{PDOC00602}
{PS50935; SSB}
{BEGIN}
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* Single-strand binding (SSB) domain profile *
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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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: October 2003 / Patterns removed, profile added and text revised.

[ 1] Meyer R.R., Laine P.S.
     "The single-stranded DNA-binding protein of Escherichia coli."
     Microbiol. Rev. 54:342-380(1990).
     PubMed=2087220
[ 2] Stroumbakis N.D., Li Z., Tolias P.P.
     "RNA- and single-stranded DNA-binding (SSB) proteins expressed during
     Drosophila melanogaster oogenesis: a homolog of bacterial and
     eukaryotic mitochondrial SSBs."
     Gene 143:171-177(1994).
     PubMed=8206370
[ 3] Dabrowski S., Olszewski M., Piatek R., Brillowska-Dabrowska A.,
     Konopa G., Kur J.
     "Identification and characterization of single-stranded-DNA-binding
     proteins from Thermus thermophilus and Thermus aquaticus - new
     arrangement of binding domains."
     Microbiology 148:3307-3315(2002).
     PubMed=12368464

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