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PROSITE documentation PDOC51740

SpoVT-AbrB domain profile





Description

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 β strands and one α helix and can be described as a pair of β hairpins linked by the α helix (see <PDB:1YSF>) [1,2].

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

Last update:

December 2014 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

SPOVT_ABRB, PS51740; SpoVT-AbrB domain profile  (MATRIX)


References

1AuthorsBobay B.G. Andreeva A. Mueller G.A. Cavanagh J. Murzin A.G.
TitleRevised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins.
SourceFEBS Lett. 579:5669-5674(2005).
PubMed ID16223496
DOI10.1016/j.febslet.2005.09.045

2AuthorsColes M. Djuranovic S. Soeding J. Frickey T. Koretke K. Truffault V. Martin J. Lupas A.N.
TitleAbrB-like transcription factors assume a swapped hairpin fold that is evolutionarily related to double-psi beta barrels.
SourceStructure 13:919-928(2005).
PubMed ID15939023
DOI10.1016/j.str.2005.03.017



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