ID   EFG_STRGG               Reviewed;         709 AA.
AC   B1W417;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=SGR_2844;
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/jb.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(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; AP009493; BAG19673.1; -; Genomic_DNA.
DR   RefSeq; WP_012379465.1; NC_010572.1.
DR   AlphaFoldDB; B1W417; -.
DR   SMR; B1W417; -.
DR   STRING; 455632.SGR_2844; -.
DR   EnsemblBacteria; BAG19673; BAG19673; SGR_2844.
DR   GeneID; 6208955; -.
DR   KEGG; sgr:SGR_2844; -.
DR   PATRIC; fig|455632.4.peg.2906; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_11; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 88967at2; -.
DR   Proteomes; UP000001685; 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..709
FT                   /note="Elongation factor G"
FT                   /id="PRO_1000091764"
FT   DOMAIN          9..296
FT                   /note="tr-type G"
FT   BINDING         18..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         86..90
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         140..143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   709 AA;  77574 MW;  5B3A22FFAD4EFA79 CRC64;
     MATTSLDLAK VRNIGIMAHI DAGKTTTTER ILFYTGVSYK IGEVHDGAAT MDWMEQEQER
     GITITSAATT CHWPLNDVDH TINIIDTPGH VDFTVEVERS LRVLDGAVTV FDGVAGVEPQ
     SETVWRQADR YGVPRICFVN KLDRTGADFF RCVDMIVDRL GATPIVMQLP IGAEADFTGV
     VDLVSMKAFV YPEEAAKGEM YNVVDIPENL QESAAEWRGK LLEAVAENDD AMMELYLEGN
     EPTQEQLHDA IRRITLASKG SADSVTVTPV FCGTAFKNKG VQPLLDAVVR YLPSPLDVEA
     IEGHDVKDPE KVIARKPSDD EPFSGLAFKI ASDPHLGKLT FVRIYSGRLE AGTAVLNSVK
     GKKERIGKIY RMHANKREEI ASVGAGDIIA VMGLKQTTTG ETLCDDKNPV ILESMDFPAP
     VIQVAIEPKS KGDQEKLGVA IQRLSEEDPS FQVHSDEETG QTIIGGMGEL HLEVLVDRMK
     REFRVEANVG KPQVAYRETI RKAVERIDYT HKKQTGGTGQ FAKVQIALEP IEGGDASYEF
     VNKVTGGRIP REYIPSVDAG AQEAMQFGIL AGYEMVGVRV TLLDGGYHEV DSSELAFKIA
     GSQAFKEGAR KASPVLLEPM MAVEVTTPED YMGDVIGDLN SRRGQIQAME ERSGARVVKG
     LVPLSEMFGY VGDLRSKTSG RASYSMQFDS YAEVPRNVAE EIIAKAKGE