EFG_RICFE
ID EFG_RICFE Reviewed; 699 AA.
AC Q8KTA8; Q4UKC7;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Elongation factor G {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-G {ECO:0000255|HAMAP-Rule:MF_00054};
GN Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=RF_1153;
OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=315456;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12140235; DOI=10.1093/oxfordjournals.molbev.a004184;
RA Amiri H., Alsmark C.M., Andersson S.G.E.;
RT "Proliferation and deterioration of Rickettsia palindromic elements.";
RL Mol. Biol. Evol. 19:1234-1243(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1525 / URRWXCal2;
RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA Parinello H., Claverie J.-M., Raoult D.;
RT "The genome sequence of Rickettsia felis identifies the first putative
RT conjugative plasmid in an obligate intracellular parasite.";
RL PLoS Biol. 3:1-12(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY62004.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF502178; AAM90929.1; -; Genomic_DNA.
DR EMBL; CP000053; AAY62004.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011271462.1; NC_007109.1.
DR AlphaFoldDB; Q8KTA8; -.
DR SMR; Q8KTA8; -.
DR STRING; 315456.RF_1153; -.
DR PRIDE; Q8KTA8; -.
DR EnsemblBacteria; AAY62004; AAY62004; RF_1153.
DR KEGG; rfe:RF_1153; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_5; -.
DR OrthoDB; 88967at2; -.
DR Proteomes; UP000008548; 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 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..699
FT /note="Elongation factor G"
FT /id="PRO_0000091197"
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:0000255|HAMAP-Rule:MF_00054"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT CONFLICT 392
FT /note="M -> I (in Ref. 1; AAM90929)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 699 AA; 77671 MW; E8FEB9C7F37D432D CRC64;
MSKINKLEHI RNIGICAHID AGKTTTTERI LYYTGKSHKI GEVHEGGATM DWMEQEQERG
ITITSAATTC RWQDKIINII DTPGHVDFTI EVERSLRVLD GAVAVFDGVA GVEPQSETVW
RQADKYNVPR MCFVNKMDRM GADFYRCVEM IKDRLGAKPL VIQLPVGIEE SFKGIIDLVK
MKAVIWKDES LGAEYFEEDI PADMKDKAEE YRAKLLDMVV ELDDAIMEKY LSGEEVTEEE
IKRLIRRGTI SAAFYPVLCG SAFKNKGVQP LLDAVVDFLP SPIDIGIVKG MEVSTGEEKD
FPISITEPFS ALAFKIMNDP FVGSLTFIRI YSGKITSGST VINTVKNKRE KIGRMLLMHA
NNREDVKEAS AGDIVALAGL KDTTTGDTLS DMDKQVILER MEFPEPVIEL AVEPKSTADQ
EKMGLALSRL AAEDPSFRVS TDHETGQTVI KGMGELHLEI IIDRMRREFK VEANIGAPQV
AYRETITKAC EIDYTHKKQS GGAGQFARVK IIFEPLKEVK DLKDEDKNKT FVFESKIVGG
AVPKEYIPGV EKGLNNIRET GVIAGYPMID FKATLVDGAF HDVDSSVLAF EIAAKAAFRE
GMPKGNPKLL EPIMKVEVIT PDEYMGDIIG DLNSRRGQIQ SMDPRGNAQV VTANVPLAEM
FGYVNTLRSL SQGRAQFSMI FSHYDQVPSQ VADIIKAKK
