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P0A6D0 (ARGR_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginine repressor
Gene names
Name:argR
Synonyms:xerA
Ordered Locus Names:b3237, JW3206
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length156 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Negatively controls the expression of the four operons of arginine biosynthesis in addition to the carAB operon. Predominantly interacts with A/T residues in ARG boxes. It also binds to a specific site in cer locus. Thus it is essential for cer-mediated site-specific recombination in ColE1. It is necessary for monomerization of the plasmid ColE1. HAMAP MF_00173

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis. [regulation] HAMAP MF_00173

Subunit structure

Homohexamer.

Subcellular location

Cytoplasm HAMAP MF_00173.

Sequence similarities

Belongs to the ArgR family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 156156Arginine repressor HAMAP MF_00173
PRO_0000205086

Experimental info

Mutagenesis211E → K: Increased affinity for ARG box in the presence of arginine.
Mutagenesis441S → F: Defective binding to ARG box.
Mutagenesis471S → L: Defective binding to ARG box.
Mutagenesis761P → L: Increased affinity for ARG box in the absence of arginine.
Mutagenesis1051A → V: Defective binding to arginine and to ARG box.
Mutagenesis1231G → D: Defective binding to arginine and to ARG box. Forms dimers not hexamers.

Secondary structure

............... 156
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6D0 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 2F104577EFC46537

FASTA15616,995
        10         20         30         40         50         60 
MRSSAKQEEL VKAFKALLKE EKFSSQGEIV AALQEQGFDN INQSKVSRML TKFGAVRTRN 

        70         80         90        100        110        120 
AKMEMVYCLP AELGVPTTSS PLKNLVLDID YNDAVVVIHT SPGAAQLIAR LLDSLGKAEG 

       130        140        150 
ILGTIAGDDT IFTTPANGFT VKDLYEAILE LFDQEL 

« Hide

References

« Hide 'large scale' references
[1]"The arginine repressor is essential for plasmid-stabilizing site-specific recombination at the ColE1 cer locus."
Stirling C.J., Szatmari G., Stewart G., Smith M.C.M., Sherratt D.J.
EMBO J. 7:4389-4395(1988) [PubMed: 3149585] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Nucleotide sequence of the argR gene of Escherichia coli K-12 and isolation of its product, the arginine repressor."
Lim D., Oppenheim J.D., Eckhardt T., Maas W.K.
Proc. Natl. Acad. Sci. U.S.A. 84:6697-6701(1987) [PubMed: 3116542] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Solution structure of the DNA-binding domain and model for the complex of multifunctional hexameric arginine repressor with DNA."
Seelander-Sunnerhagen M., Nilges M., Otting G., Carey J.
Nat. Struct. Biol. 4:819-826(1997) [PubMed: 9334747] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-78.
[6]"Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli."
van Duyne G.D., Ghosh G., Maas W.K., Sigler P.B.
J. Mol. Biol. 256:377-391(1996) [PubMed: 8594204] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 80-156.
[7]"The DNA-binding domain of the hexameric arginine repressor."
Grandori R., Lavoie T.A., Pflumm M., Tian G., Niersbach H., Maas W.K., Fairman R., Carey J.
J. Mol. Biol. 254:150-162(1995) [PubMed: 7490739] [Abstract]
Cited for: IDENTIFICATION OF DNA-BINDING DOMAIN.
[8]"Mutant Escherichia coli arginine repressor proteins that fail to bind L-arginine, yet retain the ability to bind their normal DNA-binding sites."
Burke M., Merican A.F., Sherratt D.J.
Mol. Microbiol. 13:609-618(1994) [PubMed: 7997173] [Abstract]
Cited for: MUTAGENESIS.
[9]"Mutational analysis of the arginine repressor of Escherichia coli."
Tian G., Maas W.K.
Mol. Microbiol. 13:599-608(1994) [PubMed: 7997172] [Abstract]
Cited for: MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13968 Genomic DNA. Translation: CAA32148.1.
M17532 Genomic DNA. Translation: AAA23486.1.
U18997 Genomic DNA. Translation: AAA58039.1.
U00096 Genomic DNA. Translation: AAC76269.1.
AP009048 Genomic DNA. Translation: BAE77280.1.
PIRA33888.
RefSeqNP_417704.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOYNMR-A1-78[»]
1XXAX-ray2.20A/B/C/D/E/F80-156[»]
1XXBX-ray2.60A/B/C/D/E/F80-156[»]
1XXCX-ray2.80A/B/C/D/E/F80-156[»]
ProteinModelPortalP0A6D0.
SMRP0A6D0. Positions 1-78, 81-153.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-47999N.
IntActP0A6D0. 5 interactions.
MINTMINT-1252219.

2D gel databases

ECO2DBASED014.3. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000005016; EBESCP00000005016; EBESCG00000004094.
EBESCT00000005017; EBESCP00000005017; EBESCG00000004094.
EBESCT00000016350; EBESCP00000015641; EBESCG00000015410.
GeneID947861.
GenomeReviewsGene locus JW3206 in contig AP009048_GR.
Gene locus b3237 in contig U00096_GR.
KEGGecj:JW3206.
eco:b3237.
PATRIC32121900. VBIEscCol129921_3334.

Organism-specific databases

EchoBASEEB0068.
EcoGeneEG10070. argR.

Phylogenomic databases

eggNOGCOG1438.
GeneTreeEBGT00050000010476.
HOGENOMHBG697909.
OMAMVYCLPN.
PhylomeDBP0A6D0.
ProtClustDBPRK05066.

Enzyme and pathway databases

BioCycEcoCyc:PD00194.

Gene expression databases

GenevestigatorP0A6D0.

Family and domain databases

HAMAPMF_00173. Arg_repressor.
[Tree]
InterProIPR001669. Arg_repress.
IPR020899. Arg_repress_C.
IPR020900. Arg_repress_DNA-bd.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KOK03402.
PfamPF01316. Arg_repressor. 1 hit.
PF02863. Arg_repressor_C. 1 hit.
[Graphical view]
PRINTSPR01467. ARGREPRESSOR.
ProDomPD007402. Arg_repress. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF55252. Arg_repress. 1 hit.
TIGRFAMsTIGR01529. ArgR_whole. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARGR_ECOLI
AccessionPrimary (citable) accession number: P0A6D0
Secondary accession number(s): P15282, Q2M8X6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families