ID A0A1I5YVK9_9FIRM Unreviewed; 688 AA.
AC A0A1I5YVK9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Elongation factor G {ECO:0000256|ARBA:ARBA00017872, 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 ORFNames=SAMN05444406_1704 {ECO:0000313|EMBL:SFQ48276.1};
OS Caldicoprobacter faecalis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Caldicoprobacteraceae;
OC Caldicoprobacter.
OX NCBI_TaxID=937334 {ECO:0000313|EMBL:SFQ48276.1, ECO:0000313|Proteomes:UP000198577};
RN [1] {ECO:0000313|EMBL:SFQ48276.1, ECO:0000313|Proteomes:UP000198577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20678 {ECO:0000313|EMBL:SFQ48276.1,
RC ECO:0000313|Proteomes:UP000198577};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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: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}.
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DR EMBL; FOXR01000070; SFQ48276.1; -; Genomic_DNA.
DR RefSeq; WP_025748458.1; NZ_FOXR01000070.1.
DR AlphaFoldDB; A0A1I5YVK9; -.
DR STRING; 937334.SAMN05444406_1704; -.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000198577; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000198577}.
FT DOMAIN 8..282
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 688 AA; 76620 MW; BB037F3897C809BA CRC64;
MLREVAMEKV RNIGIMAHID AGKTTTTERI LFYTGKIHRM GEVHEGTATM DWMVQEQERG
ITITSAATTA IWKGHFINII DTPGHVDFTV EVERSLRVLD GSVAIFCAKG GVEPQSETVW
RQANKYKVPR LAYVNKMDIV GADFFNVVNM IRERLGANPV PIQIPIGKEA DFRGIVDLVR
NKAIYYLDDL GTQSEEKEVP DDLKELVEEY RTKLLEVVAE QDDELMMKYL EGEELAEEEI
KAALRKATIS FKIVPVLCGS SYRNKGVQPL LDAIVDYLPS PLDLPPVVGT SPDTGGEIVR
HPSDDEPLSA LAFKVMVDPY VGKLVYVRVY SGVLRSGTYV YNTTRGTKER IGRVLRMHAD
HREEISEAYA GDIVAVVGLK NTITGHTLCD ENNPIVLESM VFPEPVIQVA IEPKTKAGQE
KLSVALQRLA EEDPTFRAFV DHETGQTIIA GMGELHLEII VDRLVREFKV EANVGKPQVA
YRETIKKAVK AEGRFIRQTG GRGQYGHVWL EVEPLEPGKG FEFVNKIVGG VIPKEYIPAV
ESGVREAMES GVLAGYPVID VRVTVFDGSY HEVDSSEMAF KVAASMAFKE AMQKADPVLL
EPIMKVEVTV PEEYMGDVIG DISSRRGRIE GTELRSGVQV IKAYVPLAEM FGYATDLRSK
TQGRGSYVMQ MSHYEEVPKN LLEKIIKK
//
