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Reviewed, UniProtKB/Swiss-Prot O31408 (ARGR_BACST)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Arginine repressor
Gene names
Name: argR
OrganismBacillus stearothermophilus (Geobacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Regulates arginine biosynthesis genes. HAMAP MF_00173

Pathway

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

Subunit structure

Homohexamer. HAMAP MF_00173

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the argR family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
Transcription
Transcription regulation
   Cellular componentCytoplasm
   LigandDNA-binding
   Molecular functionRepressor
   Technical term3D-structure
Gene Ontology (GO)
   Biological processarginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: HAMAP

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontranscription factor activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 149149Arginine repressor HAMAP MF_00173
PRO_0000205071

Secondary structure

........................... 149
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O31408-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: F15E1ACD89E006E8

FASTA14916,805
        10         20         30         40         50         60 
MNKGQRHIKI REIIMSNDIE TQDELVDRLR EAGFNVTQAT VSRDIKEMQL VKVPMANGRY 

        70         80         90        100        110        120 
KYSLPSDQRF NPLQKLKRAL VDVFIKLDGT GNLLVLRTLP GNAHAIGVLL DNLDWDEIVG 

       130        140 
TICGDDTCLI ICRTPKDAKK VSNQLLSML 

« Hide

References

[1]"The highly thermostable arginine repressor of Bacillus stearothermophilus: gene cloning and repressor-operator interactions."
Dion M., Charlier D.R.M., Wang H., Gigot D., Savchenko A., Hallet J.-N., Glansdorff N., Sakanyan V.
Mol. Microbiol. 25:385-398(1997) [PubMed: 9282750] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NCIB 8224 / CCM 2186.
[2]"Structure of the arginine repressor from Bacillus stearothermophilus."
Ni J., Sakanyan V., Charlier D., Glansdorff N., van Duyne G.D.
Nat. Struct. Biol. 6:427-432(1999) [PubMed: 10331868] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Cross-references

Sequence databases

Y09546 Genomic DNA. Translation: CAA70737.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1B4AX-ray2.50A/B/C/D/E/F2-149[»]
1B4BX-ray2.20A/B/C79-149[»]
ModBaseSearch...

Family and domain databases

HAMAPMF_00173.
[Tree]
InterProIPR001669. Arg_repress.
IPR011991. Wing_hlx_DNA_bd.
[Graphical view]
Gene3DG3DSA:3.30.1360.40. Arg_repress. 1 hit.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
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]
TIGRFAMsTIGR01529. argR_whole. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARGR_BACST
AccessionPrimary (citable) accession number: O31408
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents