|PROSITE documentation PDOC00602 [for PROSITE entry PS50935]|
The Escherichia coli single-strand binding protein  (gene ssb), also known as the helix-destabilizing protein, is a protein of 177 amino acids. It binds tightly, as a homotetramer, to single-stranded DNA (ss-DNA) and plays an important role in DNA replication, recombination and repair.
Closely related variants of SSB are encoded in the genome of a variety of large self-transmissible plasmids. SSB has also been characterized in bacteria such as Proteus mirabilis or Serratia marcescens.
Eukaryotic mitochondrial proteins that bind ss-DNA and are probably involved in mitochondrial DNA replication are structurally and evolutionary related to prokaryotic SSB. Proteins currently known to belong to this subfamily are listed below :
The SSB domain is a module of about 100 amino acids that is found in the N-terminal part of bacterial SSB proteins. It possesses conserved residues that are responsible for binding to ssDNA, tetramerization and stabilization of the monomer fold .
The profile we developed covers the entire SSB domain.Last update:
October 2003 / Patterns removed, profile added and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Meyer R.R., Laine P.S.|
|Title||The single-stranded DNA-binding protein of Escherichia coli.|
|Source||Microbiol. Rev. 54:342-380(1990).|
|2||Authors||Stroumbakis N.D., Li Z., Tolias P.P.|
|Title||RNA- and single-stranded DNA-binding (SSB) proteins expressed during Drosophila melanogaster oogenesis: a homolog of bacterial and eukaryotic mitochondrial SSBs.|
|3||Authors||Dabrowski S., Olszewski M., Piatek R., Brillowska-Dabrowska A., Konopa G., Kur J.|
|Title||Identification and characterization of single-stranded-DNA-binding proteins from Thermus thermophilus and Thermus aquaticus - new arrangement of binding domains.|