HutP

• 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 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 gene

Basic information

• Locus tag: BSU39340

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• UniProt: P10943

• KEGG entry: [3]

• E.C. number:

Expression and regulation

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

• Expression browser: hutP PubMed

• Sigma factor: SigA PubMed

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

• Regulatory mechanism:
  • CcpA: transcription repression PubMed
  • CodY: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)