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Reviewed, UniProtKB/Swiss-Prot P17893 (ARGR_BACSU)

Last modified November 4, 2008. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

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Names and origin

Protein namesRecommended name:
    Arginine repressor
Alternative name(s):
    Arginine hydroxamate resistance protein
Gene names
Name: argR
Synonyms: ahrC
Ordered Locus Names: BSU24250
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

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

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General annotation (Comments)

Function

Represses the synthesis of biosynthetic enzymes and activates the arginine catabolism. Controls the transcription of the two operons rocABC and rocDEF.

Pathway

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

Amino-acid degradation; L-arginine degradation via ADI pathway.

Subunit structure

Homohexamer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the argR family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 149149Arginine repressor
PRO_0000205072

Secondary structure

1 ....................... 149
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P17893-1 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 3608F3B023FCC293

FASTA14916,832
        10         20         30         40         50         60 
MNKGQRHIKI REIITSNEIE TQDELVDMLK QDGYKVTQAT VSRDIKELHL VKVPTNNGSY 

        70         80         90        100        110        120 
KYSLPADQRF NPLSKLKRAL MDAFVKIDSA SHMIVLKTMP GNAQAIGALM DNLDWDEMMG 

       130        140 
TICGDDTILI ICRTPEDTEG VKNRLLELL

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References

« Hide 'large scale' references
[1]"Nucleotide sequence of a Bacillus subtilis arginine regulatory gene and homology of its product to the Escherichia coli arginine repressor."
North A.K., Smith M.C.M., Baumberg S.
Gene 80:29-38(1989) [PubMed: 2507400] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
Microbiology 142:3103-3111(1996) [PubMed: 8969508] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / JH642.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"Characterization of the spoIVB and recN loci of Bacillus subtilis."
van Hoy B.E., Hoch J.A.
J. Bacteriol. 172:1306-1311(1990) [PubMed: 2106508] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-149.
[5]"Purification and initial characterization of AhrC: the regulator of arginine metabolism genes in Bacillus subtilis."
Czaplewski L.G., North A.K., Smith M.C.M., Baumberg S., Stockley P.G.
Mol. Microbiol. 6:267-275(1992) [PubMed: 1312212] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-30.
[6]"The structure of AhrC, the arginine repressor/activator protein from Bacillus subtilis."
Dennis C.A., Glykos N.M., Parsons M.R., Phillips S.E.
Acta Crystallogr. D 58:421-430(2002) [PubMed: 11856827] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

M27869 Genomic DNA. Translation: AAA22208.1.
D84432 Genomic DNA. Translation: BAA12578.1.
Z99116 Genomic DNA. Translation: CAB14356.1.
M30297 Genomic DNA. Translation: AAA22690.1.
PIRJS0275.
RefSeqNP_390305.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1F9NX-ray2.70A/B/C/D/E/F1-149[»]
2P5KX-ray1.00A1-64[»]
2P5LX-ray2.85C/D/G/H1-64[»]
2P5MX-ray1.95A/B/C68-149[»]
ModBaseSearch...

Genome annotation databases

GeneID938653.
GenomeReviewsGene locus BSU24250 in contig AL009126_GR.
KEGGbsu:BSU24250.
NMPDRfig|224308.1.peg.2429.

Organism-specific databases

SubtiListBG10309. argR. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP17893.

Enzyme and pathway databases

BioCycBSUB224308:BSU2423-MON.

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...

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Entry information

Entry nameARGR_BACSU
AccessionPrimary (citable) accession number: P17893
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 4, 2008
This is version 79 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)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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