ARGR_GEOSE
ID ARGR_GEOSE Reviewed; 149 AA.
AC O31408;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Arginine repressor;
GN Name=argR;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCIMB 8224 / CCM 2186 / NCA C-1235.1 / VKM B-718;
RX PubMed=9282750; DOI=10.1046/j.1365-2958.1997.4781845.x;
RA Dion M., Charlier D.R.M., Wang H., Gigot D., Savchenko A., Hallet J.-N.,
RA Glansdorff N., Sakanyan V.;
RT "The highly thermostable arginine repressor of Bacillus stearothermophilus:
RT gene cloning and repressor-operator interactions.";
RL Mol. Microbiol. 25:385-398(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=10331868; DOI=10.1038/8229;
RA Ni J., Sakanyan V., Charlier D., Glansdorff N., van Duyne G.D.;
RT "Structure of the arginine repressor from Bacillus stearothermophilus.";
RL Nat. Struct. Biol. 6:427-432(1999).
CC -!- FUNCTION: Regulates arginine biosynthesis genes.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
CC -!- SUBUNIT: Homohexamer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000305}.
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DR EMBL; Y09546; CAA70737.1; -; Genomic_DNA.
DR PDB; 1B4A; X-ray; 2.50 A; A/B/C/D/E/F=2-149.
DR PDB; 1B4B; X-ray; 2.20 A; A/B/C=79-149.
DR PDBsum; 1B4A; -.
DR PDBsum; 1B4B; -.
DR AlphaFoldDB; O31408; -.
DR SMR; O31408; -.
DR UniPathway; UPA00068; -.
DR EvolutionaryTrace; O31408; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034618; F:arginine binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_00173; Arg_repressor; 1.
DR InterPro; IPR001669; Arg_repress.
DR InterPro; IPR020899; Arg_repress_C.
DR InterPro; IPR036251; Arg_repress_C_sf.
DR InterPro; IPR020900; Arg_repress_DNA-bd.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR34471; PTHR34471; 1.
DR Pfam; PF01316; Arg_repressor; 1.
DR Pfam; PF02863; Arg_repressor_C; 1.
DR PRINTS; PR01467; ARGREPRESSOR.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF55252; SSF55252; 1.
DR TIGRFAMs; TIGR01529; argR_whole; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW DNA-binding; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..149
FT /note="Arginine repressor"
FT /id="PRO_0000205071"
FT HELIX 5..16
FT /evidence="ECO:0007829|PDB:1B4A"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:1B4A"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:1B4A"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1B4A"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1B4A"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1B4A"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1B4A"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:1B4B"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1B4B"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:1B4B"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:1B4B"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1B4B"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:1B4B"
FT HELIX 135..146
FT /evidence="ECO:0007829|PDB:1B4B"
SQ SEQUENCE 149 AA; 16805 MW; F15E1ACD89E006E8 CRC64;
MNKGQRHIKI REIIMSNDIE TQDELVDRLR EAGFNVTQAT VSRDIKEMQL VKVPMANGRY
KYSLPSDQRF NPLQKLKRAL VDVFIKLDGT GNLLVLRTLP GNAHAIGVLL DNLDWDEIVG
TICGDDTCLI ICRTPKDAKK VSNQLLSML