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PdaC/SigV domain-containing protein
This domain forms an alpha-beta-two layer sandwich. It is found in the Bacillus subtilis proteins anti-sigma-V factor RsiV, which downregulates SigV activity [1], and peptidoglycan-N-acetylmuramic acid deacetylase PdaC, which catalyzes the deacetylation of N-acetylmuramic acid which makes the peptidoglycan resistant to lysosyme [2]. It is found in association with Heat-shock cognate 70kd protein 44kd ATPase, Pfam:PF11738. [1]. 16274938. Identification of sigma(V)-dependent genes of Bacillus subtilis. Zellmeier S, Hofmann C, Thomas S, Wiegert T, Schumann W;. FEMS Microbiol Lett. 2005;253:221-229. [2]. 22277649. Identification and characterization of a novel polysaccharide deacetylase C (PdaC) from Bacillus subtilis. Kobayashi K, Sudiarta IP, Kodama T, Fukushima T, Ara K, Ozaki K, Sekiguchi J;. J Biol Chem. 2012;287:9765-9776. (from Pfam)
polysaccharide deacetylase family protein
This domain is found in polysaccharide deacetylase. This family of polysaccharide deacetylases includes NodB (nodulation protein B from Rhizobium) which is a chitooligosaccharide deacetylase [1]. It also includes chitin deacetylase from yeast [2], and endoxylanases which hydrolyses glucosidic bonds in xylan [3]. [1]. 9163424. Molecular basis of symbiosis between Rhizobium and legumes. Freiberg C, Fellay R, Bairoch A, Broughton WJ, Rosenthal A, Perret X;. Nature 1997;387:394-401. [2]. 9133736. Cloning and expression of two chitin deacetylase genes of Saccharomyces cerevisiae. C. Mishra, C. E. Semino, K. J. McCreath, H. de la Vega, B. J. Jones, C. A. Specht & P. W. Robbins;. Yeast 1996;13:327-336. [3]. 8170399. Evidence for a general role for high-affinity non-catalytic cellulose binding domains in microbial plant cell wall hydrolases. S. J. Millward-Sadler, D. M. Poole, B. Henrissat, G. P. Hazlewood, J. H. Clarke & H. J. Gilbert;. Mol Microbiol 1994;11:375-382. (from Pfam)
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