Difference between revisions of "HutU"

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* '''Additional information:'''
 
* '''Additional information:'''
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** number of protein molecules per cell (complex medium with amino acids, without glucose): 314 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =

Revision as of 10:08, 17 April 2014

  • Description: urocanase

Gene name hutU
Synonyms
Essential no
Product urocanase
Function histidine utilization
Gene expression levels in SubtiExpress: hutU
Metabolic function and regulation of this protein in SubtiPathways:
hutU
MW, pI 60 kDa, 5.664
Gene length, protein length 1656 bp, 552 aa
Immediate neighbours hutH, hutI
Sequences Protein DNA DNA_with_flanks
Genetic context
HutU context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
HutU expression.png



















Categories containing this gene/protein

utilization of amino acids

This gene is a member of the following regulons

CcpA regulon, CodY regulon, HutP regulon

The gene

Basic information

  • Locus tag: BSU39360

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

  • A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate = urocanate + H2O (according to Swiss-Prot)
  • Protein family: urocanase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • repressed by glucose (CcpA) PubMed
    • induced by histidine (HutP) PubMed
    • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
  • Additional information:
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 314 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

Robert A Bender
Regulation of the histidine utilization (hut) system in bacteria.
Microbiol Mol Biol Rev: 2012, 76(3);565-84
[PubMed:22933560] [WorldCat.org] [DOI] (I p)


Original publications

Christopher T Brown, Laura K Fishwick, Binna M Chokshi, Marissa A Cuff, Jay M Jackson, Travis Oglesby, Alison T Rioux, Enrique Rodriguez, Gregory S Stupp, Austin H Trupp, James S Woollcombe-Clarke, Tracy N Wright, William J Zaragoza, Jennifer C Drew, Eric W Triplett, Wayne L Nicholson
Whole-genome sequencing and phenotypic analysis of Bacillus subtilis mutants following evolution under conditions of relaxed selection for sporulation.
Appl Environ Microbiol: 2011, 77(19);6867-77
[PubMed:21821766] [WorldCat.org] [DOI] (I p)

Ken-Ichi Yoshida, Izumi Ishio, Eishi Nagakawa, Yoshiyuki Yamamoto, Mami Yamamoto, Yasutaro Fujita
Systematic study of gene expression and transcription organization in the gntZ-ywaA region of the Bacillus subtilis genome.
Microbiology (Reading): 2000, 146 ( Pt 3);573-579
[PubMed:10746760] [WorldCat.org] [DOI] (P p)

J M Zalieckas, L V Wray, S H Fisher
trans-acting factors affecting carbon catabolite repression of the hut operon in Bacillus subtilis.
J Bacteriol: 1999, 181(9);2883-8
[PubMed:10217782] [WorldCat.org] [DOI] (P p)

S H Fisher, K Rohrer, A E Ferson
Role of CodY in regulation of the Bacillus subtilis hut operon.
J Bacteriol: 1996, 178(13);3779-84
[PubMed:8682780] [WorldCat.org] [DOI] (P p)

L V Wray, S H Fisher
Analysis of Bacillus subtilis hut operon expression indicates that histidine-dependent induction is mediated primarily by transcriptional antitermination and that amino acid repression is mediated by two mechanisms: regulation of transcription initiation and inhibition of histidine transport.
J Bacteriol: 1994, 176(17);5466-73
[PubMed:8071225] [WorldCat.org] [DOI] (P p)