ARGR_ALKHC
ID ARGR_ALKHC Reviewed; 149 AA.
AC Q9K973;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Arginine repressor {ECO:0000255|HAMAP-Rule:MF_00173};
GN Name=argR {ECO:0000255|HAMAP-Rule:MF_00173}; Synonyms=ahrC;
GN OrderedLocusNames=BH2777;
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 [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: Regulates arginine biosynthesis genes. {ECO:0000255|HAMAP-
CC Rule:MF_00173}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00173}.
CC -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000255|HAMAP-
CC Rule:MF_00173}.
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DR EMBL; BA000004; BAB06496.1; -; Genomic_DNA.
DR PIR; A83997; A83997.
DR RefSeq; WP_010898925.1; NC_002570.2.
DR PDB; 5CJ9; X-ray; 2.41 A; A=6-149.
DR PDBsum; 5CJ9; -.
DR AlphaFoldDB; Q9K973; -.
DR SMR; Q9K973; -.
DR STRING; 272558.10175398; -.
DR EnsemblBacteria; BAB06496; BAB06496; BAB06496.
DR KEGG; bha:BH2777; -.
DR eggNOG; COG1438; Bacteria.
DR HOGENOM; CLU_097103_3_0_9; -.
DR OMA; IMGTICG; -.
DR OrthoDB; 1640037at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001258; Chromosome.
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; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..149
FT /note="Arginine repressor"
FT /id="PRO_0000205066"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:5CJ9"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:5CJ9"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:5CJ9"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:5CJ9"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:5CJ9"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:5CJ9"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:5CJ9"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:5CJ9"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:5CJ9"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:5CJ9"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:5CJ9"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:5CJ9"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:5CJ9"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:5CJ9"
SQ SEQUENCE 149 AA; 16836 MW; 7075A0992DC4F454 CRC64;
MNKGQRHIKI REIIANNDVE TQDELVEQLK AAGYNVTQAT VSRDIKELHL VKVPMMDGRY
KYSLPADQRF NPLQKLKRGL VDSFVSIDRT DNLIVMKTLP GNAHAIGALI DNLDWTEIMG
TICGDDTILI ICKDKQDGPV VTERFLNML
