ID   EFG_BIFA0               Reviewed;         709 AA.
AC   B8DTV6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=BLA_1147;
OS   Bifidobacterium animalis subsp. lactis (strain AD011).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=442563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD011;
RX   PubMed=19011029; DOI=10.1128/jb.01515-08;
RA   Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA   Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT   "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT   lactis AD011.";
RL   J. Bacteriol. 191:678-679(2009).
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; CP001213; ACL29435.1; -; Genomic_DNA.
DR   RefSeq; WP_004269068.1; NC_011835.1.
DR   AlphaFoldDB; B8DTV6; -.
DR   SMR; B8DTV6; -.
DR   STRING; 442563.BLA_1147; -.
DR   EnsemblBacteria; ACL29435; ACL29435; BLA_1147.
DR   GeneID; 66532972; -.
DR   KEGG; bla:BLA_1147; -.
DR   HOGENOM; CLU_002794_4_1_11; -.
DR   OMA; AATTCHW; -.
DR   Proteomes; UP000002456; 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..709
FT                   /note="Elongation factor G"
FT                   /id="PRO_1000201440"
FT   DOMAIN          10..295
FT                   /note="tr-type G"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         91..95
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         145..148
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   709 AA;  78551 MW;  04C26C7F7E0EA423 CRC64;
     MALDVLTNLN QVRNIGIMAH IDAGKTTTTE RILFYTGKNY KIGETHEGAS TMDFMAQEKE
     RGITIQSAAT TCFWNRQTHD PDEKFQINII DTPGHVDFTA EVERSLRVLD GAVAVFDGKE
     GVEPQSETVW RQADKYGVPR ICFINKMDKL GADFYYSVST IKEKLGATPL VVQLPIGAEN
     DFSGVVDLIR MKAYVWNDIK DDQGAHYDTV EIPDDLKERA EQYRSELLDQ VAETDEELLE
     KYLENGDLSE QEIRGAIRQL TIAREAYPVL CGSAFKDKGV QPMLDAVVDY LPSPEDVPSI
     VGFDPSDESV EIDRKPTMDD PFSALVFKIS THPFYGKLVF VRVYSGSVKP GDNVLDSTKG
     KKERVGKIFQ MHADKENPVD AAEAGNIYTF VGLKNVTTGD TLCDEKHPIS LESMTFPDPV
     IEVAVEPKTK ADQEKMSLAL AKLSDEDPTF QVKTDEESGQ TLISGMGELQ LDIIVDRMRR
     EFKVECNVGK PQVAYRETIR KAVMNQEYTH KKQTGGSGQF AKVLMNFEPL DTENGEVYEF
     VNEVTGGHIT KEFIPSIDAG VQEAMESGIL AGFPVVGVKA TVTDGQVHDV DSSEMAFKIA
     GSMCFKEAAP KAKPVILEPI MAVEVRTPEE YMGDVMGDLN SRRGSIQSMN DATGVKVIDA
     KVPLSEMFGY IGDLRSKTQG RAMFTMQMDS YAEVPKAVAD EIIKAQRGE