Difference between revisions of "Hbs"
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
− | * '''Localization:''' | + | * '''[[Localization]]:''' |
** associated with the nucleoid in vegetative cells and forespores {{PubMed|9068655,10715001}} | ** associated with the nucleoid in vegetative cells and forespores {{PubMed|9068655,10715001}} | ||
− | ** membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] | + | ** membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] |
=== Database entries === | === Database entries === |
Revision as of 14:29, 30 September 2011
- 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
|
Contents
Categories containing this gene/protein
DNA condensation/ segregation, essential genes, membrane proteins, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU22790
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: DbpA subfamily (according to Swiss-Prot)
- Paralogous protein(s): YonN
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylation on Thr-4 PubMed
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure: 1HUU (Geobacillus stearothermophilus)
- UniProt: P08821
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: hbs PubMed
- Additional information:
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
- Mohamed Marahiel, University of Marburg, Germany Homepage
Your additional remarks
References
Reviews
Original publications
Christopher Collier, Cristina Machón, Geoff S Briggs, Wiep Klaas Smits, Panos Soultanas
Untwisting of the DNA helix stimulates the endonuclease activity of Bacillus subtilis Nth at AP sites.
Nucleic Acids Res: 2012, 40(2);739-50
[PubMed:21954439]
[WorldCat.org]
[DOI]
(I p)
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)