ID   EFG1_ANADE              Reviewed;         697 AA.
AC   Q2IJ93;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Elongation factor G 1 {ECO:0000255|HAMAP-Rule:MF_00054};
DE            Short=EF-G 1 {ECO:0000255|HAMAP-Rule:MF_00054};
GN   Name=fusA1 {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=Adeh_1948;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA   Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA   Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000251; ABC81719.1; -; Genomic_DNA.
DR   RefSeq; WP_011421001.1; NC_007760.1.
DR   AlphaFoldDB; Q2IJ93; -.
DR   SMR; Q2IJ93; -.
DR   STRING; 290397.Adeh_1948; -.
DR   PRIDE; Q2IJ93; -.
DR   EnsemblBacteria; ABC81719; ABC81719; Adeh_1948.
DR   KEGG; ade:Adeh_1948; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_7; -.
DR   OMA; AATTCHW; -.
DR   Proteomes; UP000001935; 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 1"
FT                   /id="PRO_0000263423"
FT   DOMAIN          8..283
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;  77345 MW;  F7ABC70884203F59 CRC64;
     MARTTPLERY RNFGIMAHID AGKTTTTERI LFYTGVTHKI GEVHEGTTVM DWMEQERERG
     ITITSAATTA FWRDHRLNII DTPGHVDFTI EVERSLRVLD GACAVFDAVQ GVQPQSETVW
     RQADKYEVPR ICFINKMDRV GADYFHAVDT IREKLGARPL PLHVPIGAED KFRGMVDLLK
     MKGITFDDET MGAKYQEVEI PADLAAQAKE YRAKLEETVA EIDDELMAKY LDGKPLSNDE
     LMRGIRRGTL EMKFFPVLCG TAFKNKGVQQ ILDAVVDFLP SPVDIPAMKG VDAKGNDVVR
     KTSDAEPFSA LAFKIMNDPF VGNLTFFRVY SGRLEAGSYV YNSTKDKKER IGRLLQMHAN
     KREEIKEVYA GDIAAAVGLR ASTTGDTLCA EDAPVILERM EFPEPVIHIA IEPKTKGDQD
     KMGVALQRLQ MEDPSFRVHT DEETGQTIIG GMGELHLEIL VDRMFREFKV EANVGKPQVA
     YRETITRTVE AEGRYIRQTG GRGQYGHCWL RLHPQEPGKG FEFENAIVGG VIPKEFISPI
     QKGIEEAMTS GVLAGYPMVD LKVELFDGSY HDVDSSEMAF KIAGSMGFKE GAAKASPVLL
     EPIMAVEVTT PDDYMGDVIG DLNSRRGKIH AMNPRAGVQV IEAHVPLAEM FGYATDLRSK
     TQGRATYSMQ FAHYAQVPAS IAETIVTKAK GVAAGAK