Hbs

• Description: non-specific DNA-binding protein Hbsu
  
  

Gene name	hbs
Synonyms	dbpA
Essential	yes PubMed
Product	non-specific DNA-binding protein Hbsu
Function	DNA packaging, function of the signal recognition complex
MW, pI	9 kDa, 9.501
Gene length, protein length	276 bp, 92 aa
Immediate neighbours	folE, spoIVA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

DNA condensation/ segregation, essential genes, membrane proteins, phosphoproteins

This gene is a member of the following regulons

LexA regulon, SigH regulon

The gene

Basic information

• Locus tag: BSU22790

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: DbpA subfamily (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylation on Thr-4 PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: cytoplasm (according to Swiss-Prot), membrane associated PubMed

Database entries

• Structure: 1HUU (Geobacillus stearothermophilus)

• UniProt: P08821

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: hbs PubMed

• Sigma factor: SigA PubMed, SigH PubMed

• Regulation:
  • induced by DNA damage (LexA) PubMed

• Regulatory mechanism:
  • LexA: transcription repression PubMed

• Additional information:
  • mRNA is protected from degradation by RnjA by initiating ribosomes PubMed
  • Hbs is present with about 50,000 copies per genome in vegetative cells and spores, it is one of the most abundant proteins in B. subtilis PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Ciaran Condon, IBPC, Paris, France Homepage

References

Reviews

Wolfgang Klein, Mohamed A Marahiel
Structure-function relationship and regulation of two Bacillus subtilis DNA-binding proteins, HBsu and AbrB.
J Mol Microbiol Biotechnol: 2002, 4(3);323-9
[PubMed:11931565] [WorldCat.org] (P p)

Original publications

Roula Daou-Chabo, Ciarán Condon
RNase J1 endonuclease activity as a probe of RNA secondary structure.
RNA: 2009, 15(7);1417-25
[PubMed:19458035] [WorldCat.org] [DOI] (I p)

Roula Daou-Chabo, Nathalie Mathy, Lionel Bénard, Ciarán Condon
Ribosomes initiating translation of the hbs mRNA protect it from 5'-to-3' exoribonucleolytic degradation by RNase J1.
Mol Microbiol: 2009, 71(6);1538-50
[PubMed:19210617] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Nora Au, Elke Kuester-Schoeck, Veena Mandava, Laura E Bothwell, Susan P Canny, Karen Chachu, Sierra A Colavito, Shakierah N Fuller, Eli S Groban, Laura A Hensley, Theresa C O'Brien, Amish Shah, Jessica T Tierney, Louise L Tomm, Thomas M O'Gara, Alexi I Goranov, Alan D Grossman, Charles M Lovett
Genetic composition of the Bacillus subtilis SOS system.
J Bacteriol: 2005, 187(22);7655-66
[PubMed:16267290] [WorldCat.org] [DOI] (P p)

M A Ross, P Setlow
The Bacillus subtilis HBsu protein modifies the effects of alpha/beta-type, small acid-soluble spore proteins on DNA.
J Bacteriol: 2000, 182(7);1942-8
[PubMed:10715001] [WorldCat.org] [DOI] (P p)

P Köhler, M A Marahiel
Mutational analysis of the nucleoid-associated protein HBsu of Bacillus subtilis.
Mol Gen Genet: 1998, 260(5);487-91
[PubMed:9894920] [WorldCat.org] [DOI] (P p)

P Köhler, M A Marahiel
Association of the histone-like protein HBsu with the nucleoid of Bacillus subtilis.
J Bacteriol: 1997, 179(6);2060-4
[PubMed:9068655] [WorldCat.org] [DOI] (P p)

B Micka, M A Marahiel
The DNA-binding protein HBsu is essential for normal growth and development in Bacillus subtilis.
Biochimie: 1992, 74(7-8);641-50
[PubMed:1382620] [WorldCat.org] [DOI] (P p)

B Micka, N Groch, U Heinemann, M A Marahiel
Molecular cloning, nucleotide sequence, and characterization of the Bacillus subtilis gene encoding the DNA-binding protein HBsu.
J Bacteriol: 1991, 173(10);3191-8
[PubMed:1902464] [WorldCat.org] [DOI] (P p)