ARGR1_STRP3
ID ARGR1_STRP3 Reviewed; 157 AA.
AC P0CZ68; Q7CEX2; Q879A7;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Arginine regulator;
GN Name=argR1; OrderedLocusNames=SpyM3_1198;
OS Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=198466;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-595 / MGAS315;
RX PubMed=12122206; DOI=10.1073/pnas.152298499;
RA Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT encoded toxins, the high-virulence phenotype, and clone emergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014074; AAM79805.1; -; Genomic_DNA.
DR RefSeq; WP_002989056.1; NC_004070.1.
DR AlphaFoldDB; P0CZ68; -.
DR SMR; P0CZ68; -.
DR EnsemblBacteria; AAM79805; AAM79805; SpyM3_1198.
DR KEGG; spg:SpyM3_1198; -.
DR HOGENOM; CLU_097103_3_1_9; -.
DR OMA; IMGTICG; -.
DR UniPathway; UPA00254; -.
DR Proteomes; UP000000564; 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_0000205130"
SQ SEQUENCE 157 AA; 18011 MW; 4B9D8D48B59B87D2 CRC64;
MNKKETRHQL IRSLISETTI HTQQELQERL QKNGITITQA TLSRDMKELN LVKVTSGNDT
HYEALAISQT RWEHRLRFYM EDALVMLKIV QHQIILKTLP GLAQSFGSIL DAMQIPEIVA
TVCGDDTCLI VCEDNEQAKA CYETLSHYTP PFFFSNK