ID   ARGR_STRGC              Reviewed;         156 AA.
AC   Q8GND0; A8AYK6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Arginine regulator;
GN   Name=argR; Synonyms=arcR; OrderedLocusNames=SGO_1588;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=12406748; DOI=10.1128/aem.68.11.5549-5553.2002;
RA   Dong Y., Chen Y.-Y.M., Snyder J.A., Burne R.A.;
RT   "Isolation and molecular analysis of the gene cluster for the arginine
RT   deiminase system from Streptococcus gordonii DL1.";
RL   Appl. Environ. Microbiol. 68:5549-5553(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
RN   [3]
RP   DNA-BINDING PROPERTIES.
RX   PubMed=16428398; DOI=10.1128/jb.188.3.941-949.2006;
RA   Zeng L., Dong Y., Burne R.A.;
RT   "Characterization of cis-acting sites controlling arginine deiminase gene
RT   expression in Streptococcus gordonii.";
RL   J. Bacteriol. 188:941-949(2006).
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:0000269|PubMed:12406748}.
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC       pathway.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000305}.
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DR   EMBL; AF534569; AAN65260.1; -; Genomic_DNA.
DR   EMBL; CP000725; ABV10990.1; -; Genomic_DNA.
DR   RefSeq; WP_012130653.1; NC_009785.1.
DR   AlphaFoldDB; Q8GND0; -.
DR   SMR; Q8GND0; -.
DR   STRING; 467705.SGO_1588; -.
DR   EnsemblBacteria; ABV10990; ABV10990; SGO_1588.
DR   GeneID; 61440963; -.
DR   KEGG; sgo:SGO_1588; -.
DR   eggNOG; COG1438; Bacteria.
DR   HOGENOM; CLU_097103_3_1_9; -.
DR   OMA; MIYKIFS; -.
DR   UniPathway; UPA00254; -.
DR   Proteomes; UP000001131; 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   1: Evidence at protein level;
KW   Activator; Arginine metabolism; Cytoplasm; DNA-binding; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..156
FT                   /note="Arginine regulator"
FT                   /id="PRO_0000254658"
SQ   SEQUENCE   156 AA;  17816 MW;  DDB26C901CA6E2D6 CRC64;
     MNKIESRHRL IRSLIMEKKV HTQQELQELL EANGVIVTQS TLSRDMKALN LVKVTENNIS
     YYVINSIAPS RWEKRLRFYM EDALIMLRPV QNQVVMKTLP GLAQSFGAIL DALELPQIVA
     TVCGDDVCLI ICEDNPSAIE CFDKLKEFAP PFFFSK