McsB; Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity.

Class III stress response-related ATPase; Belongs to the ClpA/ClpB family.

ATP-dependent Clp protease-like (class III stress gene) ClpE; Belongs to the ClpA/ClpB family.

Transcriptional regulator; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.

Conserved hypothetical protein YacL; Putative Nucleotide binding protein, PINc.

DNA repair protein RadA; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.

ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. ClpXP1 is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family.

DNA binding protein; Participates in a DNA-damage check-point that is active prior to asymmetric division when DNA is damaged. DisA forms globular foci that rapidly scan along the chromosomes during sporulation, searching for lesions. When a lesion is present, DisA pauses at the lesion site. This triggers a cellular response that culminates in a temporary block in sporulation initiation.

Switch protein/serine kinase and anti-sigma factor (inhibitory sigma-B binding protein); Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B).