|PROSITE documentation PDOC50801|
The STAS domain is found in the C-terminal cytoplasmic part of anion transporters from eukaryotes and many bacteria, as well as in the bacterial anti-sigma-factor antagonists (ASAs). It was named STAS after sulfate transporters and anti-sigma-factor antagonist .
Malfunctions in members of the SLC26A family of anion transporters are involved in three human diseases: diastrophic dysplasia/achondrogenesis type 1B (DTDST), Pendred's syndrome (PDS) and congenital chloride diarrhea (CLD). These proteins contain 12 transmembrane helices followed by a cytoplasmic STAS domain at the C-terminus. The importance of the STAS domain in these transporters is illustrated by the fact that a number of mutations in PDS and DTDST map to it .
The activity of bacterial sigma transcription factors is controlled by a regulatory cascade involving an anti-sigma-factor, the ASA and a phosphatase. The antisigma-factor binds to sigma and holds it in an inactive complex. The ASA can also interact with the anti-sigma-factor, allowing the release of the active sigma factor. As the anti-sigma-factor is a protein kinase, it can phosphorylate the anti-sigma antagonist on a conserved serine residue of the STAS domain. This phosphorylation inactivates the ASA that can be reactivated through dephosphorylation by a phosphatase [1,2]. The STAS domain of the ASA SpoIIAA binds GTP and ATP and possesses a weak NTPase activity. Strong sequence conservation suggests that the STAS domain could possess general NTP-binding activity and it has been proposed that the NTPs are likely to elicit specific conformational changes in the STAS domain through binding and/or hydrolysis .
Resolution of the solution structure of the ASA SpoIIAA from Bacillus subtilis (see <PDB:1AUZ>) has shown that the STAS domain consists of a four-stranded β-sheet and four α helices. The STAS domain forms a characteristic α-helical handle-like structure [1,3].
Some proteins known to contain a STAS domain are listed below:
The profile we developed covers the entire STAS domain.Last update:
April 2002 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Aravind L. Koonin E.V.|
|Title||The STAS domain - a link between anion transporters and antisigma-factor antagonists.|
|Source||Curr. Biol. 10:R53-R55(2000).|
|2||Authors||Feucht A. Daniel R.A. Errington J.|
|Title||Characterization of a morphological checkpoint coupling cell-specific transcription to septation in Bacillus subtilis.|
|Source||Mol. Microbiol. 33:1015-1026(1999).|
|3||Authors||Kovacs H. Comfort D. Lord M. Campbell I.D. Yudkin M.D.|
|Title||Solution structure of SpoIIAA, a phosphorylatable component of the system that regulates transcription factor sigmaF of Bacillus subtilis.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 95:5067-5071(1998).|