Difference between revisions of "SsbA"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 279 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 279 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 2199 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 2199 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 263 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 147 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 3701 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 14:15, 17 April 2014

  • Description: single-strand DNA-binding protein, part of the replisome

Gene name ssbA
Synonyms ssb
Essential yes PubMed
Product single-strand DNA-binding protein
Function DNA replication, DNA repair/ recombination
Gene expression levels in SubtiExpress: ssbA
Interactions involving this protein in SubtInteract: SsbA
MW, pI 18 kDa, 4.822
Gene length, protein length 516 bp, 172 aa
Immediate neighbours rpsR, rpsF
Sequences Protein DNA DNA_with_flanks
Genetic context
Ssb context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SsbA expression.png















Categories containing this gene/protein

DNA replication, DNA repair/ recombination, essential genes, phosphoproteins

This gene is a member of the following regulons

ComK regulon, stringent response

The gene

Basic information

  • Locus tag: BSU40900

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:
    • SsbA inhibits ssDNA phosphorylase activity of PnpA PubMed
    • SsbA co-assembles onto SsbB-coated ssDNA PubMed
  • Protein family:
  • Paralogous protein(s): SsbB

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity: Phosphorylation of Ssb increases binding to single-stranded DNA in vitro almost 200-fold PubMed

Database entries

  • Structure: 3VDY 3VDY (SsbB in complex with ssDNA, 63% identity, 87% similarity) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
    • ComK: transcription activation PubMed
  • Additional information:
    • the mRNA contains a structured motif in the 5' UTR upstream of the rpsF ORF that is bound by RpsF-RpsR heterodimers and may be implicated in autogenous regulation PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 279 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 2199 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 263 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 147 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 3701 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Dusica Vujaklija, Boris Macek
Detecting posttranslational modifications of bacterial SSB proteins.
Methods Mol Biol: 2012, 922;205-18
[PubMed:22976189] [WorldCat.org] [DOI] (I p)

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