Difference between revisions of "HutP"

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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU39340 hutP]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU39340 hutP]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/histidine.html His]'''
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=hutP hutP]'''
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 16 kDa, 6.057   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 16 kDa, 6.057   

Revision as of 12:00, 7 January 2014

  • 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:
hutP
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
500px















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:
    • HutP binds its RNA target to cause antitermination in the presence of histidine PubMed

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

Additional publications: PubMed

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)