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STAS domain-containing protein
The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C-terminal region of Sulphate transporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding function [1]. [1]. 10662676. The STAS domain - a link between anion transporters and. antisigma-factor antagonists. Aravind L, Koonin EV;. CurrBiol 2000;10:53-55. (from Pfam)
ATP-binding protein
The STAS (after Sulphate Transporter and AntiSigma factor antagonist) domain is found in the C terminal region of Sulphate transporters and bacterial antisigma factor antagonists. It has been suggested that this domain may have a general NTP binding function [2]. [1]. 9560229. Solution structure of SpoIIAA, a phosphorylatable component of. the system that regulates transcription factor sigmaF of. Bacillus subtilis.. Kovacs H, Comfort D, Lord M, Campbell ID, Yudkin MD;. Proc Natl Acad Sci U S A 1998;95:5067-5071.. [2]. 10662676. The STAS domain - a link between anion transporters and. antisigma-factor antagonists. Aravind L, Koonin EV;. CurrBiol 2000;10:53-55. (from Pfam)
anti-sigma factor antagonist
This superfamily includes small (105-125 residue) proteins related to SpoIIAA of Bacillus subtilis, an anti-anti-sigma factor. SpoIIAA can bind to and inhibit the anti-sigma F factor SpoIIAB. Also, it can be phosphorylated by SpoIIAB on a Ser residue at position 59 of the seed alignment. A similar arrangement is inferred for RsbV, an anti-anti-sigma factor for sigma B. This Ser is fairly well conserved within a motif resembling MXS[STA]G[VIL]X[VIL][VILF] among homologous known or predicted anti-anti-sigma factors. Regions similar to SpoIIAA and apparently homologous, but differing considerably near the phosphorlated Ser of SpoIIAA, appear in a single copy in several longer proteins, but score below the trusted cutoff currently set for this superfamily HMM.
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