ID   ARGR1_CLOPE             Reviewed;         151 AA.
AC   Q46172;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, sequence version 2.
DT   25-MAY-2022, entry version 139.
DE   RecName: Full=Arginine regulator;
GN   Name=argR1; Synonyms=ahrC, argR; OrderedLocusNames=CPE0172;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=9053381; DOI=10.1111/j.1574-6968.1997.tb10186.x;
RA   Ohtani K., Bando M., Swe T., Banu S., Oe M., Hayashi H., Shimizu T.;
RT   "Collagenase gene (colA) is located in the 3'-flanking region of the
RT   perfringolysin O (pfoA) locus in Clostridium perfringens.";
RL   FEMS Microbiol. Lett. 146:155-159(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC   -!- FUNCTION: Regulates the transcription of the arc operon, involved in
CC       arginine catabolism. {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC       pathway.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000305}.
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DR   EMBL; X97768; CAA66368.1; -; Genomic_DNA.
DR   EMBL; BA000016; BAB79878.1; -; Genomic_DNA.
DR   RefSeq; WP_003457490.1; NC_003366.1.
DR   AlphaFoldDB; Q46172; -.
DR   SMR; Q46172; -.
DR   EnsemblBacteria; BAB79878; BAB79878; BAB79878.
DR   GeneID; 29572713; -.
DR   KEGG; cpe:CPE0172; -.
DR   HOGENOM; CLU_097103_3_0_9; -.
DR   OMA; IMGTICG; -.
DR   UniPathway; UPA00254; -.
DR   Proteomes; UP000000818; 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:0019547; P:arginine catabolic process to ornithine; 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.
PE   3: Inferred from homology;
KW   Arginine metabolism; Cytoplasm; DNA-binding; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..151
FT                   /note="Arginine regulator"
FT                   /id="PRO_0000205079"
FT   CONFLICT        126
FT                   /note="K -> T (in Ref. 1; CAA66368)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144..151
FT                   /note="KELDSLRV -> RN (in Ref. 1; CAA66368)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   151 AA;  17427 MW;  9A9D411E0E4C9A9C CRC64;
     MSNLEKSLRH EVILDIIESK CICKQEELII ELKECGINVT QATLSRDLHE MNIIRKSFEN
     HEHRYIVTKE DKFIKKFKNI FKSSVRSISM QEYFISVNTL DGMASLIGEF IDRLGDGRIA
     GTVAKKNHIL VLCRSVNATQ QIFKELDSLR V