ID   ARGR_STAES              Reviewed;         150 AA.
AC   Q8CP40;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 2.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Arginine repressor {ECO:0000255|HAMAP-Rule:MF_00173};
GN   Name=argR {ECO:0000255|HAMAP-Rule:MF_00173}; OrderedLocusNames=SE_1201;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO04800.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE015929; AAO04800.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_764756.1; NC_004461.1.
DR   RefSeq; WP_002456185.1; NZ_WBME01000006.1.
DR   AlphaFoldDB; Q8CP40; -.
DR   SMR; Q8CP40; -.
DR   STRING; 176280.SE_1201; -.
DR   EnsemblBacteria; AAO04800; AAO04800; SE_1201.
DR   GeneID; 50018681; -.
DR   KEGG; sep:SE_1201; -.
DR   PATRIC; fig|176280.10.peg.1171; -.
DR   eggNOG; COG1438; Bacteria.
DR   HOGENOM; CLU_097103_3_0_9; -.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000001411; 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_0000205120"
SQ   SEQUENCE   150 AA;  17128 MW;  A02D47BE8092B0E9 CRC64;
     MPKKSVRHIK IREIISNEQI ETQDELVKRL NEYDLNVTQA TVSRDIKELQ LIKVPAPTGQ
     YVYSLPNDRR YHPLEKLGRY LMDSFVNIEG TGNLLVLKTL PGNAQSIGAI LDQIDWDEVL
     GTICGDDTCL LICRDEEASE EIKTRIFNLL