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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)
DUF3298 domain-containing protein
This family of bacterial protein C-terminal regions is highly conserved but the function is not known. Several members are annotated as being endo-1,4-beta-xylanase-like, but this could not be confirmed, and the structure can be defined as a heat-shock cognate 70kd protein 44kd ATPase. [1]. 17174329. The solution structure of antigen MPT64 from Mycobacterium tuberculosis defines a new family of beta-grasp proteins. Wang Z, Potter BM, Gray AM, Sacksteder KA, Geisbrecht BV, Laity JH;. J Mol Biol. 2007;366:375-381. (from Pfam)
DUF3298 and DUF4163 domain-containing protein
DUF3298 and DUF4163 domain-containing protein similar to Bacillus subtilis anti-sigma-V factor RsiV that negatively regulates SigV activity through direct interaction
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