=TP_0450;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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; AE000520; AAC65438.1; -; Genomic_DNA.
DR PIR; C71322; C71322.
DR RefSeq; WP_010881898.1; NC_021490.2.
DR AlphaFoldDB; O83464; -.
DR SMR; O83464; -.
DR STRING; 243276.TPANIC_0450a; -.
DR PRIDE; O83464; -.
DR EnsemblBacteria; AAC65438; AAC65438; TP_0450.
DR GeneID; 57878974; -.
DR KEGG; tpa:TP_0450; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_12; -.
DR OMA; AVCQIPW; -.
DR OrthoDB; 88967at2; -.
DR Proteomes; UP000000811; 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..683
FT /note="Elongation factor G 2"
FT /id="PRO_0000091255"
FT DOMAIN 4..279
FT /note="tr-type G"
FT BINDING 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 77..81
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 683 AA; 75802 MW; E0543E02FAA72AF1 CRC64;
MRQQQMRNIG IMAHVDAGKT TTTERMLFYT GKIHRMGEID DGATTMDWMV QEQERGITIQ
SAATTVRWRE VDITIIDTPG HVDFTAEVER ALRVLDGVVV VLCAVGRVQP QTETVWYQAD
RYDIPRVCFV NKMDRIGADF FSVLDQVHNK FGIDAVALQI PIGSGTSFEG VIDLITMKEI
FWDAASSGEQ MEYRPIQSAR IAQAREAREK MLDVISIYSD EVTECVLAGE HVPVQLLHAE
IRKAVRERRY VPFLCGSSRH NLGVQPLLDA VVEYLPAPQE RKAVEGFHVQ KKEPVFIAPT
AEGPLLALVF KIQYEREAGL LCYVRMYSGK LRTGDSIVNI GKKKRERVYR ILRMHSNKSE
TVECIQAGDI AVIVGLKSAQ TGDSVGDGSC PVVLESMHFP EPVISVSLEP MDASSRDKLQ
ETLGILSRED PTFSVREDAE TGQLLISGMG ELHLDVLTTR MREDFNVQVR VGKPHVTYRE
SIRKTVERTL RVQRVIGGKE YMAGLTLRVE ARKRGAGNEF FCQVKELRGT VCTAHTAPAE
IIGAVEHAIR GAWDGGIQSG YPCVDVGVHL LSVEYQELTS SPFIFEAAAV QAFGEACVAA
EPYVLEPIMS VELSCAQENV GDVMNVIIQR GGIILGMDSK HGRELVHAQA PMKKMFGFST
DVRSASRGGA SFTMRFSHFE SCA
