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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)
ParB/RepB/Spo0J family partition protein
ParB/RepB/Spo0J family partition protein may be involved in segregation and competition between plasmids and chromosomes, such as the ParB/SpoJ-type DNA-binding component of the prokaryotic parABS partitioning system
This HMM represents the most well-conserved core of a set of chromosomal and plasmid partition proteins related to ParB, including Spo0J, RepB, and SopB. Spo0J has been shown to bind a specific DNA sequence that, when introduced into a plasmid, can serve as partition site. Study of RepB, which has nicking-closing activity, suggests that it forms a transient protein-DNA covalent intermediate during the strand transfer reaction.
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