HutU

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• BsubCyc: BSU39360

• 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:

• Interactions:

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU39360

• Structure: 2FKN

• UniProt: P25503

• KEGG entry: [3]

• E.C. number: 4.2.1.49

Expression and regulation

• Operon: hutP-hutH-hutU-hutI-hutG-hutM PubMed

• Expression browser: hutU PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by glucose (CcpA) PubMed
  • induced by histidine (HutP) PubMed
  • repressed during growth in the presence of branched chain amino acids (CodY) PubMed

• Regulatory mechanism:
  • CcpA: transcription repression PubMed
  • CodY: transcription repression PubMed
  • HutP: transcriptional antitermination at a protein-dependent RNA switch located between hutP and hutH 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:

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)