Difference between revisions of "HutP"

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(References)
(Original publications)
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<pubmed>17395359 16427271 </pubmed>
 
<pubmed>17395359 16427271 </pubmed>
 
==Original publications==
 
==Original publications==
<pubmed>12903241,16672620,8682780, 8071225 </pubmed>
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<pubmed>12903241,8682780, 8071225 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 19:11, 8 February 2010

  • Description: transcriptional antiterminator of the hut operon

Gene name hutP
Synonyms hutP1
Essential no
Product transcriptional antiterminator
Function regulation of histidine utilization
Metabolic function and regulation of this protein in SubtiPathways:
His
MW, pI 16 kDa, 6.057
Gene length, protein length 453 bp, 151 aa
Immediate neighbours abn2, hutH
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
HutP context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU39340

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: hutP 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:

Database entries

  • Structure: 3BOY (complex bound to the hut mRNA), 1WPT
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

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

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Thirumananseri Kumarevel
Structural insights of HutP-mediated regulation of transcription of the hut operon in Bacillus subtilis.
Biophys Chem: 2007, 128(1);1-12
[PubMed:17395359] [WorldCat.org] [DOI] (P p)

Penmetcha K R Kumar, Thirumananseri Kumarevel, Hiroshi Mizuno
Structural basis of HutP-mediated transcription anti-termination.
Curr Opin Struct Biol: 2006, 16(1);18-26
[PubMed:16427271] [WorldCat.org] [DOI] (P p)

Original publications

M Oda, N Kobayashi, Y Kurusu, M Fujita
Analysis of histidine-dependent antitermination in Bacillus subtilis hut operon.
Nucleic Acids Symp Ser: 2000, (44);5-6
[PubMed:12903241] [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)