ID   EFG_MYCPN               Reviewed;         688 AA.
AC   P75544;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
GN   Name=fusA; Synonyms=fus; OrderedLocusNames=MPN_227; ORFNames=MP604;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96252.1; -; Genomic_DNA.
DR   PIR; S73930; S73930.
DR   RefSeq; NP_109915.1; NC_000912.1.
DR   RefSeq; WP_010874584.1; NC_000912.1.
DR   AlphaFoldDB; P75544; -.
DR   SMR; P75544; -.
DR   STRING; 272634.MPN_227; -.
DR   EnsemblBacteria; AAB96252; AAB96252; MPN_227.
DR   GeneID; 66609127; -.
DR   KEGG; mpn:MPN_227; -.
DR   PATRIC; fig|272634.6.peg.246; -.
DR   HOGENOM; CLU_002794_4_1_14; -.
DR   OMA; AATTCHW; -.
DR   BioCyc; MPNE272634:G1GJ3-364-MON; -.
DR   Proteomes; UP000000808; 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..688
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091163"
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   688 AA;  76500 MW;  762E430061A7DFA4 CRC64;
     MARTVDLINF RNFGIMAHID AGKTTTSERI LFHSGRIHKI GETHDGESVM DWMEQEKERG
     ITITSAATSV SWKNCSLNLI DTPGHVDFTV EVERSLRVLD GAIAVLDAQM GVEPQTETVW
     RQASRYEVPR IIFVNKMDKT GANFERSVQS IQQRLGVKAV PIQLPIGAEN DFNGIIDLIE
     EKVYFFDGGK EEKAEEKPIP DQFKDQVKQM RAHLVEEVAN FDDQLMADYL EGKEISIADI
     KRCIRKGVIG CQFFPVLCGS AFKNKGIKLL LDAVVDFLPS PVDVPQAKAY GEDGNEVLIS
     ASDDAPFVGL AFKVATDPFV GRLTFVRVYS GVLKSGSYVK NVRKNKKERV SRLVKMHAQN
     RNEIEEIRAG DICAIIGLKD TTTGETLVDD KIDVQLEAMQ FAQPVISLAV EPKTKADQEK
     MSIALSKLAE EDPTFKTFTD PETGQTIIAG MGELHLDILV DRMRREFKVE VNVGAPQVSF
     RETFNKESEV EGKYIKQSGG RGQYGHVKIR FEPNKDKGFE FVDKIVGGRI PREYIKPVQA
     GLENAMASGP LAGYPMIDIK ATLFDGSFHE VDSSEMAFKI AASLALKEAG KVCSPVLLEP
     IMAIEVTVPE QYFGDTMGDI SSRRGLIEGT EQRDNVQVIK AKVPLKEMFG YATDLRSFSQ
     GRGNYVMQFS HYAETPKSVV NEIIATKK