Difference between revisions of "UreC"
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* '''Additional information:''' | * '''Additional information:''' | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium): 178 {{PubMed|24696501}} | ||
=Biological materials = | =Biological materials = |
Revision as of 10:03, 17 April 2014
- Description: urease (alpha subunit)
Gene name | ureC |
Synonyms | |
Essential | no |
Product | urease (alpha subunit) |
Function | utilization of urea as alternative nitrogen source |
Gene expression levels in SubtiExpress: ureC | |
Interactions involving this protein in SubtInteract: UreC | |
Metabolic function and regulation of this protein in SubtiPathways: ureC | |
MW, pI | 61 kDa, 5.091 |
Gene length, protein length | 1707 bp, 569 aa |
Immediate neighbours | ywnA, ureB |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
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: BSU36640
Phenotypes of a mutant
Database entries
- BsubCyc: BSU36640
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Urea + H2O = CO2 + 2 NH3 (according to Swiss-Prot)
- Protein family: urease family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s): nickel
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- BsubCyc: BSU36640
- Structure:
- UniProt: P77837
- KEGG entry: [3]
- E.C. number: 3.5.1.5
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
- number of protein molecules per cell (minimal medium with glucose and ammonium): 178 PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
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
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)