ID I7LK47_9CLOT Unreviewed; 693 AA.
AC I7LK47;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=CAAU_2109 {ECO:0000313|EMBL:CCJ34193.1};
OS Caloramator australicus RC3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Caloramator.
OX NCBI_TaxID=857293 {ECO:0000313|EMBL:CCJ34193.1, ECO:0000313|Proteomes:UP000007652};
RN [1] {ECO:0000313|EMBL:CCJ34193.1, ECO:0000313|Proteomes:UP000007652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RC3 {ECO:0000313|EMBL:CCJ34193.1,
RC ECO:0000313|Proteomes:UP000007652};
RX PubMed=21421756; DOI=10.1128/JB.00193-11;
RA Ogg C.D., Patel B.K.C.;
RT "Draft genome sequence of Caloramator australicus strain RC3T, a
RT thermoanaerobe from the Great Artesian Basin of Australia.";
RL J. Bacteriol. 193:2664-2665(2011).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCJ34193.1}.
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DR EMBL; CAKP01000112; CCJ34193.1; -; Genomic_DNA.
DR RefSeq; WP_008909449.1; NZ_CAKP01000112.1.
DR AlphaFoldDB; I7LK47; -.
DR STRING; 857293.CAAU_2109; -.
DR eggNOG; COG0480; Bacteria.
DR OrthoDB; 9804431at2; -.
DR Proteomes; UP000007652; 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:UP000007652}.
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 693 AA; 76754 MW; 1C6AE8F82D4F218B CRC64;
MPRTFPLEKV RNIGIMAHID AGKTTTTERI LFYTGRTHKL GEVHEGAATM DWMVQEQERG
ITITSAATTC QWKGHVINII DTPGHVDFTV EVERSLRVLD GAVAVFCAKG GVEPQSETVW
RQADKYGVPR IAYVNKMDIM GADFFNVIQM MKDRLGTKPV AIQLPIGKED TFKGVIDLIK
NEAIIYVDDL GTQAEETEVP EDMKDIVEEY RTHLIEAVAE TDEELMMKYL EGEEFTEEEI
KVALRKATIS GELVPVVCGS SYKNKGVQLL LDAVVEYLPS PVDIPSVKGI NPDSGEEDER
HASDDEPLSA LAFKIMADPF VGKLAFVRVY SGVLTAGTYV LNSTKGKKER IGRLVKMHAN
HREDVEEIRA GDIGACVGLK EVITGDTLCD PDKPIILEKM EFPEPVIHVA IEPKTKAGQE
KMALALQKLS EEDPSFKTYT DQETGQTIIA GMGELHLEII VDRLQREFKV ECNVGKPQVA
YKETVRKAVK AEGKFVRQSG GRGQYGHCWI ELIPQERGKG YEFVNNIVGG VIPKEYIPAI
DNGIQEAMLS GVVAGYPVMD VKVILFDGSY HEVDSSEMAF KIAGSMAFKN AMQKADPVLL
EPIMKVEVVV PEEYMGDVIG DINSRRGRIE GMEPRGGAQV IRAYVPLAEM FGYATTLRSR
TQGRGTYVMQ FDHYEEVPAS IQAQIVGAKE KNA
//
