ARGR_SHIFL
ID ARGR_SHIFL Reviewed; 156 AA.
AC P0A6D2; P15282;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Arginine repressor;
GN Name=argR; OrderedLocusNames=SF3277, S3492;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Regulates arginine biosynthesis genes. {ECO:0000250}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000305}.
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DR EMBL; AE005674; AAN44741.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18551.1; -; Genomic_DNA.
DR RefSeq; NP_709034.1; NC_004337.2.
DR RefSeq; WP_001257846.1; NZ_WPGW01000026.1.
DR AlphaFoldDB; P0A6D2; -.
DR SMR; P0A6D2; -.
DR STRING; 198214.SF3277; -.
DR EnsemblBacteria; AAN44741; AAN44741; SF3277.
DR EnsemblBacteria; AAP18551; AAP18551; S3492.
DR GeneID; 1027085; -.
DR GeneID; 66672867; -.
DR KEGG; sfl:SF3277; -.
DR KEGG; sfx:S3492; -.
DR PATRIC; fig|198214.7.peg.3883; -.
DR HOGENOM; CLU_097103_2_0_6; -.
DR OMA; MVYCLPP; -.
DR OrthoDB; 1640037at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
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;
KW DNA recombination; DNA-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..156
FT /note="Arginine repressor"
FT /id="PRO_0000205113"
SQ SEQUENCE 156 AA; 16995 MW; 2F104577EFC46537 CRC64;
MRSSAKQEEL VKAFKALLKE EKFSSQGEIV AALQEQGFDN INQSKVSRML TKFGAVRTRN
AKMEMVYCLP AELGVPTTSS PLKNLVLDID YNDAVVVIHT SPGAAQLIAR LLDSLGKAEG
ILGTIAGDDT IFTTPANGFT VKDLYEAILE LFDQEL