ID   EFG_MYCPU               Reviewed;         692 AA.
AC   Q98QD8;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
GN   Name=fusA; OrderedLocusNames=MYPU_4280;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC13601.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL445564; CAC13601.1; ALT_INIT; Genomic_DNA.
DR   PIR; D90565; D90565.
DR   RefSeq; WP_041364095.1; NC_002771.1.
DR   AlphaFoldDB; Q98QD8; -.
DR   SMR; Q98QD8; -.
DR   STRING; 272635.MYPU_4280; -.
DR   EnsemblBacteria; CAC13601; CAC13601; CAC13601.
DR   KEGG; mpu:MYPU_4280; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_14; -.
DR   OrthoDB; 88967at2; -.
DR   BioCyc; MPUL272635:G1GT6-432-MON; -.
DR   Proteomes; UP000000528; 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; Reference proteome.
FT   CHAIN           1..692
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091164"
FT   DOMAIN          8..282
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   692 AA;  77010 MW;  2B5CC18C34507EB2 CRC64;
     MSREYDLKDY RNIGIMAHID AGKTTTTERI LFHTGKIHKI GETHDGGSQM DFMAQEKERG
     ITITSAATTA FWRGKRINII DTPGHVDFTV EVERSLRVLD GAVAVLDAQS GVEPQTETVW
     RQATNYKVPR IVFVNKMDKA GANLEESIKS VKTRLNGNAV AIQLNMGSES DYRGHIDLVE
     MKAWEFDGKP EENGKEIEIP AEYLEAAQIE RSKLIEAVSS FDDEVMMLAL EEQEIPVDLL
     KSAIRKATLT SEFFPVVCGT AFKNKGVKAM IDAVVDYLPS PLDVPAIKGY FQEKEVLVTA
     SDENDFSALA FKIMNDPFVG SLTFFRVYSG ILSKGSYVYN TTKDKKERIG RILQMHANSR
     EEIDEVRTGD IAAAVGLKDT TTGDTIVGDK SKHIILEKMV FPEPVISQAL EPESKAATEK
     LSLGLQKLAA EDPTFRTFTD TETGQTIIAG MGELHLDIIV DRLRREFGVQ VKVGAPQVSY
     RETITAKADV EGKYIKQSGG KGQYGHVWIT FEPNPNNGFE FVDKIVGGKI PKEYIKTIQK
     GLEEKMASGI LAGYPMIDLK ATLFDGSYHE VDSSEMAYKI AASMALTKAK DVVKTVLLEP
     IMDVSVVFPK EYYGDVVGDL SRRRGQIIND ETRSDGASVI KSHVPLSEMF GYATDLRSMT
     KGRGTYQMHF DHYERTPRNI ADEIIKKRNI KN