ID   ARGR_CLOBM              Reviewed;         150 AA.
AC   B1KT46;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Arginine repressor {ECO:0000255|HAMAP-Rule:MF_00173};
GN   Name=argR {ECO:0000255|HAMAP-Rule:MF_00173}; OrderedLocusNames=CLK_1268;
OS   Clostridium botulinum (strain Loch Maree / Type A3).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=498214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Loch Maree / Type A3;
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: 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; CP000962; ACA55363.1; -; Genomic_DNA.
DR   RefSeq; WP_012343354.1; NC_010520.1.
DR   AlphaFoldDB; B1KT46; -.
DR   SMR; B1KT46; -.
DR   EnsemblBacteria; ACA55363; ACA55363; CLK_1268.
DR   KEGG; cbl:CLK_1268; -.
DR   HOGENOM; CLU_097103_3_0_9; -.
DR   OMA; IMGTICG; -.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000000722; 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   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..150
FT                   /note="Arginine repressor"
FT                   /id="PRO_1000097866"
SQ   SEQUENCE   150 AA;  16467 MW;  3B07C075214863DA CRC64;
     MKVSRHAKIL EIINSKDIDT QEELAEELKK MGMNVTQATV SRDIKELKLI KVLGNTGKYK
     YATINHTESY MSDKLINIFA QTVINVENID KLIIIKAISG SAPAAAEAID TLGFDGVAGT
     IAGDNTIFVM ARTNEKAQEI TMKLKKIINA