EFG_RICPR
ID EFG_RICPR Reviewed; 699 AA.
AC P41084;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Elongation factor G;
DE Short=EF-G;
GN Name=fusA; OrderedLocusNames=RP132;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=8892818; DOI=10.1128/jb.178.21.6192-6199.1996;
RA Syvaenen A.-C., Amiri H., Jamal A., Andersson S.G.E., Kurland C.G.;
RT "A chimeric disposition of the elongation factor genes in Rickettsia
RT prowazekii.";
RL J. Bacteriol. 178:6192-6199(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
RC STRAIN=Madrid E;
RA Wood D.O.;
RT "Organization of genes contiguous to sdhA in Rickettsia prowazekii.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
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; Z54171; CAA90884.1; -; Genomic_DNA.
DR EMBL; AJ235270; CAA14601.1; -; Genomic_DNA.
DR EMBL; U02603; AAA18331.1; -; Unassigned_DNA.
DR PIR; B71723; B71723.
DR RefSeq; NP_220524.1; NC_000963.1.
DR RefSeq; WP_004599757.1; NC_000963.1.
DR PDB; 6NOT; X-ray; 2.40 A; A/B=1-699.
DR PDBsum; 6NOT; -.
DR AlphaFoldDB; P41084; -.
DR SMR; P41084; -.
DR STRING; 272947.RP132; -.
DR EnsemblBacteria; CAA14601; CAA14601; CAA14601.
DR GeneID; 57569260; -.
DR KEGG; rpr:RP132; -.
DR PATRIC; fig|272947.5.peg.134; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_5; -.
DR OMA; AATTCHW; -.
DR Proteomes; UP000002480; 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; cd01434; EFG_mtEFG1_IV; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..699
FT /note="Elongation factor G"
FT /id="PRO_0000091201"
FT DOMAIN 8..283
FT /note="tr-type G"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 263
FT /note="F -> L (in Ref. 1; CAA90884)"
FT /evidence="ECO:0000305"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:6NOT"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:6NOT"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 205..219
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 225..231
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:6NOT"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:6NOT"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:6NOT"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 323..336
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:6NOT"
FT TURN 344..347
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 363..370
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 408..418
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 420..433
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 448..454
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 455..466
FT /evidence="ECO:0007829|PDB:6NOT"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 490..496
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 507..515
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 530..535
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 547..558
FT /evidence="ECO:0007829|PDB:6NOT"
FT TURN 562..564
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 570..579
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 591..601
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 608..621
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 622..624
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 625..634
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 638..645
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 648..656
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 657..659
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 663..670
FT /evidence="ECO:0007829|PDB:6NOT"
FT TURN 671..673
FT /evidence="ECO:0007829|PDB:6NOT"
FT STRAND 676..686
FT /evidence="ECO:0007829|PDB:6NOT"
FT HELIX 689..695
FT /evidence="ECO:0007829|PDB:6NOT"
SQ SEQUENCE 699 AA; 77750 MW; 8A34834D6770BA2B CRC64;
MSKINKLEQI RNIGICAHID AGKTTTTERI LYYTGKSHKI GEVHEGGATM DWMEQEQERG
ITITSAATTC RWQDKVINII DTPGHVDFTI EVERSLRVLD GAVAVFDGVA GVEPQSETVW
RQADKYNVPR MCFVNKMDRM GADFYRCVEM IKDRLGARSL IIQLPIGIEE NFKGIVNLIK
MKAVIWKDES LGAEYFEEDI PADMQDKAAE YRARLLDMVV ELDDTIMEQY LSGAEITEEQ
IKILIRKGTI EARFYPILCG SAFKNKGVQP LLDAIVDFLP SPIDIGIVKG IEVSTSEEKD
FPISIVEPFS ALAFKIMNDP FVGSLTFIRI YSGKITSGAT VINTVKNKRE KIGRMLLMHA
NNREDIKEAS AGDIVALAGL KDTSTGDTLS DIDKQVVLER MEFPEPVIEL AVEPKSTADQ
EKMGLALSRL AAEDPSFRVS TDHETGQTVI KGMGELHLEI IIDRMRREFK VEANIGAPQV
AYRETITTAC EIDYTHKKQS GGAGQFARVK IIFEPLKDVI DLKDEDKNKT FVFESKIVGG
AVPKEYIPGV EKGLNNIRET GVIAGYPMID FKATLVDGAF HDVDSSVLAF EIAAKGAFRE
GMQKGNPKLL EPIMKVEVIT PDEYMGDIIG DLNSRRGQIQ NMDPRGNAQV VTAHVPLAEM
FGYVNTLRSL SQGRAQFSMI FSHYDQVPSQ VADMIKAKK
