P0A6D0 (ARGR_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 63.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Arginine repressor | ||||||
| Gene names |
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| Organism | Escherichia coli (strain K12) | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 156 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 | |
| Sequence similarities | Belongs to the ArgR family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Arginine biosynthesis DNA recombination Transcription Transcription regulation |
| Cellular component | Cytoplasm |
| Ligand | DNA-binding |
| Molecular function | Repressor |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW plasmid recombinationInferred from mutant phenotype Ref.1. Source: EcoliWiki transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding transcription factor activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||
Molecule processing | |||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 156 | 156 | Arginine repressor HAMAP MF_00173 | PRO_0000205086 | |||||||||||||||||||
Experimental info | |||||||||||||||||||||||
| Mutagenesis | 21 | 1 | E → K: Increased affinity for ARG box in the presence of arginine. | ||||||||||||||||||||
| Mutagenesis | 44 | 1 | S → F: Defective binding to ARG box. | ||||||||||||||||||||
| Mutagenesis | 47 | 1 | S → L: Defective binding to ARG box. | ||||||||||||||||||||
| Mutagenesis | 76 | 1 | P → L: Increased affinity for ARG box in the absence of arginine. | ||||||||||||||||||||
| Mutagenesis | 105 | 1 | A → V: Defective binding to arginine and to ARG box. | ||||||||||||||||||||
| Mutagenesis | 123 | 1 | G → D: Defective binding to arginine and to ARG box. Forms dimers not hexamers. | ||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||
| Helix | 83 – 85 | 3 | |||||||||||||||||||||
| Beta strand | 96 – 101 | 6 | |||||||||||||||||||||
| Helix | 105 – 112 | 8 | |||||||||||||||||||||
| Helix | 117 – 119 | 3 | |||||||||||||||||||||
| Beta strand | 121 – 126 | 6 | |||||||||||||||||||||
| Beta strand | 128 – 135 | 8 | |||||||||||||||||||||
| Helix | 141 – 151 | 11 | |||||||||||||||||||||
Sequences
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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. | ||||||||||||||||||||||||||||||
| PIR | A33888. | ||||||||||||||||||||||||||||||
| RefSeq | NP_417704.1. NC_000913.2. | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P0A6D0. | ||||||||||||||||||||||||||||||
| SMR | P0A6D0. Positions 1-78, 81-153. | ||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||
| DIP | DIP-47999N. | ||||||||||||||||||||||||||||||
| IntAct | P0A6D0. 5 interactions. | ||||||||||||||||||||||||||||||
| MINT | MINT-1252219. | ||||||||||||||||||||||||||||||
2D gel databases | |||||||||||||||||||||||||||||||
| ECO2DBASE | D014.3. 6TH EDITION. | ||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||
| EnsemblBacteria | EBESCT00000005016; EBESCP00000005016; EBESCG00000004094. EBESCT00000005017; EBESCP00000005017; EBESCG00000004094. EBESCT00000016350; EBESCP00000015641; EBESCG00000015410. | ||||||||||||||||||||||||||||||
| GeneID | 947861. | ||||||||||||||||||||||||||||||
| GenomeReviews | Gene locus JW3206 in contig AP009048_GR. Gene locus b3237 in contig U00096_GR. | ||||||||||||||||||||||||||||||
| KEGG | ecj:JW3206. eco:b3237. | ||||||||||||||||||||||||||||||
| PATRIC | 32121900. VBIEscCol129921_3334. | ||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||
| EchoBASE | EB0068. | ||||||||||||||||||||||||||||||
| EcoGene | EG10070. argR. | ||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||
| eggNOG | COG1438. | ||||||||||||||||||||||||||||||
| GeneTree | EBGT00050000010476. | ||||||||||||||||||||||||||||||
| HOGENOM | HBG697909. | ||||||||||||||||||||||||||||||
| OMA | MVYCLPN. | ||||||||||||||||||||||||||||||
| PhylomeDB | P0A6D0. | ||||||||||||||||||||||||||||||
| ProtClustDB | PRK05066. | ||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||
| BioCyc | EcoCyc:PD00194. | ||||||||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||||||||
| Genevestigator | P0A6D0. | ||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||
| HAMAP | MF_00173. Arg_repressor. [Tree] | ||||||||||||||||||||||||||||||
| InterPro | IPR001669. Arg_repress. IPR020899. Arg_repress_C. IPR020900. Arg_repress_DNA-bd. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view] | ||||||||||||||||||||||||||||||
| Gene3D | G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit. | ||||||||||||||||||||||||||||||
| KO | K03402. | ||||||||||||||||||||||||||||||
| Pfam | PF01316. Arg_repressor. 1 hit. PF02863. Arg_repressor_C. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| PRINTS | PR01467. ARGREPRESSOR. | ||||||||||||||||||||||||||||||
| ProDom | PD007402. Arg_repress. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||||||||||||||||||||
| SUPFAM | SSF55252. Arg_repress. 1 hit. | ||||||||||||||||||||||||||||||
| TIGRFAMs | TIGR01529. ArgR_whole. 1 hit. | ||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||
Entry information
| Entry name | ARGR_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0A6D0 Secondary accession number(s): P15282, Q2M8X6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic 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 |

Clusters with