Stress responsive alpha-beta barrel (IPR013097)

Short name: Dabb

Overlapping homologous superfamilies

Domain relationships



The stress-response A/B barrel domain is found in a class of stress-response proteins in plants. It is also found in some bacterial fructose-bisphosphate aldolase such as at the C terminus of a fructose 1,6-bisphosphate aldolase from Hydrogenophilus thermoluteolus (Q9ZA13) [PMID: 10705449]. Q93NG5 is found in the pA01 plasmid, which encodes genes for molybdopterin uptake and degradation of plant alkaloid nicotine.

The stress-response A/B barrel domain forms a very stable dimer. This dimer belongs to the superfamily of dimeric alpha+beta barrels in which the two beta-sheets form a beta-barrel. The two molecules in the dimer are related by a 2-fold axis parallel to helix H1 and beta-strands B3 and B4. C-terminal residues extending from the beta4 strand of each monomer wrap around and connect with the beta2 strand and alpha1 helix of the opposing monomer to form the dimer interface [PMID: 15364906, PMID: 15213437, PMID: 15371455].The outer surface of the beta-sheets of the two molecules forms a beta-barrel-like structure defining a central pore.

The function of the stress-response A/B barrel domain is unknown [PMID: 15364906, PMID: 15213437, PMID: 15371455], but it is upregulated in response to salt stress in Populus balsamifera (balsam poplar) [PMID: 14704136].

Some proteins known to contain a stress response A/B barrel domain are listed below:

- Arabidopsis thaliana At3g17210

- Arabidopsis thaliana At5g22580

-Populus tremula stable protein 1 (SP-1)(Populus species), a thermostable stress-responsive protein.

- Pseudomonas hydrogenothermophila fructose 1,6-bisphosphate aldolase (cbbA).

The structure of one of these proteins has been solved (Q9LUV2) and the domain forms an alpha-beta barrel dimer [PMID: 14872131].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles