EFG_ALKHC
ID EFG_ALKHC Reviewed; 692 AA.
AC Q9Z9L7; Q9KGD9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Elongation factor G;
DE Short=EF-G;
GN Name=fusA; Synonyms=fus; OrderedLocusNames=BH0131;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=10192928; DOI=10.1271/bbb.63.452;
RA Takami H., Takaki Y., Nakasone K., Hirama C., Inoue A., Horikoshi K.;
RT "Sequence analysis of a 32-kb region including the major ribosomal protein
RT gene clusters from alkaliphilic Bacillus sp. strain C-125.";
RL Biosci. Biotechnol. Biochem. 63:452-455(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000305}.
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DR EMBL; AB017508; BAA75268.1; -; Genomic_DNA.
DR EMBL; BA000004; BAB03850.1; -; Genomic_DNA.
DR PIR; C83666; C83666.
DR PIR; T44380; T44380.
DR RefSeq; WP_010896314.1; NC_002570.2.
DR AlphaFoldDB; Q9Z9L7; -.
DR SMR; Q9Z9L7; -.
DR STRING; 272558.10172743; -.
DR EnsemblBacteria; BAB03850; BAB03850; BAB03850.
DR KEGG; bha:BH0131; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_9; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 88967at2; -.
DR Proteomes; UP000001258; 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..692
FT /note="Elongation factor G"
FT /id="PRO_0000091066"
FT DOMAIN 8..282
FT /note="tr-type G"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 115
FT /note="Q -> H (in Ref. 1; BAA75268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 692 AA; 76889 MW; 2819AE8E5547E81E CRC64;
MAREFSLENT RNIGIMAHID AGKTTTTERI LFYTGRIHKI GETHEGASQM DWMEQEQERG
ITITSAATTA QWKNNRINII DTPGHVDFTV EVERSLRVLD GAVAVLDAQS GVEPQTETVW
RQATTYGVPR VVFVNKMDKT GADFLYSVST LHDRLQANAH PIQLPIGAED NFEGIIDLVD
MVAYFYEDDL GTRTEAKEIP DEYKEQAQEY HEKLVEAAAE LDEELMMKYL EGEELTKDEL
KAAIRKGTCN VEFYPVLCGS AFKNKGVQLM LDAVLDYLPS PLDVPAIKGH VPDTEEEAVR
KPGDDQPFAA LAFKVMTDPY VGKLTFFRVY SGTLDSGSYV KNSTKDKRER VGRILQMHAN
HREEISTVYS GDIAAAVGLK DTSTGDTLCD EKNLVILESM EFPEPVIHLS VEPKSKADQD
KMGLALAKLA EEDPTFKTHT DEETGQTIIA GMGELHLDII VDRLRREFKV EANVGAPQVS
YRETIRQAAQ VEGKFVRQSG GRGQYGHVWI EFSPNEEGAG FEFVNGIVGG VVPREYIPSV
QAGLEEALEN GLLAGYPVID IKAKLFDGSY HDVDSSEMAF KIAASMALKN AKSKCNPVLL
EPMMKVEVVV PEEYMGDVMG DITSRRGRVE GMEARGNAQV VKAFVPLAEM FGYATSLRSR
TQGRGTYTMF FDHYEEVPKS ISEEIIKKNS GE
