PROSITE documentation PDOC51740SpoVT-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
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References
| 1 | Authors | Bobay B.G. Andreeva A. Mueller G.A. Cavanagh J. Murzin A.G. |
| Title | Revised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins. | |
| Source | FEBS Lett. 579:5669-5674(2005). | |
| PubMed ID | 16223496 | |
| DOI | 10.1016/j.febslet.2005.09.045 |
| 2 | Authors | Coles M. Djuranovic S. Soeding J. Frickey T. Koretke K. Truffault V. Martin J. Lupas A.N. |
| Title | AbrB-like transcription factors assume a swapped hairpin fold that is evolutionarily related to double-psi beta barrels. | |
| Source | Structure 13:919-928(2005). | |
| PubMed ID | 15939023 | |
| DOI | 10.1016/j.str.2005.03.017 |
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