Putative morphogen; Involved in cell division and chromosome segregation. May influence the activity of FtsZ. Binds DNA, but does not seem to function as a transcription factor ; Belongs to the WhiA family.

Putative acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the arylamine N-acetyltransferase family.

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.

Catabolite repression HPr-like protein; Along with seryl-phosphorylated HPr, phosphorylated Crh is implicated in carbon catabolite repression (CCR) of levanase, inositol dehydrogenase, and beta-xylosidase. Exerts its effect on CCR by interacting with CcpA.

Putative triphosphate pyrophosphate hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the Nudix hydrolase family.

Bifunctional glucosamine-1-phosphate N-acetyltransferase/UDP-N-acetylglucosamine pyrophosphorylase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belon [...]

Serine protein kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the PrkA family.

Peptidoglycan glycosyltransferase (penicillin-binding proteins 1A and 1B); Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits).

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 [...]