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poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB
GHL13 is a family of hypothetical glycoside hydrolases. [1]. 20556855. Gh101 family of glycoside hydrolases: subfamily structure and. evolutionary connections with other families.. Naumoff DG;. J Bioinform Comput Biol. 2010;8:437-451.. [2]. 21954604. [Endo-alpha-1-4-polygalactosaminidases and their homologues:. structure and evolution].. Naumov DG, Stepushchenko OO;. Mol Biol (Mosk). 2011;45:703-714.. [3]. 22295578. [GHL1-GHL15: new families of hypothetical glycoside hydrolases].. Naumov DG;. Mol Biol (Mosk). 2011;45:1073-1083. (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)
Two well-characterized systems produce polysaccharide based on N-acetyl-D-glucosamine in straight chains with beta-1,6 linkages. These are encoded by the icaADBC operon in Staphylococcus species, where the system is designated polysaccharide intercellular adhesin (PIA), and the pgaABCD operon in Gram-negative bacteria such as E. coli. Both systems include a putative polysaccharide deacetylase. The PgaB protein, described here, contains an additional domain lacking from its Gram-positive counterpart IcaB (TIGR03933). Deacetylation by this protein appears necessary to allow export through the porin PgaA
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