ID   EFG1_STRCO              Reviewed;         708 AA.
AC   P40173; Q9L0K3;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Elongation factor G 1;
DE            Short=EF-G 1;
GN   Name=fusA; Synonyms=fus; OrderedLocusNames=SCO4661; ORFNames=SCD840A.07;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 616-708.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=7918656; DOI=10.1016/0167-4781(94)90085-x;
RA   van Wezel G.P., Woudt L.P., Vervenne R., Verdurmen M.L., Vijgenboom E.,
RA   Bosch L.;
RT   "Cloning and sequencing of the tuf genes of Streptomyces coelicolor
RT   A3(2).";
RL   Biochim. Biophys. Acta 1219:543-547(1994).
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; AL939121; CAB81852.1; -; Genomic_DNA.
DR   EMBL; X77039; CAA54328.1; -; Genomic_DNA.
DR   PIR; S50137; S50137.
DR   RefSeq; NP_628821.1; NC_003888.3.
DR   RefSeq; WP_003974302.1; NZ_VNID01000028.1.
DR   AlphaFoldDB; P40173; -.
DR   SMR; P40173; -.
DR   STRING; 100226.SCO4661; -.
DR   GeneID; 1100102; -.
DR   KEGG; sco:SCO4661; -.
DR   PATRIC; fig|100226.15.peg.4732; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_11; -.
DR   InParanoid; P40173; -.
DR   OMA; AATTCHW; -.
DR   PhylomeDB; P40173; -.
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; 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..708
FT                   /note="Elongation factor G 1"
FT                   /id="PRO_0000091227"
FT   DOMAIN          9..295
FT                   /note="tr-type G"
FT   BINDING         18..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         86..90
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         140..143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   708 AA;  77657 MW;  36602998061D3B1B CRC64;
     MATTSLDLAK VRNIGIMAHI DAGKTTTTER ILFYTGVSYK IGEVHDGAAT MDWMEQEQER
     GITITSAATT CHWPLEDNDY TINIIDTPGH VDFTVEVERS LRVLDGAVTV FDGVAGVEPQ
     SETVWRQADR YGVPRICFVN KLDRTGAEFH RCVDMISDRL GAQPLVMQLP IGAEADFQGV
     VDLVRMKALV WSADAAKGEM YDVVDIPATH TEAAEEWRGK LVEAVAENDE EVMELFLEGQ
     EPTEEQLYAA IRRVTIASGK SSDTTVTPVF CGTAFKNKGV QPLLDAVVRY LPTPLDVEAI
     EGHDVKDPEV VVKRKPSEDE PLAALAFKIM SDPHLGKLTF VRVYSGRLVS GTAVLNSVKG
     RKERIGKIYR MHANKREEIE SVGAGDIVAV MGLKQTTTGE TLSDDKSPVI LESMDFPAPV
     IQVAIEPKSK GDQEKLGVAI QRLAEEDPSF QVHTNEETGQ TIIGGMGELH LEVLVDRMRR
     EFKVEANVGK PQVAYRETIR KTVERVDYTH KKQTGGTGQF AKVQIAIEPI EGGDASYEFV
     NKVTGGRIPK EYIPSVDAGA QEAMQFGILA GYEMTGVRVT LIDGGYHEVD SSELAFKIAG
     SQAFKEAARK ASPVLLEPMM AVEVTTPEDY MGDVIGDINS RRGQIQAMEE RMGARVVKGL
     VPLSEMFGYV GDLRSKTSGR ASYSMQFDSY AEVPRNVAEE IIAKAKGE