ID   EFG_MYCS5               Reviewed;         696 AA.
AC   Q4A703;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Elongation factor G {ECO:0000255|HAMAP-Rule:MF_00054};
DE            Short=EF-G {ECO:0000255|HAMAP-Rule:MF_00054};
GN   Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=MS53_0047;
OS   Mycoplasmopsis synoviae (strain 53) (Mycoplasma synoviae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=262723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=53;
RX   PubMed=16077101; DOI=10.1128/jb.187.16.5568-5577.2005;
RA   Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L.,
RA   Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R.,
RA   Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M.,
RA   Brocchi M., Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S.,
RA   Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G.,
RA   Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA   Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S.,
RA   Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B.,
RA   Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA   Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F.,
RA   Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B.,
RA   Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C.,
RA   Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L.,
RA   Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R.,
RA   Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA   Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C.,
RA   Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P.,
RA   Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A.;
RT   "Swine and poultry pathogens: the complete genome sequences of two strains
RT   of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL   J. Bacteriol. 187:5568-5577(2005).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00054}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00054}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00054}.
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DR   EMBL; AE017245; AAZ43468.1; -; Genomic_DNA.
DR   RefSeq; WP_011283211.1; NC_007294.1.
DR   AlphaFoldDB; Q4A703; -.
DR   SMR; Q4A703; -.
DR   STRING; 262723.MS53_0047; -.
DR   EnsemblBacteria; AAZ43468; AAZ43468; MS53_0047.
DR   KEGG; msy:MS53_0047; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_14; -.
DR   OMA; AATTCHW; -.
DR   Proteomes; UP000000549; 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..696
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000225219"
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:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         135..138
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   696 AA;  77260 MW;  A8CDC86FFFFF1A88 CRC64;
     MARDYDLKDY RNIGIMAHID AGKTTTTERI LYHTGKIHKI GETHDGVSQM DWMEQEKERG
     ITITSAATTA YWKNKRINII DTPGHVDFTV EVERSLRVLD GAVAVLDAQS GVEPQTETVW
     RQATNYKVPR IVYVNKMDKA GADFEAAVAS VKSRLGGNAV AIQWPIGSES NFNGIIDLVT
     MTATTYNGES AEEEFPMEIP TDLLDVAKAK RQELLEAAAN FDEEVMMMVL EGADVDIDTF
     KNTIRKATLT SEFFPVVCGT SFKNKGVKKM IDAVVDYLPS PLDIPPIKAY LNDQETDVVA
     TDDGEFAALA FKVMTDPFVG SLTFFRVYRG VLEKGSYVYN STKEQKERIG RILQMHANNR
     VEIDECRAGD IAAAVGLKFT TTGDTLVGEK SPKVVLEKMV FPEPVISQAL EPESKAANEK
     LSLGLQKLSA EDPTFRTYTD EETGQTIISG MGELHLDIIV DRLKREFGVK VKVGAPQVSY
     RETITKSAEV EGKHIKQSGG KGQYGHVWLK FEPNHDQGFE FIDKIVGGKI PKEYIKPIQK
     GLEEKMAVGI LAGYPMIDVK ATLFDGSYHD VDSSELAYKI AASKALTKAK DLIGTVLLEP
     IMDVSVVVPS DHMGDVIGDL SRRRGLISDQ EQRNDGAVIV RAKVPLSEMF GYSTELRSMT
     SGRGTYQMQF DHYEKCPKNI SDEIIKKRNI QNKDEE