UreA

• Description: urease (gamma subunit)
  
  

Gene name	ureA
Synonyms
Essential	no
Product	urease (gamma subunit)
Function	utilization of urea as alternative nitrogen source
Gene expression levels in SubtiExpress: ureA
Interactions involving this protein in SubtInteract: UreA
Metabolic function and regulation of this protein in SubtiPathways: ureA
MW, pI	11 kDa, 4.98
Gene length, protein length	315 bp, 105 aa
Immediate neighbours	ureB, ywzE
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

utilization of nitrogen sources other than amino acids

This gene is a member of the following regulons

CodY regulon, GlnR regulon, PucR regulon, SigH regulon, TnrA regulon

The gene

Basic information

• Locus tag: BSU36660

Database entries

• BsubCyc: BSU36660

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Urea + H₂O = CO₂ + 2 NH₃ (according to Swiss-Prot)

• Protein family: urease gamma subunit family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • UreA-UreB-UreC

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU36660

• Structure: 2FVH (from Mycobacterium tuberculosis, 57% identity, 62% similarity)

• UniProt: P75030

• KEGG entry: [3]

• E.C. number: 3.5.1.5

Expression and regulation

• Operon: ureA-ureB-ureC PubMed

• Expression browser: ureA PubMed

• Sigma factor: SigA PubMed, SigH PubMed

• Regulation:
  • induced by nitrogen limitation (GlnR, TnrA) PubMed
  • induced in the presence of purine nucleotides (inducer: allantoin) (PucR) PubMed
  • repressed during growth in the presence of branched chain amino acids (CodY) PubMed

• Regulatory mechanism:
  • GlnR: transcription repression PubMed
  • TnrA: transcription activation PubMed
  • PucR: transcription activation PubMed
  • CodY: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Mark A Farrugia, Lee Macomber, Robert P Hausinger
Biosynthesis of the urease metallocenter.
J Biol Chem: 2013, 288(19);13178-85
[PubMed:23539618] [WorldCat.org] [DOI] (I p)

Stephen W Ragsdale
Nickel-based Enzyme Systems.
J Biol Chem: 2009, 284(28);18571-5
[PubMed:19363030] [WorldCat.org] [DOI] (P p)

Original publications

Boris R Belitsky, Abraham L Sonenshein
Genetic and biochemical analysis of CodY-binding sites in Bacillus subtilis.
J Bacteriol: 2008, 190(4);1224-36
[PubMed:18083814] [WorldCat.org] [DOI] (I p)

Jong Kyong Kim, Scott B Mulrooney, Robert P Hausinger
Biosynthesis of active Bacillus subtilis urease in the absence of known urease accessory proteins.
J Bacteriol: 2005, 187(20);7150-4
[PubMed:16199586] [WorldCat.org] [DOI] (P p)

Virginie Molle, Yoshiko Nakaura, Robert P Shivers, Hirotake Yamaguchi, Richard Losick, Yasutaro Fujita, Abraham L Sonenshein
Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis.
J Bacteriol: 2003, 185(6);1911-22
[PubMed:12618455] [WorldCat.org] [DOI] (P p)

Jaclyn L Brandenburg, Lewis V Wray, Lars Beier, Hanne Jarmer, Hans H Saxild, Susan H Fisher
Roles of PucR, GlnR, and TnrA in regulating expression of the Bacillus subtilis ure P3 promoter.
J Bacteriol: 2002, 184(21);6060-4
[PubMed:12374841] [WorldCat.org] [DOI] (P p)

L V Wray, A E Ferson, S H Fisher
Expression of the Bacillus subtilis ureABC operon is controlled by multiple regulatory factors including CodY, GlnR, TnrA, and Spo0H.
J Bacteriol: 1997, 179(17);5494-501
[PubMed:9287005] [WorldCat.org] [DOI] (P p)

M R Atkinson, S H Fisher
Identification of genes and gene products whose expression is activated during nitrogen-limited growth in Bacillus subtilis.
J Bacteriol: 1991, 173(1);23-7
[PubMed:1670935] [WorldCat.org] [DOI] (P p)