ID   EFG_CHLTR               Reviewed;         694 AA.
AC   O84444;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
GN   Name=fusA; OrderedLocusNames=CT_437;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC68036.1; -; Genomic_DNA.
DR   PIR; F71514; F71514.
DR   RefSeq; NP_219949.1; NC_000117.1.
DR   RefSeq; WP_009871792.1; NC_000117.1.
DR   AlphaFoldDB; O84444; -.
DR   SMR; O84444; -.
DR   STRING; 813.O172_02385; -.
DR   EnsemblBacteria; AAC68036; AAC68036; CT_437.
DR   GeneID; 884230; -.
DR   KEGG; ctr:CT_437; -.
DR   PATRIC; fig|272561.5.peg.472; -.
DR   HOGENOM; CLU_002794_4_1_0; -.
DR   InParanoid; O84444; -.
DR   OMA; AATTCHW; -.
DR   Proteomes; UP000000431; 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..694
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091105"
FT   DOMAIN          9..288
FT                   /note="tr-type G"
FT   BINDING         18..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         82..86
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   694 AA;  76538 MW;  58BDA7CA96D0A8E8 CRC64;
     MSDQEFGLDA IRNIGIMAHI DAGKTTTTER ILFYAGRTHK IGEVHEGGAT MDWMEQEQER
     GITITSAATT VFWLGAKINI IDTPGHVDFT IEVERSLRVL DGAVAVFDAV SGVEPQSETV
     WRQANKYGVP RIAFVNKMDR MGANYFGAIE SMREKLGANA IPVHCPIGSE SQFVGMVDLI
     SQKTLYFLEE TLGAKWEERE IPEDLQEQCA TLRMQLLEEL ATVDESNEAF MEKVLENPDS
     ITEEEIHTVM RKGVIEGKIN PVLCGSAFKN KGVQQLLDVI VKWLPSPLDR GNVRGINLKT
     GEEVSLKPSK DGPLAALAFK IMTDPYVGRI TFIRIYSGTL KKGSAILNST KDKKERISRL
     LEMHANERTD RDEFTVGDIG ACVGLKFSVT GDTLCDENQE IVLERIEAPE PVIDMAIEPK
     SKGDREKLAQ ALSALSEEDP TFRVSTNEET GQTIISGMGE LHLDILRDRM IREFRVEANV
     GKPQVSYKET ITKTSNSETK YVKQSGGRGQ YAHVCLEIEP NEPGKGNEVV SKIVGGVIPK
     EYIPAVIKGV EEGLNSGVLA GYGLVDVKVS IVFGSYHEVD SSEMAFKICG SMAVKEACRK
     ALPVILEPIM KVTVITPEDH LGDVIGDLNR RRGKILGQES SRNMAQVSAE VPLSEMFGYM
     TSLRSLTSGR ATSTMEPAFF AKVPQKIQEE IVKK