ARGR_SALTY
ID ARGR_SALTY Reviewed; 156 AA.
AC P0A1B3; P37170;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Arginine repressor;
GN Name=argR; OrderedLocusNames=STM3360;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25, FUNCTION,
RP PATHWAY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=LT2;
RX PubMed=1583685; DOI=10.1016/0022-2836(92)91022-h;
RA Lu C.-D., Houghton J.E., Abdelal A.T.;
RT "Characterization of the arginine repressor from Salmonella typhimurium and
RT its interactions with the carAB operator.";
RL J. Mol. Biol. 225:11-24(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Negatively controls the expression of the four operons of
CC arginine biosynthesis in addition to the carAB operon. Predominantly
CC interacts with A/T residues in ARG boxes. {ECO:0000269|PubMed:1583685}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
CC {ECO:0000269|PubMed:1583685}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:1583685}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:1583685}.
CC -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000305}.
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DR EMBL; M75913; AAA27027.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22229.1; -; Genomic_DNA.
DR PIR; S21802; S21802.
DR RefSeq; NP_462270.1; NC_003197.2.
DR RefSeq; WP_001257852.1; NC_003197.2.
DR AlphaFoldDB; P0A1B3; -.
DR SMR; P0A1B3; -.
DR STRING; 99287.STM3360; -.
DR PaxDb; P0A1B3; -.
DR EnsemblBacteria; AAL22229; AAL22229; STM3360.
DR GeneID; 1254883; -.
DR KEGG; stm:STM3360; -.
DR PATRIC; fig|99287.12.peg.3561; -.
DR HOGENOM; CLU_097103_2_0_6; -.
DR OMA; MVYCLPP; -.
DR PhylomeDB; P0A1B3; -.
DR BioCyc; SENT99287:STM3360-MON; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001014; 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: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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Direct protein sequencing; DNA-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..156
FT /note="Arginine repressor"
FT /id="PRO_0000205111"
SQ SEQUENCE 156 AA; 17066 MW; 4936CEDE85F35FAC CRC64;
MRSSAKQEEL VRAFKALLKE EKFSSQGEIV LALQDQGFEN INQSKVSRML TKFGAVRTRN
AKMEMVYCLP AELGVPTTSS PLKNLVLDID YNDAVVVIHT SPGAAQLIAR LLDSLGKAEG
ILGTIAGDDT IFTTPASGFS VRDLYEAILE LFEQEL