{PDOC51740}
{PS51740; SPOVT_ABRB}
{BEGIN}
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* SpoVT-AbrB domain profile *
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The SpoVT-AbrB  domain  is  a  DNA-binding  domain  found  in  a large protein
superfamily [1,2], which includes:

 - Bacterial  antibiotic  resistance  protein  B  (AbrB),  a  transition-state
   regulator.
 - Bacterial  SpoVT,  a  late  sporulation  factor  that  modulates forespore-
   specific sigma G-dependent transcription.
 - Bacterial PrlF, an antitoxin component of a toxin-antitoxin (TA) module.
 - Bacterial transcription factors (antitoxins) of plasmid maintenance systems
   (VapB, MvpT, VppA ,VagC, PemI, MazE, ChpS).
 - Bacterial transcriptional regulator MraZ, involved in the expression of the
   division and  cell wall (dcw) cluster. It contains two copies of the SpoVT-
   AbrB domain.
 - Bacterial endoribonuclease SymE.
 - Sulfolobus solfataricus repressor-like proteins SSo7c3 and SSo7c4.

The SpoVT-AbrB  domain  contains four beta strands and one alpha helix and can
be described  as  a  pair  of  beta  hairpins  linked  by the alpha helix (see
<PDB:1YSF>) [1,2].

The profile we developed covers the entire SpoVT-AbrB domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: December 2014 / First entry.

[ 1] Bobay B.G., Andreeva A., Mueller G.A., Cavanagh J., Murzin A.G.
     "Revised structure of the AbrB N-terminal domain unifies a diverse
     superfamily of  putative DNA-binding proteins."
     FEBS Lett. 579:5669-5674(2005).
     PubMed=16223496; DOI=10.1016/j.febslet.2005.09.045
[ 2] Coles M., Djuranovic S., Soeding J., Frickey T., Koretke K.,
     Truffault V., Martin J., Lupas A.N.
     "AbrB-like transcription factors assume a swapped hairpin fold that is
     evolutionarily related to double-psi beta barrels."
     Structure 13:919-928(2005).
     PubMed=15939023; DOI=10.1016/j.str.2005.03.017

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