ID EFG1_TREPA Reviewed; 695 AA.
AC O83748;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=Elongation factor G 1;
DE Short=EF-G 1;
GN Name=fusA; Synonyms=fusA-2; OrderedLocusNames=TP_0767;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC 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; AAC65735.1; -; Genomic_DNA.
DR PIR; D71283; D71283.
DR RefSeq; WP_010882212.1; NC_021490.2.
DR AlphaFoldDB; O83748; -.
DR SMR; O83748; -.
DR STRING; 243276.TP_0767; -.
DR EnsemblBacteria; AAC65735; AAC65735; TP_0767.
DR GeneID; 57879289; -.
DR KEGG; tpa:TP_0767; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_0_12; -.
DR OrthoDB; 9804431at2; -.
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; 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; Reference proteome.
FT CHAIN 1..695
FT /note="Elongation factor G 1"
FT /id="PRO_0000091254"
FT DOMAIN 6..282
FT /note="tr-type G"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 82..86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 695 AA; 76831 MW; 46529989BFE97E4E CRC64;
MSRGISTFRN IGISAHIDSG KTTLSERILF YCDRIHAIHE VRGKDGVGAT MDNMELERER
GITIQSASTQ VQWKGHTINV IDTPGHVDFT IEVERSLRVL DGAVLVLCSV AGVQSQSITV
DRQLRRYHVP RISFINKCDR TGANPFKVCA QLREKLSLNA HLMQLPIGLE DRLEGVIDLI
SLKALYFEGE SGAHVREAPI PEQYQADVKK YRDELIDAAS LFSDELAEAY LEGTETDQLI
RAAVRAGTIA EKFVPVFCGS AYKNKGIQPL LDAITYYLPD PTEVTNTALD LDRAEEPVTL
STDADAPVVA LGFKLEDGKY GQLTYVRVYQ GTIKKGAELF NVRARKKFKV GRLVRMNSNQ
MEDISEGTPG DIVALFGVDC ASGDTFCSGD LNYAMTSMFV PEPVISLSIT PKDKRSADQV
SKALNRFTKE DPTFRSFVDP ESNQTIIQGM GELHLDVYIE RMRREYKCEV ETGMPQVAYR
EAISARADFN YTHKKQTGGS GQFGRVAGFI EPIAGQDYEF VDQIKGGVIP NEFIPSCDKG
FRTAVKKGTL IGFPIVGVRV TINDGQSHPV DSSDMAFQAA AIGAFREAYN GAKPVVLEPI
MRVSVEGPQE FQGSVFGLIN QRRGVVVSSA DDEQFSRVDA EVPLSEMFGF STVLRSSTQG
KAEYSMEFAK YGKAPQGVTD SLIKEYQEKR KAEQR
//
