ID   EFG_META1               Reviewed;         697 AA.
AC   B3PME9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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};
GN   OrderedLocusNames=MARTH_orf312;
OS   Metamycoplasma arthritidis (strain 158L3-1) (Mycoplasma arthritidis).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC   Metamycoplasma.
OX   NCBI_TaxID=243272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=158L3-1;
RX   PubMed=18573899; DOI=10.1128/iai.00516-08;
RA   Dybvig K., Zuhua C., Lao P., Jordan D.S., French C.T., Tu A.H.,
RA   Loraine A.E.;
RT   "Genome of Mycoplasma arthritidis.";
RL   Infect. Immun. 76:4000-4008(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001047; ACF07201.1; -; Genomic_DNA.
DR   RefSeq; WP_012498158.1; NC_011025.1.
DR   AlphaFoldDB; B3PME9; -.
DR   SMR; B3PME9; -.
DR   STRING; 243272.MARTH_orf312; -.
DR   PRIDE; B3PME9; -.
DR   EnsemblBacteria; ACF07201; ACF07201; MARTH_orf312.
DR   KEGG; mat:MARTH_orf312; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_14; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 88967at2; -.
DR   Proteomes; UP000008812; 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..697
FT                   /note="Elongation factor G"
FT                   /id="PRO_1000091735"
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   697 AA;  77771 MW;  4BF4BA609A4FFBFF CRC64;
     MAREYKLEDY RNIGIMAHID AGKTTTTERV LFHTGKIHKI GETHEGESQM DWMVQEQERG
     ITITSAATTA YWGGKRLNII DTPGHVDFTV EVERSLRVLD GAVAVLDAQS GVEPQTETVW
     RQATNYNVPR IVYVNKMDKA GANFKASTES LRKLLGANAH PIQLNIGEEA QFTGIIDLVE
     MKAYEFDGKP EENMKEIPIP AHLLDEATLM RSSLIESVAD FDEEIMEALL EEKEVSIEKI
     KAAIRKATLS ATYFPVVCGT SFKNKGVKLM LNAIVDYLPS PLDIPPMKAY KGEGEISIPA
     SDDEFFSSLA FKVMNDPYVG NLTFFRVYSG ILNKGTYLYN STKGEKERIG RILLMHANSR
     TDIDEVRTGD IGAAVGLKFT TTGDTLIDEK HKDIVLENMN FPEPVISQAL EPASKDASEK
     LSLALQRLAA EDPTFKYYTD EETGQTIIAG MGELHLDIIV DRLKREFKVA ANVGAPQVSY
     RETITKSAEV EGIHKKQSGG KGQYGHVWIK YEPNPDKGFE FVDKIVGGKI PKEYIKSIEK
     GLKEKMEIGI LAGYPLIDVK ATLFDGSYHE VDSSELAYKI AASKSLTKGR EMLGTVLLEP
     IMDVAVVIPE DFFGDVMGDI SRRRGQVRDN ETRNDGAHVI KAYIPLSEMF GYATELRSMT
     TGRGTYQMWF DHYEKLPRNL ADEIIKKRGG KVKIDED