ARGR_ECOLI
ID ARGR_ECOLI Reviewed; 156 AA.
AC P0A6D0; P15282; Q2M8X6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Arginine repressor;
GN Name=argR; Synonyms=xerA; OrderedLocusNames=b3237, JW3206;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3149585; DOI=10.1002/j.1460-2075.1988.tb03338.x;
RA Stirling C.J., Szatmari G., Stewart G., Smith M.C.M., Sherratt D.J.;
RT "The arginine repressor is essential for plasmid-stabilizing site-specific
RT recombination at the ColE1 cer locus.";
RL EMBO J. 7:4389-4395(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3116542; DOI=10.1073/pnas.84.19.6697;
RA Lim D., Oppenheim J.D., Eckhardt T., Maas W.K.;
RT "Nucleotide sequence of the argR gene of Escherichia coli K-12 and
RT isolation of its product, the arginine repressor.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6697-6701(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [6]
RP STRUCTURE BY NMR OF 1-78.
RX PubMed=9334747; DOI=10.1038/nsb1097-819;
RA Seelander-Sunnerhagen M., Nilges M., Otting G., Carey J.;
RT "Solution structure of the DNA-binding domain and model for the complex of
RT multifunctional hexameric arginine repressor with DNA.";
RL Nat. Struct. Biol. 4:819-826(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 80-156.
RX PubMed=8594204; DOI=10.1006/jmbi.1996.0093;
RA van Duyne G.D., Ghosh G., Maas W.K., Sigler P.B.;
RT "Structure of the oligomerization and L-arginine binding domain of the
RT arginine repressor of Escherichia coli.";
RL J. Mol. Biol. 256:377-391(1996).
RN [8]
RP IDENTIFICATION OF DNA-BINDING DOMAIN.
RX PubMed=7490739; DOI=10.1006/jmbi.1995.0607;
RA Grandori R., Lavoie T.A., Pflumm M., Tian G., Niersbach H., Maas W.K.,
RA Fairman R., Carey J.;
RT "The DNA-binding domain of the hexameric arginine repressor.";
RL J. Mol. Biol. 254:150-162(1995).
RN [9]
RP MUTAGENESIS.
RX PubMed=7997173; DOI=10.1111/j.1365-2958.1994.tb00455.x;
RA Burke M., Merican A.F., Sherratt D.J.;
RT "Mutant Escherichia coli arginine repressor proteins that fail to bind L-
RT arginine, yet retain the ability to bind their normal DNA-binding sites.";
RL Mol. Microbiol. 13:609-618(1994).
RN [10]
RP MUTAGENESIS.
RX PubMed=7997172; DOI=10.1111/j.1365-2958.1994.tb00454.x;
RA Tian G., Maas W.K.;
RT "Mutational analysis of the arginine repressor of Escherichia coli.";
RL Mol. Microbiol. 13:599-608(1994).
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. It also binds to a specific
CC site in cer locus. Thus it is essential for cer-mediated site-specific
CC recombination in ColE1. It is necessary for monomerization of the
CC plasmid ColE1.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
CC -!- SUBUNIT: Homohexamer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the ArgR family. {ECO:0000305}.
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DR EMBL; X13968; CAA32148.1; -; Genomic_DNA.
DR EMBL; M17532; AAA23486.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58039.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76269.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77280.1; -; Genomic_DNA.
DR PIR; A33888; A33888.
DR RefSeq; NP_417704.1; NC_000913.3.
DR RefSeq; WP_001257846.1; NZ_STEB01000012.1.
DR PDB; 1AOY; NMR; -; A=1-78.
DR PDB; 1XXA; X-ray; 2.20 A; A/B/C/D/E/F=80-156.
DR PDB; 1XXB; X-ray; 2.60 A; A/B/C/D/E/F=80-156.
DR PDB; 1XXC; X-ray; 2.80 A; A/B/C/D/E/F=80-156.
DR PDBsum; 1AOY; -.
DR PDBsum; 1XXA; -.
DR PDBsum; 1XXB; -.
DR PDBsum; 1XXC; -.
DR AlphaFoldDB; P0A6D0; -.
DR SMR; P0A6D0; -.
DR BioGRID; 4259436; 24.
DR DIP; DIP-47999N; -.
DR IntAct; P0A6D0; 5.
DR STRING; 511145.b3237; -.
DR jPOST; P0A6D0; -.
DR PaxDb; P0A6D0; -.
DR PRIDE; P0A6D0; -.
DR EnsemblBacteria; AAC76269; AAC76269; b3237.
DR EnsemblBacteria; BAE77280; BAE77280; BAE77280.
DR GeneID; 66672867; -.
DR GeneID; 947861; -.
DR KEGG; ecj:JW3206; -.
DR KEGG; eco:b3237; -.
DR PATRIC; fig|1411691.4.peg.3491; -.
DR EchoBASE; EB0068; -.
DR eggNOG; COG1438; Bacteria.
DR HOGENOM; CLU_097103_2_0_6; -.
DR InParanoid; P0A6D0; -.
DR OMA; MVYCLPP; -.
DR PhylomeDB; P0A6D0; -.
DR BioCyc; EcoCyc:PD00194; -.
DR UniPathway; UPA00068; -.
DR EvolutionaryTrace; P0A6D0; -.
DR PRO; PR:P0A6D0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IDA:EcoCyc.
DR GO; GO:0034618; F:arginine binding; IDA:EcoCyc.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:2000143; P:negative regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
DR GO; GO:0042150; P:plasmid recombination; IMP:EcoliWiki.
DR GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IMP:EcoCyc.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR GO; GO:1900079; P:regulation of arginine biosynthetic process; IMP:EcoCyc.
DR GO; GO:1900081; P:regulation of arginine catabolic process; IEP:EcoCyc.
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 3D-structure; 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_0000205086"
FT MUTAGEN 21
FT /note="E->K: Increased affinity for ARG box in the presence
FT of arginine."
FT MUTAGEN 44
FT /note="S->F: Defective binding to ARG box."
FT MUTAGEN 47
FT /note="S->L: Defective binding to ARG box."
FT MUTAGEN 76
FT /note="P->L: Increased affinity for ARG box in the absence
FT of arginine."
FT MUTAGEN 105
FT /note="A->V: Defective binding to arginine and to ARG box."
FT MUTAGEN 123
FT /note="G->D: Defective binding to arginine and to ARG box.
FT Forms dimers not hexamers."
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:1AOY"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:1AOY"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:1AOY"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1AOY"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1AOY"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:1XXA"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:1XXA"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1XXA"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:1XXA"
FT TURN 113..120
FT /evidence="ECO:0007829|PDB:1XXA"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:1XXA"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:1XXA"
FT HELIX 141..149
FT /evidence="ECO:0007829|PDB:1XXA"
SQ SEQUENCE 156 AA; 16995 MW; 2F104577EFC46537 CRC64;
MRSSAKQEEL VKAFKALLKE EKFSSQGEIV AALQEQGFDN INQSKVSRML TKFGAVRTRN
AKMEMVYCLP AELGVPTTSS PLKNLVLDID YNDAVVVIHT SPGAAQLIAR LLDSLGKAEG
ILGTIAGDDT IFTTPANGFT VKDLYEAILE LFDQEL
