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ARGR1_STRP6
ID   ARGR1_STRP6             Reviewed;         157 AA.
AC   Q5XAY0;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Arginine regulator;
GN   Name=argR1; OrderedLocusNames=M6_Spy1298;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
CC   -!- FUNCTION: Regulates the transcription of the arc operon, involved in
CC       arginine catabolism. {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; CP000003; AAT87433.1; -; Genomic_DNA.
DR   RefSeq; WP_002989056.1; NC_006086.1.
DR   AlphaFoldDB; Q5XAY0; -.
DR   SMR; Q5XAY0; -.
DR   EnsemblBacteria; AAT87433; AAT87433; M6_Spy1298.
DR   KEGG; spa:M6_Spy1298; -.
DR   HOGENOM; CLU_097103_3_1_9; -.
DR   OMA; IMGTICG; -.
DR   UniPathway; UPA00254; -.
DR   Proteomes; UP000001167; 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   3: Inferred from homology;
KW   Arginine metabolism; Cytoplasm; DNA-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..157
FT                   /note="Arginine regulator"
FT                   /id="PRO_0000205132"
SQ   SEQUENCE   157 AA;  18011 MW;  4B9D8D48B59B87D2 CRC64;
     MNKKETRHQL IRSLISETTI HTQQELQERL QKNGITITQA TLSRDMKELN LVKVTSGNDT
     HYEALAISQT RWEHRLRFYM EDALVMLKIV QHQIILKTLP GLAQSFGSIL DAMQIPEIVA
     TVCGDDTCLI VCEDNEQAKA CYETLSHYTP PFFFSNK
 
 
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