SpoIIAA-phosphate serine phosphatase; Normally needed for pro-sigma E processing during sporulation but can be bypassed in vegetative cells. Activates SpoIIAA by dephosphorylation.

Protein kinase; Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan. Another group did not detect phosphorylation of EF-G. PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests [...]

Putative protein kinase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.

Protein tyrosine kinase; May be involved in the regulation of capsular polysaccharide biosynthesis. Autophosphorylates in vitro. Phosphorylates and activates in vitro two UDP-glucose dehydrogenases, YwqF and TuaD, as well as the DNA-binding proteins Ssb and SsbB; Belongs to the CpsD/CapB family.

Protein tyrosine-phosphatase; Dephosphorylates the phosphotyrosine-containing proteins YwqD, YwqF and Ssb.

Chromosome-anchoring protein RacA; Required for the formation of axial filaments and for anchoring the origin regions at the cell poles in sporulating cells, thus ensuring proper chromosome segregation in the prespore. Binds in a dispersed manner throughout the chromosome but preferentially to sites clustered in the origin portion of the chromosome, causing condensation of the chromosome and its remodeling into an elongated, anchored structure; Belongs to the RacA family.

Protein tyrosine kinase; Evidence 2b: Function of strongly homologous gene; enzyme; Belongs to the CpsD/CapB family.

Regulator of SpoIVFB (stage IV sporulation); Implicated in the coupling of mother cell to forespore gene expression. Required for spore formation at 37 degrees Celsius, but not at 30 degrees Celsius. SpoIVFA plays a central role in both maintaining the SpoIVFA/BofA/SpoIVFB complex and anchoring it to the outer forespore membrane. SpoIVFA brings BofA into close proximity to SpoIVFB, allowing BofA to inhibit SpoIVFB. Increased accumulation of SpoIVFA seems to inhibit the activity of SpoIVFB and thus regulates the activation of sigma-K.

Phosphorylated protein phosphatase; Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. Dephosphorylates phosphorylated CgsA, EF-Tu and YezB.