ID A0A0G4AZC5_9BACT Unreviewed; 698 AA.
AC A0A0G4AZC5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Elongation factor G {ECO:0000256|HAMAP-Rule:MF_00054};
DE Short=EF-G {ECO:0000256|HAMAP-Rule:MF_00054};
GN Name=fusA {ECO:0000256|HAMAP-Rule:MF_00054,
GN ECO:0000313|EMBL:AKM80082.1};
GN ORFNames=UW38_C0001G0217 {ECO:0000313|EMBL:AKM80082.1};
OS Candidatus Saccharibacteria bacterium GW2011_GWC2_44_17.
OC Bacteria; Candidatus Saccharibacteria.
OX NCBI_TaxID=1619070 {ECO:0000313|EMBL:AKM80082.1, ECO:0000313|Proteomes:UP000035655};
RN [1] {ECO:0000313|EMBL:AKM80082.1, ECO:0000313|Proteomes:UP000035655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:0000256|HAMAP-
CC Rule:MF_00054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|ARBA:ARBA00005870, ECO:0000256|HAMAP-
CC Rule:MF_00054}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00054}.
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DR EMBL; CP011211; AKM80082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4AZC5; -.
DR STRING; 1619070.UW38_C0001G0217; -.
DR KEGG; sbag:UW38_C0001G0217; -.
DR PATRIC; fig|1619070.4.peg.210; -.
DR Proteomes; UP000035655; 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; cd01886; EF-G; 1.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR CDD; cd04088; EFG_mtEFG_II; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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; IPR047872; EFG_IV.
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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_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 NCBIfam; TIGR00484; EF-G; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
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; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00054};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00054}.
FT DOMAIN 9..287
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 18..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 85..89
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 698 AA; 76553 MW; C0B78F5500F98629 CRC64;
MAEKNVPLKD FRNIGIIAHI DAGKTTTTEG ILYRTGINHK IGQVKGDDPA GATTDWMAQE
KERGITITSA AVTAFWKGHK INIIDTPGHI DFTAEVERSL RVLDGAVTVF DGKMGVEAQT
ETVWRQANKY GVPRICFINK INQTGGDFYK SLETIHNRLS RQALPIHLPI GFEKEINGVV
DLVDMKAYTY TDYTDHELVP GEIPADMLDK AKNARSLLVE AAVEADDELF ERFLDKGEES
ITIDELKAAL RKRVLAGDFF LVTGGDGRGV IVEKVLDLAA DYLPSPLDVD AIWGENPKTG
EEVQRKPDVT EPLSALAFKI ATDPFVGKLI FVRVYSGTLK AGSYVLNTTT GNKERVGRIV
RMHADKREEI DEIAAGDIAA VVGLKETFTG ATLADPAHPI TLESITFPEP PVSIAVEPKT
KSDQEKMGIA LQRLAEEDPT FRIHTDEETG QTIMSGMGEL HLDILIDRMK REFNVEANIG
EPQVAFRETI RGTSEVQGKH AKQSGGRGQY GDVWIRFEPN ETGKGFEFTD AIKGGVVPQE
YRKPVEQGIV ETLNGGVIAG YPVVDIKATL YDGSYHDVDS SELAFKLAGS LATREGIKQA
KPVILEPVMK VEVTTPEEFM GDVIGDLNAR RGRIEAMEDL QGGAKLVRGI VPLASMFGYT
NDIRSMSQGR AASTMELAQY EEVPPNVAQE IIEKRASK
//
