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ARGR2_BACC1
ID   ARGR2_BACC1             Reviewed;         149 AA.
AC   Q731B9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Arginine repressor {ECO:0000255|HAMAP-Rule:MF_00173};
GN   Name=argR2 {ECO:0000255|HAMAP-Rule:MF_00173}; OrderedLocusNames=BCE_4247;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS43148.1; -; Genomic_DNA.
DR   RefSeq; WP_001032581.1; NC_003909.8.
DR   AlphaFoldDB; Q731B9; -.
DR   SMR; Q731B9; -.
DR   EnsemblBacteria; AAS43148; AAS43148; BCE_4247.
DR   GeneID; 59155251; -.
DR   GeneID; 64199525; -.
DR   KEGG; bca:BCE_4247; -.
DR   HOGENOM; CLU_097103_3_0_9; -.
DR   OMA; IMGTICG; -.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000002527; 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..149
FT                   /note="Arginine repressor"
FT                   /id="PRO_0000205061"
SQ   SEQUENCE   149 AA;  16928 MW;  51F35245A25BECA9 CRC64;
     MNKGQRHIKI REIIANKEIE TQDELVDILR NEGFNVTQAT VSRDIKELHL VKVPLHDGRY
     KYSLPADQRF NPLQKLKRNL VDSFVKLDTA GHMLVLKTLP GNAHSLGALI DHLEWDEIIG
     TICGDDTCLI ICRTPEDTGV VSDRFLNML
 
 
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