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
Get the DNA and protein sequences
(Barbe et al., 2009)
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

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)

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

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)