SsbB

• Description: single-strand DNA-binding protein
  
  

Gene name	ssbB
Synonyms	ywpH
Essential	no
Product	single-strand DNA-binding protein
Function	required for efficient genetic transformation
Gene expression levels in SubtiExpress: ssbB
Interactions involving this protein in SubtInteract: SsbB
MW, pI	12 kDa, 6.876
Gene length, protein length	339 bp, 113 aa
Immediate neighbours	glcR, ywpG
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

DNA replication, genetic competence, DNA repair/ recombination, phosphoproteins

This gene is a member of the following regulons

ComK regulon

The gene

Basic information

• Locus tag: BSU36310

Database entries

• BsubCyc: BSU36310

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • binds and protects internalized foreign ssDNA PubMed

• Protein family:

• Paralogous protein(s): SsbA

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-55 PubMed
  • phosphorylated on Tyr by PtkA, dephosphorylated by PtpZ PubMed

• Cofactors:

• Effectors of protein activity: phosphorylation strongly increases DNA-binding activity PubMed

• Interactions:
  • forms tetramers PubMed
  • SsbB-ComFA PubMed
  • SsbB-CoiA PubMed
  • SsbB-DprA PubMed
  • SsbB-RecA PubMed

• Localization:
  • localizes to cell poles in competent cells PubMed
  • localizes to the DNA entry pole during transformation PubMed

Database entries

• BsubCyc: BSU36310

• Structure: 3VDY 3VDY (in complex with ssDNA) PubMed

• UniProt: C0SPB6

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:
  • ssbB PubMed
  • ssbB-glcR PubMed (this is unlikely according to PubMed)

• Expression browser: ssbB PubMed

• Sigma factor:

• Regulation:
  • expressed at the onset of stationary phase PubMed

• Regulatory mechanism:
  • ComK: transcription activation PubMed

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 144 PubMed

Biological materials

• Mutant:

• Expression vector: for expression, purification in E. coli with N-terminal His-tag, pRSETA available in Gerth lab

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Justin S Lenhart, Jeremy W Schroeder, Brian W Walsh, Lyle A Simmons
DNA repair and genome maintenance in Bacillus subtilis.
Microbiol Mol Biol Rev: 2012, 76(3);530-64
[PubMed:22933559] [WorldCat.org] [DOI] (I p)

Original publications

Tribhuwan Yadav, Begoña Carrasco, James Hejna, Yuki Suzuki, Kunio Takeyasu, Juan C Alonso
Bacillus subtilis DprA recruits RecA onto single-stranded DNA and mediates annealing of complementary strands coated by SsbB and SsbA.
J Biol Chem: 2013, 288(31);22437-50
[PubMed:23779106] [WorldCat.org] [DOI] (I p)

Aimee H Marceau, Douglas A Bernstein, Brian W Walsh, Walker Shapiro, Lyle A Simmons, James L Keck
Protein interactions in genome maintenance as novel antibacterial targets.
PLoS One: 2013, 8(3);e58765
[PubMed:23536821] [WorldCat.org] [DOI] (I p)

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

Tribhuwan Yadav, Begoña Carrasco, Angela R Myers, Nicholas P George, James L Keck, Juan C Alonso
Genetic recombination in Bacillus subtilis: a division of labor between two single-strand DNA-binding proteins.
Nucleic Acids Res: 2012, 40(12);5546-59
[PubMed:22373918] [WorldCat.org] [DOI] (I p)

Naomi Kramer, Jeanette Hahn, David Dubnau
Multiple interactions among the competence proteins of Bacillus subtilis.
Mol Microbiol: 2007, 65(2);454-64
[PubMed:17630974] [WorldCat.org] [DOI] (P p)

Ivan Mijakovic, Dina Petranovic, Boris Macek, Tina Cepo, Matthias Mann, Julian Davies, Peter R Jensen, Dusica Vujaklija
Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine.
Nucleic Acids Res: 2006, 34(5);1588-96
[PubMed:16549871] [WorldCat.org] [DOI] (I e)

Jeanette Hahn, Berenike Maier, Bert Jan Haijema, Michael Sheetz, David Dubnau
Transformation proteins and DNA uptake localize to the cell poles in Bacillus subtilis.
Cell: 2005, 122(1);59-71
[PubMed:16009133] [WorldCat.org] [DOI] (P p)

Cordula Lindner, Reindert Nijland, Mariska van Hartskamp, Sierd Bron, Leendert W Hamoen, Oscar P Kuipers
Differential expression of two paralogous genes of Bacillus subtilis encoding single-stranded DNA binding protein.
J Bacteriol: 2004, 186(4);1097-105
[PubMed:14762004] [WorldCat.org] [DOI] (P p)

Mitsuo Ogura, Hirotake Yamaguchi, Kazuo Kobayashi, Naotake Ogasawara, Yasutaro Fujita, Teruo Tanaka
Whole-genome analysis of genes regulated by the Bacillus subtilis competence transcription factor ComK.
J Bacteriol: 2002, 184(9);2344-51
[PubMed:11948146] [WorldCat.org] [DOI] (P p)