ID   EFG_MICLU               Reviewed;         701 AA.
AC   P09952;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
GN   Name=fusA; Synonyms=fus;
OS   Micrococcus luteus (Micrococcus lysodeikticus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX   NCBI_TaxID=1270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3654584; DOI=10.1128/jb.169.10.4770-4777.1987;
RA   Ohama T., Yamao F., Muto A., Osawa S.;
RT   "Organization and codon usage of the streptomycin operon in Micrococcus
RT   luteus, a bacterium with a high genomic G + C content.";
RL   J. Bacteriol. 169:4770-4777(1987).
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; M17788; AAA25319.1; -; Genomic_DNA.
DR   PIR; C26956; C26956.
DR   AlphaFoldDB; P09952; -.
DR   SMR; P09952; -.
DR   STRING; 1232675.GCA_000309825_02164; -.
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..701
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091153"
FT   DOMAIN          6..285
FT                   /note="tr-type G"
FT   BINDING         15..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         79..83
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         133..136
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   701 AA;  77425 MW;  25E49F4CF350E236 CRC64;
     MLTDLHKVRN IGIMAHIDAG KTTTTERHLF YTGVNHKLGE THDGGATTDW MEQEKERGIT
     ITSAAVTCFW NDHQINIIDN PGHVDFTVEV ERSLRVLDGA VAVFDGKEGV EPQSETVWRQ
     ADKYDVPRIC FVNKMDKLGA DFYFTVDTIV KRLGARPLVM QLPIGAENDF VGVVDLISMK
     AFVWPGDANG IVTMGASYEI EIRQLQEKAE EEYRNELVEA VAETSEELME KYLEGEELTV
     EEIQAGVRQL TVNAEAYPVF CGSAFKNRGV QPMLDAVVAY LPNPLDAGPV KGHAVNDEEV
     VLEREVSKEA PFSALAFKIA THPFFGTLTF IRVYSGRLES GAQVLNATKG KKERIGKLFQ
     MHANKENPVD EVVAGHIYAV IGLKDTTTGD TLCDPANPII LESMTFPEPV ISVAIEPKTK
     GDQEKLSTAI QKLVAEDPTF RVNLNEETGQ TEIGGMGELH LDVFVDRMKR EFKVEANVGK
     PQVAYRETIK RKVDKVDYTH KKQTGGSGQF AKVQLSFEPL DTPRGTVYEF ENAITGGRVP
     REYIPSVDAG IQDAMKFGVL AGYPMVRVKA TSLDGAYHDV DSSEMAFRIA GSQAFKEGVR
     KATPIILEPL MAVEVRTPEE FMGDVIGDLN SRRGQIQIQS MEDATGVKVV NALVPLSEMF
     GYIGDLRSKT QGRAVYSMTF HSYAEVPKAV ADEIVQKSQG E