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EFG2_STRCO
ID   EFG2_STRCO              Reviewed;         686 AA.
AC   O87844;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Elongation factor G 2;
DE            Short=EF-G 2;
GN   Name=fusB; OrderedLocusNames=SCO6589; ORFNames=SC8A6.10;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939128; CAA19782.1; -; Genomic_DNA.
DR   PIR; T35777; T35777.
DR   RefSeq; NP_630668.1; NC_003888.3.
DR   RefSeq; WP_011031026.1; NZ_VNID01000002.1.
DR   AlphaFoldDB; O87844; -.
DR   SMR; O87844; -.
DR   STRING; 100226.SCO6589; -.
DR   GeneID; 1102028; -.
DR   KEGG; sco:SCO6589; -.
DR   PATRIC; fig|100226.15.peg.6696; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_11; -.
DR   InParanoid; O87844; -.
DR   OMA; HKRGEVH; -.
DR   PhylomeDB; O87844; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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   GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
DR   CDD; cd16262; EFG_III; 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..686
FT                   /note="Elongation factor G 2"
FT                   /id="PRO_0000091228"
FT   DOMAIN          7..280
FT                   /note="tr-type G"
FT   BINDING         16..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         80..84
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         134..137
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   686 AA;  72921 MW;  BCFC581BFC9FAFC2 CRC64;
     MRTNPLTTVR NLGILAHVDA GKTTVTERIL YLTGTTHKRG EVHDGTTVTD FDPQERDRGI
     TIFAAAVSCA WAGHRINLID TPGHVDFADE VERSLRVLDG AVAVFDAVAG VEPQSESVWR
     QADRHGVPRI AFVNKMDRAG ADLDAAVASI RERLHPVPLV VQLPIGTEDG FTGVVDLPRM
     RALVWADGAD AAEEGPVPGT LREEAARRRR VLEEAVAERH PGALEEFCDR ETLTAATLTG
     ALRDLTRTGD GVVVLCGSAY RNRGVEPLLD AVVAYLPSPL DVPPVRGTHD GAERERPADP
     AAPMAALAFK VNATPTGRLT YLRVYSGTIG KGDTVWDAGT RRTERIGRIL RVRADRHDPL
     ERAVAGDIVA VVGLKTARAG STLCAPGAPL LLEPPGVAEP VVHVAVEARR STETDRLAAA
     LARLTEEDPS LALRTDPETA QTVLSGMGEL HLEVAVERVR REYGLEVTVG RPGVAYRETV
     GEGVTGFVHR HVKQDGGAGQ FAHIVLDVEP WEQDADGDGA GGGFVFRSTV VGGRVPQEYV
     RAVEAGCRDA LAEGPLGGHP VTGLRVTLTD GRTHVKDSSD TAFRTAGRFG LRDALRASGM
     ILLEPVVEVT VTVPEDGVGG VLGDLAARRG RVTGSDPRGG AVVVTATVPL AELFGYATRL
     RSRTQGRGTF TARPTGYAQA PAAVVR
 
 
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