Difference between revisions of "Hbs"
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===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
| − | essential | + | essential {{PubMed|12682299,1382620}} |
=== Database entries === | === Database entries === | ||
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=== Additional information=== | === Additional information=== | ||
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* '''Interactions:''' | * '''Interactions:''' | ||
| − | * '''Localization:''' | + | * '''Localization:''' |
| + | ** associated with the nucleoid in vegetative cells and forespores {{PubMed|9068655,10715001}} | ||
| + | ** membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed] | ||
=== Database entries === | === Database entries === | ||
| Line 140: | Line 140: | ||
<pubmed>11931565,</pubmed> | <pubmed>11931565,</pubmed> | ||
==Original publications== | ==Original publications== | ||
| − | <pubmed>1382620,1902464,10715001,9068655,9894920,16267290, 19458035, 19210617, 18763711, 17218307 </pubmed> | + | <pubmed>1382620, 1902464,10715001,9068655,9894920,16267290, 19458035, 19210617, 18763711, 17218307 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 14:25, 4 May 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):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylation on Thr-4 PubMed
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
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
Your additional remarks
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)
