ID   ARGR_MYCLE              Reviewed;         167 AA.
AC   P57992;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Arginine repressor;
GN   Name=argR; OrderedLocusNames=ML1411;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Regulates arginine biosynthesis genes. {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000305}.
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DR   EMBL; AL583922; CAC30362.1; -; Genomic_DNA.
DR   PIR; E87085; E87085.
DR   RefSeq; NP_302004.1; NC_002677.1.
DR   RefSeq; WP_010908325.1; NC_002677.1.
DR   AlphaFoldDB; P57992; -.
DR   SMR; P57992; -.
DR   STRING; 272631.ML1411; -.
DR   EnsemblBacteria; CAC30362; CAC30362; CAC30362.
DR   KEGG; mle:ML1411; -.
DR   PATRIC; fig|272631.5.peg.2616; -.
DR   Leproma; ML1411; -.
DR   eggNOG; COG1438; Bacteria.
DR   HOGENOM; CLU_097103_1_1_11; -.
DR   OMA; IMGTICG; -.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000000806; 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..167
FT                   /note="Arginine repressor"
FT                   /id="PRO_0000205102"
SQ   SEQUENCE   167 AA;  17120 MW;  916EF092DB868423 CRC64;
     MTHGASKTTP ETTRAGRQAR IVAILSSTSV RSQSELATLL ADDGIDVTQA TLSRDLEELG
     AVKLRGADGG VGVYVVPEDG SPVRGVSGGT ARLSRLLSEL LVSADSSANL AVLRTPPGAA
     DYLASAIDRA ALPYVVGTIA GDDTVFVAAR EPMTGSELAT VLESLNR