ID   EFG_ARTPT               Reviewed;         697 AA.
AC   P13550;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
GN   Name=fusA; Synonyms=fus;
OS   Arthrospira platensis (Spirulina platensis).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Arthrospira.
OX   NCBI_TaxID=118562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2505055; DOI=10.1007/bf00330947;
RA   Buttarelli F.R., Calogero R.A., Tiboni O., Gualerzi C.O., Pon C.L.;
RT   "Characterization of the str operon genes from Spirulina platensis and
RT   their evolutionary relationship to those of other prokaryotes.";
RL   Mol. Gen. Genet. 217:97-104(1989).
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; X15646; CAA33672.1; -; Genomic_DNA.
DR   PIR; S04390; S04390.
DR   AlphaFoldDB; P13550; -.
DR   SMR; P13550; -.
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..697
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091213"
FT   DOMAIN          8..287
FT                   /note="tr-type G"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         135..138
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   697 AA;  76775 MW;  2BC6DA183B7DEB2C CRC64;
     MARTIPLERV RNIGIAAHID AGKTTTTERI LFYSGVVHKM GEVHEGTAVT DWMAQERERG
     ITITAAAIST SWLDHRINII DTPGHVDFTI EVERSMRVLD GVIAVFCSVG GVQPQSETVW
     RQAERYQVPR IAFINKMDRT GADFFKVYGQ IRDRLRANAV PIQVPVGRES DFHGLVDLVA
     MKTYLYTNDL GTDIQVSDEI PEEVQDLVAE YREKLLEAVA ETDEALMEKY LEQLEGGEAL
     TEEEIRHSLR QGTIKGLIVP VICGSSFKNR GVQRLLDAVV DYLPAPTEVP PIKGVLPDGE
     EGVRYADDDA PLSALAFKVM ADPYGRLTFV RVYSGVLQKG SYIYNATKNK KERISRLIVL
     KSDERIEVEE LRAGDLGAAL GLKDTLTGDT ICDEANSIIL ESLYIPEPVI SVAVEPKTKQ
     DMEKLSKALQ SLSEEDPTFR VSIDSETNQT VIAGMGELHL EILVDRMLRE FKVEANIGAP
     QVAYRETIRK SIRTEGKFIR QSGGKGQYGH VVIELEPGEP GSGFEFVSKI VGGSVPKEYI
     NPAEQGMKEA CESGVIAGYP LIDVKATLVD GSYHEVDSSE MAFKIAGSMA IKNGVTKASP
     VLLEPMMKVE VEVPEDFIGN VIGDLNSRRG QIEGQETDQS QSIAKVVAKV PLATMFGYAT
     DIRSKTQGRG VFSMEFSHYE EVPRSVAETI IAKSKGN