ID   ARGR_STRSU              Reviewed;         157 AA.
AC   Q3C167;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Arginine regulator;
GN   Name=argR;
OS   Streptococcus suis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=I9841/1;
RX   PubMed=12446626; DOI=10.1128/jb.184.24.6768-6776.2002;
RA   Winterhoff N., Goethe R., Gruening P., Valentin-Weigand P.;
RT   "Identification and characterization of two temperature-induced surface-
RT   associated proteins of Streptococcus suis with high homologies to members
RT   of the arginine deiminase system of Streptococcus pyogenes.";
RL   J. Bacteriol. 184:6768-6776(2002).
CC   -!- FUNCTION: In the presence of arginine, coactivates the transcription of
CC       the arcABDC operon, with other regulatory proteins such as ArcR and
CC       CcpA. {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; AF546864; ABB17163.1; -; Genomic_DNA.
DR   RefSeq; WP_002941715.1; NZ_WODB01000009.1.
DR   AlphaFoldDB; Q3C167; -.
DR   SMR; Q3C167; -.
DR   STRING; 996306.SSUR61_1255; -.
DR   GeneID; 8153608; -.
DR   eggNOG; COG1438; Bacteria.
DR   OMA; IMGTICG; -.
DR   OrthoDB; 1640037at2; -.
DR   UniPathway; UPA00254; -.
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   Activator; Arginine metabolism; Cytoplasm; DNA-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..157
FT                   /note="Arginine regulator"
FT                   /id="PRO_0000254659"
SQ   SEQUENCE   157 AA;  17862 MW;  A841EB6138E3EED7 CRC64;
     MNKIESRHQL ILSLIMEKKI HTQQELQELL EVNGVSVTQS TLSRDIKMLN LVKVNEDDSS
     HYVINPIAPT RWEKRLRLYM EDALVMLKPI QHQVVLKTLP GLANSFGSIL DAMEIPQIVA
     TVCGDDVCLI ICEDVEGAQA CFEHLKQFTP PFFFSKL