ID   EFG_BIFLO               Reviewed;         707 AA.
AC   Q8G5B6;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=BL1098;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN24906.1; -; Genomic_DNA.
DR   RefSeq; NP_696270.1; NC_004307.2.
DR   RefSeq; WP_003832662.1; NC_004307.2.
DR   AlphaFoldDB; Q8G5B6; -.
DR   SMR; Q8G5B6; -.
DR   STRING; 206672.BL1098; -.
DR   EnsemblBacteria; AAN24906; AAN24906; BL1098.
DR   GeneID; 66504765; -.
DR   KEGG; blo:BL1098; -.
DR   PATRIC; fig|206672.9.peg.806; -.
DR   HOGENOM; CLU_002794_4_1_11; -.
DR   OMA; AATTCHW; -.
DR   PhylomeDB; Q8G5B6; -.
DR   Proteomes; UP000000439; 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..707
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091077"
FT   DOMAIN          9..293
FT                   /note="tr-type G"
FT   BINDING         18..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         90..94
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         144..147
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   707 AA;  78137 MW;  7E928EEA3C654974 CRC64;
     MAEEISDLHD VRNIGIMAHI DAGKTTTTER ILFYTGKNYK IGETHDGAST MDFMAQEQER
     GITIQSAATT CFWSRQSHDT KDKFQINIID TPGHVDFTAE VERSLRVLDG AVAVFDGKEG
     VEPQSETVWR QADKYGVPRI CFINKMDKLG ANFYYSVDTI KEKLGATPIV MQLPIGSEND
     FTGVVDLVEM QAYVWNGTEE LGAKYDTTEI PDDLKDKAQE YHEKLVEAAA EADDDLMNKF
     FEDGDLSKED IRAGVRKLTI AKEAFPIFCG SAFKDKGVQP MLDGVVDYLP SPEDVPAIKG
     YKPGDESVEI DRHPVKSDPF AALVFKISTH PFYGKLVFVR VYSGSVVPGD SVLDSTREKK
     ERIGKIFQMH ADKENPMDRA DAGNIYTFVG LKNVTTGDTL CAIDDPITLD SMTFPDPVIQ
     VAVEPKTKAD QEKMGIALSK LAEEDPTFQV TTDEESGQTL IAGMGELQLD IIVDRMRREF
     KVECNQGKPQ VAYRETIRKA VMDQGYTHKK QTGGSGQFAK VLMNFEPLDT TEGKTFEFEN
     KVTGGHISAE FIGPIEAGVK EAMESGVLAG FPVVGVKATV TDGQMHPVDS SEMAFKLAGS
     MCFKEAAPKA KPVILEPIMK VEVRTPEEYM GEVIGDLNQR RGNIQSMTDG VGVKVIDAKV
     PLSEMFGYIG DLRSKTQGRA MFTMEMDSYD EVPKSVSEEI IKAQRGE