EFG2_CUPMC
ID EFG2_CUPMC Reviewed; 702 AA.
AC Q1LAN7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Elongation factor G 2 {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-G 2 {ECO:0000255|HAMAP-Rule:MF_00054};
GN Name=fusA2 {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=Rmet_5930;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OG Plasmid megaplasmid CH34.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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}.
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DR EMBL; CP000353; ABF12789.1; -; Genomic_DNA.
DR RefSeq; WP_008645473.1; NC_007974.2.
DR AlphaFoldDB; Q1LAN7; -.
DR SMR; Q1LAN7; -.
DR STRING; 266264.Rmet_5930; -.
DR PRIDE; Q1LAN7; -.
DR EnsemblBacteria; ABF12789; ABF12789; Rmet_5930.
DR GeneID; 60823727; -.
DR KEGG; rme:Rmet_5930; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_4; -.
DR OMA; FRVVQMM; -.
DR OrthoDB; 88967at2; -.
DR Proteomes; UP000002429; Plasmid megaplasmid CH34.
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; Plasmid;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..702
FT /note="Elongation factor G 2"
FT /id="PRO_0000263488"
FT DOMAIN 8..290
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 88..92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 702 AA; 77270 MW; E8D767FF8C6FFDB8 CRC64;
MPRKTPIERY RNIGISAHID AGKTTTTERI LFYTGVNHKL GEVHDGAATM DWMEQEQERG
ITITSAATTA FWKGMANNYP EHRINIIDTP GHVDFTIEVE RSMRVLDGAC MVYDAVGGVQ
PQSETVWRQA NKYSVPRIAF VNKMDRVGAD FFRVRTQIAD RLKGNAVPIQ IPVGAEDHFK
GVVDLVKMRA IVWDDDSQGV RFEYTDIPPE LVATAKEWHD KMVEAAAEAS EELLERYLSG
EPLSEEEIKT GLRKRTVAGE IVPMLCGSAF KNKGVQAMLD AVIDYLPSPV DVPAILGHTE
DDKEAERHPS DDEPFSALAF KIMTDPFVGQ LIFFRVYSGV VNSGDTVYNP VKGKRERLGR
ILQMHANVRN EIKEVRAGDI AAAVGLKEAT TGDTLCDPDK VIILERMSFP EPVISQAVEP
KTKADQEKMG IALNRLAQED PSFRVATDEE SGQTIISGMG ELHLEILVDR MKREFGVEAS
VGKPQVAYRE TIKGKARDVE GKFIKQSGGR GQYGHVVLDV EPMPQGGGYE FVDAIKGGVV
PREFIPAVDK GIRETLETGV LAGYPVVDVK ATLVFGSYHD VDSNENAFRM AGSMAFKEGM
RRAKPVLLEP MMAVEVETPE EFTGNVMGDL SSRRGMVHGM EDIAGGGGKI VRAEVPLATM
FGYSTSLRSL TQGRATFTME FKHYAEAPAN VAEAVINARK VG
