ID   ARGR_SHIDS              Reviewed;         156 AA.
AC   Q32BA2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Arginine repressor {ECO:0000255|HAMAP-Rule:MF_00173};
GN   Name=argR {ECO:0000255|HAMAP-Rule:MF_00173}; OrderedLocusNames=SDY_3413;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB63403.1; -; Genomic_DNA.
DR   RefSeq; WP_001257846.1; NC_007606.1.
DR   RefSeq; YP_404894.1; NC_007606.1.
DR   AlphaFoldDB; Q32BA2; -.
DR   SMR; Q32BA2; -.
DR   STRING; 300267.SDY_3413; -.
DR   EnsemblBacteria; ABB63403; ABB63403; SDY_3413.
DR   GeneID; 66672867; -.
DR   KEGG; sdy:SDY_3413; -.
DR   PATRIC; fig|300267.13.peg.4071; -.
DR   HOGENOM; CLU_097103_2_0_6; -.
DR   OMA; MVYCLPP; -.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000002716; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; DNA-binding;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..156
FT                   /note="Arginine repressor"
FT                   /id="PRO_1000023598"
SQ   SEQUENCE   156 AA;  16995 MW;  2F104577EFC46537 CRC64;
     MRSSAKQEEL VKAFKALLKE EKFSSQGEIV AALQEQGFDN INQSKVSRML TKFGAVRTRN
     AKMEMVYCLP AELGVPTTSS PLKNLVLDID YNDAVVVIHT SPGAAQLIAR LLDSLGKAEG
     ILGTIAGDDT IFTTPANGFT VKDLYEAILE LFDQEL