HutP

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  • Description: transcriptional antiterminator of the hut operon

Gene name hutP
Synonyms hutP1
Essential no
Product transcriptional antiterminator
Function regulation of histidine utilization
Gene expression levels in SubtiExpress: hutP
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 yxzL, hutH
Sequences Protein DNA DNA_with_flanks
Genetic context
HutP context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
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Categories containing this gene/protein

utilization of amino acids, transcription factors and their control, RNA binding regulators

This gene is a member of the following regulons

CcpA regulon, CodY regulon

The HutP regulon: hutH-hutU-hutI-hutG-hutM

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:

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


Original publications

Balasundaresan Dhakshnamoorthy, Hiroshi Mizuno, Penmetcha K R Kumar
Alternative binding modes of l-histidine guided by metal ions for the activation of the antiterminator protein HutP of Bacillus subtilis.
J Struct Biol: 2013, 183(3);512-518
[PubMed:23748184] [WorldCat.org] [DOI] (I p)

Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538] [WorldCat.org] [DOI] (I e)

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)

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)

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)