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Protein

Arginine repressor

Gene

argR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Pathwayi: L-arginine biosynthesis

This protein regulates the pathway L-arginine biosynthesis, which is part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

  • arginine biosynthetic process Source: UniProtKB-UniPathway
  • negative regulation of DNA-templated transcription, initiation Source: EcoCyc
  • plasmid recombination Source: EcoliWiki
  • protein oligomerization Source: InterPro
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis, DNA recombination, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:PD00194.
ECOL316407:JW3206-MONOMER.
UniPathwayiUPA00068.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine repressor
Gene namesi
Name:argR
Synonyms:xerA
Ordered Locus Names:b3237, JW3206
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10070. argR.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211E → K: Increased affinity for ARG box in the presence of arginine.
Mutagenesisi44 – 441S → F: Defective binding to ARG box.
Mutagenesisi47 – 471S → L: Defective binding to ARG box.
Mutagenesisi76 – 761P → L: Increased affinity for ARG box in the absence of arginine.
Mutagenesisi105 – 1051A → V: Defective binding to arginine and to ARG box.
Mutagenesisi123 – 1231G → D: Defective binding to arginine and to ARG box. Forms dimers not hexamers.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 156156Arginine repressorPRO_0000205086Add
BLAST

Proteomic databases

EPDiP0A6D0.
PaxDbiP0A6D0.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

BioGridi4259436. 5 interactions.
DIPiDIP-47999N.
IntActiP0A6D0. 5 interactions.
MINTiMINT-1252219.
STRINGi511145.b3237.

Structurei

Secondary structure

1
156
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 1910Combined sources
Helixi26 – 3611Combined sources
Helixi43 – 5311Combined sources
Beta strandi56 – 594Combined sources
Beta strandi65 – 684Combined sources
Beta strandi85 – 917Combined sources
Beta strandi96 – 1016Combined sources
Turni102 – 1043Combined sources
Helixi105 – 1128Combined sources
Turni113 – 1208Combined sources
Beta strandi121 – 1266Combined sources
Beta strandi128 – 1358Combined sources
Helixi141 – 1499Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0A6D0.
SMRiP0A6D0. Positions 1-153.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6D0.

Family & Domainsi

Sequence similaritiesi

Belongs to the ArgR family.Curated

Phylogenomic databases

eggNOGiENOG410682Y. Bacteria.
COG1438. LUCA.
HOGENOMiHOG000242730.
InParanoidiP0A6D0.
KOiK03402.
OMAiLNQERFG.
OrthoDBiEOG6Z9B6J.
PhylomeDBiP0A6D0.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.1360.40. 1 hit.
HAMAPiMF_00173. Arg_repressor.
InterProiIPR001669. Arg_repress.
IPR020899. Arg_repress_C.
IPR024946. Arg_repress_C-like.
IPR020900. Arg_repress_DNA-bd.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01316. Arg_repressor. 1 hit.
PF02863. Arg_repressor_C. 1 hit.
[Graphical view]
PRINTSiPR01467. ARGREPRESSOR.
ProDomiPD007402. Arg_repress. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55252. SSF55252. 1 hit.
TIGRFAMsiTIGR01529. argR_whole. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A6D0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSSAKQEEL VKAFKALLKE EKFSSQGEIV AALQEQGFDN INQSKVSRML
60 70 80 90 100
TKFGAVRTRN AKMEMVYCLP AELGVPTTSS PLKNLVLDID YNDAVVVIHT
110 120 130 140 150
SPGAAQLIAR LLDSLGKAEG ILGTIAGDDT IFTTPANGFT VKDLYEAILE

LFDQEL
Length:156
Mass (Da):16,995
Last modified:June 7, 2005 - v1
Checksum:i2F104577EFC46537
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA33888.
RefSeqiNP_417704.1. NC_000913.3.
WP_001257846.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76269; AAC76269; b3237.
BAE77280; BAE77280; BAE77280.
GeneIDi947861.
KEGGiecj:JW3206.
eco:b3237.
PATRICi32121900. VBIEscCol129921_3334.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA33888.
RefSeqiNP_417704.1. NC_000913.3.
WP_001257846.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP0A6D0.
SMRiP0A6D0. Positions 1-153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259436. 5 interactions.
DIPiDIP-47999N.
IntActiP0A6D0. 5 interactions.
MINTiMINT-1252219.
STRINGi511145.b3237.

Proteomic databases

EPDiP0A6D0.
PaxDbiP0A6D0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76269; AAC76269; b3237.
BAE77280; BAE77280; BAE77280.
GeneIDi947861.
KEGGiecj:JW3206.
eco:b3237.
PATRICi32121900. VBIEscCol129921_3334.

Organism-specific databases

EchoBASEiEB0068.
EcoGeneiEG10070. argR.

Phylogenomic databases

eggNOGiENOG410682Y. Bacteria.
COG1438. LUCA.
HOGENOMiHOG000242730.
InParanoidiP0A6D0.
KOiK03402.
OMAiLNQERFG.
OrthoDBiEOG6Z9B6J.
PhylomeDBiP0A6D0.

Enzyme and pathway databases

UniPathwayiUPA00068.
BioCyciEcoCyc:PD00194.
ECOL316407:JW3206-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A6D0.
PROiP0A6D0.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.1360.40. 1 hit.
HAMAPiMF_00173. Arg_repressor.
InterProiIPR001669. Arg_repress.
IPR020899. Arg_repress_C.
IPR024946. Arg_repress_C-like.
IPR020900. Arg_repress_DNA-bd.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01316. Arg_repressor. 1 hit.
PF02863. Arg_repressor_C. 1 hit.
[Graphical view]
PRINTSiPR01467. ARGREPRESSOR.
ProDomiPD007402. Arg_repress. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55252. SSF55252. 1 hit.
TIGRFAMsiTIGR01529. argR_whole. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  6. "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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-78.
  7. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 80-156.
  8. Cited for: IDENTIFICATION OF DNA-BINDING DOMAIN.
  9. "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] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  10. "Mutational analysis of the arginine repressor of Escherichia coli."
    Tian G., Maas W.K.
    Mol. Microbiol. 13:599-608(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.

Entry informationi

Entry nameiARGR_ECOLI
AccessioniPrimary (citable) accession number: P0A6D0
Secondary accession number(s): P15282, Q2M8X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: March 16, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.