EFG_CLOB1
ID EFG_CLOB1 Reviewed; 689 AA.
AC A7FZ72;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=CLB_3540;
OS Clostridium botulinum (strain ATCC 19397 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441770;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19397 / Type A;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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; CP000726; ABS35002.1; -; Genomic_DNA.
DR RefSeq; WP_003357512.1; NC_009697.1.
DR AlphaFoldDB; A7FZ72; -.
DR SMR; A7FZ72; -.
DR PRIDE; A7FZ72; -.
DR GeneID; 5187731; -.
DR KEGG; cba:CLB_3540; -.
DR HOGENOM; CLU_002794_4_1_9; -.
DR OMA; AATTCHW; -.
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.
FT CHAIN 1..689
FT /note="Elongation factor G"
FT /id="PRO_0000335839"
FT DOMAIN 9..283
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 82..86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 689 AA; 76395 MW; E905C2BE1C1B141A CRC64;
MANKEYPLAK FRNIGIMAHI DAGKTTATER ILFYTGKTHK IGETHEGAAT MDWMEQEQER
GITITSAATT CFWKDHQVNI IDTPGHVDFT VEVERSLRVL DGAVTILDAK SGVEPQTETV
WRQADNYKVP RMVFINKMDK LGADFLMSVG TLRERLHANA VPLQLPIGAE DSFSGIIDLV
KNDAVIYKDD LGTVMDETEI PEDMKEIAEE YRTMLLEAVA EVDEDIMMKY LEGEEISVEE
IKTALRKGVL ANKIVPVLCG SAYKNKGVQL LLDAIIEFMP SPLDIEDVKG TEPTTGEEMT
RPADAKAPLA ALAFKIATDP FIGKLAFTRI YSGTMKSGTY VFNSNKGKRE RIGRLVKMHA
NHREDVEELK AGELGAIVGL KDTTTGDTLC DDADPIILEN MEFPEPVIDV SIEPKTKAGQ
EKMGIALAKL AEEDPTFRTY TNQETGQTII AGMGELHLEI IVDRLIREFK VECNVGQPQV
AYKETIKKHV KAEGKFIRQS GGRGQYGHCW IEMMPTEGEY EFQNAVVGGS IPKEYIPAID
NGIQEASQSG IIAGYPVINF KVKLFDGSYH DVDSSEMAFK IAGSMAFKNA MSKADAVLLE
PSMKVEVVVP EEYMGDVIGD INSRRGRIEG MTPRAGAEVI RAFVPLSEMF GYATTLRSKT
QGRGNYVMQF DHYEEVPKSI QDKVIGERK