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ParB N-terminal domain-containing protein
Proteins containing this domain include Escherichia coli plasmid protein ParB and mammalian Sulfiredoxin-1. ParB is involved in chromosome partition. It localises to both poles of the predivisional cell following completion of DNA replication [1]. Sulfiredoxin-1 contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4 [2]. [1]. 12603730. Productive interaction between the chromosome partitioning proteins, ParA and ParB, is required for the progression of the cell cycle in Caulobacter crescentus. Figge RM, Easter J, Gober JW;. Mol Microbiol. 2003;47:1225-1237. [2]. 15448164. Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine. Chang TS, Jeong W, Woo HA, Lee SM, Park S, Rhee SG;. J Biol Chem. 2004;279:50994-51001. (from Pfam)
L-serine kinase SbnI
SbnI is involved in staphyloferrin B biosynthesis.
bifunctional transcriptional regulator/O-phospho-L-serine synthase SbnI
SbnI is a bifunctional protein involved in staphyloferrin B (staphylobactin) biosynthesis in Staphylococcus aureus and other members of the genus. It is a bifunctional protein. The N-terminal region is heme-binding, and loses the ability to bind DNA when heme is bound. Under low iron conditions, the biosynthesis operon for staphyloferrin B, a carboxylate-type siderophore, is derepressed. The C-terminal domain is a kinase that acts on free serine, producing O-phospho-L-serine, which is used as one of the precursors of staphyloferrin B.
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