PROSITE documentation PDOC00602Single-strand binding (SSB) domain profile
The Escherichia coli single-strand binding protein [1] (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 [2]:
- Mammalian protein Mt-SSB (P16).
- Xenopus Mt-SSBs and Mt-SSBr.
- Drosophila MtSSB.
- Yeast protein RIM1.
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 [3].
The profile we developed covers the entire SSB domain.
Last update:October 2003 / Patterns removed, profile added and text revised.
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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). | |
| PubMed ID | 2087220 |
| 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. | |
| Source | Gene 143:171-177(1994). | |
| PubMed ID | 8206370 |
| 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. | |
| Source | Microbiology 148:3307-3315(2002). | |
| PubMed ID | 12368464 |
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