EFG2_POLSJ
ID EFG2_POLSJ Reviewed; 704 AA.
AC Q123W3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=Bpro_4287;
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX NCBI_TaxID=296591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500;
RX PubMed=18723656; DOI=10.1128/aem.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE46179.1; -; Genomic_DNA.
DR RefSeq; WP_011485168.1; NC_007948.1.
DR AlphaFoldDB; Q123W3; -.
DR SMR; Q123W3; -.
DR STRING; 296591.Bpro_4287; -.
DR PRIDE; Q123W3; -.
DR EnsemblBacteria; ABE46179; ABE46179; Bpro_4287.
DR KEGG; pol:Bpro_4287; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_4; -.
DR OMA; NHKMGEV; -.
DR OrthoDB; 88967at2; -.
DR Proteomes; UP000001983; 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; Reference proteome.
FT CHAIN 1..704
FT /note="Elongation factor G 2"
FT /id="PRO_0000263482"
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 704 AA; 77871 MW; 92243ADF2C1E3E2F CRC64;
MTRKTPIERY RNIGISAHID AGKTTTTERI LFYTGVNYKL GEVHEGTATM DWMEQEQERG
ITITSAATTA FWKGMAGNYP EHRINIIDTP GHVDFTIEVE RSMRVLDGAV MVYDSVGGVQ
PQSETVWRQA NKYKVPRIAF VNKMDRVGAD FFRVQRQIGE RMKGVAVPVQ IPIGAEDHFQ
GVVDLVKMKA IVWDDISQGL HFEYRDIPDE LLATARTWRD KMIEAAAEAS EPLLEKYLAG
EALSEDEIRQ GIRQRTVANE IVPMLCGSAF KNKGVQALLD AIIDYLPSPV DVPAILGHTE
DDKTAERHPG DNEPFSALAF KVMTDPFVGQ LIFFRVYSGV VKTGDTVYIP GKTRKERLGR
LLQMHANVRQ EIKEVHAGDI AAAVGLKDVT TGDTLCDPDK VIMLERMVFP EPVISQAVEP
KTQADQEKMG VALHRLAQED PSFRVQTDEE SGQTIISGMG ELHLEILVDR MKREFGVDAT
VGKPQVAYRE TIKQAVKDVE GKFIKQSGGR GQYGHAVLNV EPQPPGKGYE FVDAIKGGVV
PREYIPAVDK GIQDALTAGV LASYPVVDVK ATLVFGSSHD VDSNENAFRM AGAIAFREAL
RRARPILLEP MMAVEVEMPE DFMGHVMGDL STRRGMIQGM EDIAGGGGKL VRAEVPLSEM
FGYSTTLRSL TQGRATYTME FKHYTEAPAD VSEAIIRGKG MGRQ