N-acetylmuramoyl-L-alanine amidase; Cleaves the peptide side chain from the N-acetylmuramic acid residues in peptidoglycan. This is a step in the formation of muramic delta-lactam residues in spore cortex.

Exported N-acetylmuramic acid deacetylase; Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N- acetylchitohexaose) as a substrate; Belongs to the polysaccharide deacetylase family.

N-acetylmuramoyl-L-alanine amidase; Cleaves the peptide side chain from the N-acetylmuramic acid residues in peptidoglycan. This is a step in the formation of muramic delta-lactam residues in spore cortex.

Anti-sigma factor (antagonist of sigma(F)) and serine kinase; Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti- anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.

N-acetylmuramoyl-L-alanine amidase; Cleaves the peptide side chain from the N-acetylmuramic acid residues in peptidoglycan. This is a step in the formation of muramic delta-lactam residues in spore cortex.

Morphogenetic stage IV sporulation protein; ATPase. Has a role at an early stage in the morphogenesis of the spore coat outer layers. Its ATP hydrolysis is required for proper assembly of the spore coat. Forms a basement layer around the outside surface of the forespore and self-assembles irreversibly into higher order structures by binding and hydrolyzing ATP thus creating a durable and stable platform upon which thereafter morphogenesis of the coat can take place. Required for proper localization of spore coat protein CotE and sporulation-specific proteins including SpoVM.

N-acetylmuramoyl-L-alanine amidase; Cleaves the peptide side chain from the N-acetylmuramic acid residues in peptidoglycan. This is a step in the formation of muramic delta-lactam residues in spore cortex.

Penicillin-binding protein; Penicillin-binding protein with an unknown catalytic activity. May have a specialized role in the morphogenesis of spore cortex, which is a modified form of peptidoglycan. Pore cortex formation is determined primarily by the mother cell.

N-acetylmuramoyl-L-alanine amidase; Cleaves the peptide side chain from the N-acetylmuramic acid residues in peptidoglycan. This is a step in the formation of muramic delta-lactam residues in spore cortex.

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

Exported N-acetylmuramic acid deacetylase; Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N- acetylchitohexaose) as a substrate; Belongs to the polysaccharide deacetylase family.

N-acetylmuramoyl-L-alanine amidase; Cleaves the peptide side chain from the N-acetylmuramic acid residues in peptidoglycan. This is a step in the formation of muramic delta-lactam residues in spore cortex.

Exported N-acetylmuramic acid deacetylase; Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N- acetylchitohexaose) as a substrate; Belongs to the polysaccharide deacetylase family.

Anti-sigma factor (antagonist of sigma(F)) and serine kinase; Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti- anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.

Exported N-acetylmuramic acid deacetylase; Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N- acetylchitohexaose) as a substrate; Belongs to the polysaccharide deacetylase family.

Morphogenetic stage IV sporulation protein; ATPase. Has a role at an early stage in the morphogenesis of the spore coat outer layers. Its ATP hydrolysis is required for proper assembly of the spore coat. Forms a basement layer around the outside surface of the forespore and self-assembles irreversibly into higher order structures by binding and hydrolyzing ATP thus creating a durable and stable platform upon which thereafter morphogenesis of the coat can take place. Required for proper localization of spore coat protein CotE and sporulation-specific proteins including SpoVM.

Exported N-acetylmuramic acid deacetylase; Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N- acetylchitohexaose) as a substrate; Belongs to the polysaccharide deacetylase family.

Penicillin-binding protein; Penicillin-binding protein with an unknown catalytic activity. May have a specialized role in the morphogenesis of spore cortex, which is a modified form of peptidoglycan. Pore cortex formation is determined primarily by the mother cell.

Exported N-acetylmuramic acid deacetylase; Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N- acetylchitohexaose) as a substrate; Belongs to the polysaccharide deacetylase family.

Small acid-soluble spore protein (alpha-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light.

Exported N-acetylmuramic acid deacetylase; Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N- acetylchitohexaose) as a substrate; Belongs to the polysaccharide deacetylase family.

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

Exported N-acetylmuramic acid deacetylase; Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N- acetylchitohexaose) as a substrate; Belongs to the polysaccharide deacetylase family.

Putative glycosyltransferase associated to biofilm formation; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.

Exported N-acetylmuramic acid deacetylase; Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N- acetylchitohexaose) as a substrate; Belongs to the polysaccharide deacetylase family.

Spore cortex lytic enzyme; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type cp: cell process; Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.

Exported N-acetylmuramic acid deacetylase; Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N- acetylchitohexaose) as a substrate; Belongs to the polysaccharide deacetylase family.

Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.

Exported N-acetylmuramic acid deacetylase; Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N- acetylchitohexaose) as a substrate; Belongs to the polysaccharide deacetylase family.

Putative epimerase modification of peptidoglycan; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the glycosyl hydrolase 18 family.

Anti-sigma factor (antagonist of sigma(F)) and serine kinase; Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti- anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.

N-acetylmuramoyl-L-alanine amidase; Cleaves the peptide side chain from the N-acetylmuramic acid residues in peptidoglycan. This is a step in the formation of muramic delta-lactam residues in spore cortex.

Anti-sigma factor (antagonist of sigma(F)) and serine kinase; Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti- anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.

Exported N-acetylmuramic acid deacetylase; Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N- acetylchitohexaose) as a substrate; Belongs to the polysaccharide deacetylase family.

Anti-sigma factor (antagonist of sigma(F)) and serine kinase; Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti- anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.

Morphogenetic stage IV sporulation protein; ATPase. Has a role at an early stage in the morphogenesis of the spore coat outer layers. Its ATP hydrolysis is required for proper assembly of the spore coat. Forms a basement layer around the outside surface of the forespore and self-assembles irreversibly into higher order structures by binding and hydrolyzing ATP thus creating a durable and stable platform upon which thereafter morphogenesis of the coat can take place. Required for proper localization of spore coat protein CotE and sporulation-specific proteins including SpoVM.

Anti-sigma factor (antagonist of sigma(F)) and serine kinase; Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti- anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.

Small acid-soluble spore protein (alpha-type SASP); SASP are bound to spore DNA. They are double-stranded DNA- binding proteins that cause DNA to change to an a-like conformation. They protect the DNA backbone from chemical and enzymatic cleavage and are thus involved in dormant spore's high resistance to UV light.

Morphogenetic stage IV sporulation protein; ATPase. Has a role at an early stage in the morphogenesis of the spore coat outer layers. Its ATP hydrolysis is required for proper assembly of the spore coat. Forms a basement layer around the outside surface of the forespore and self-assembles irreversibly into higher order structures by binding and hydrolyzing ATP thus creating a durable and stable platform upon which thereafter morphogenesis of the coat can take place. Required for proper localization of spore coat protein CotE and sporulation-specific proteins including SpoVM.

N-acetylmuramoyl-L-alanine amidase; Cleaves the peptide side chain from the N-acetylmuramic acid residues in peptidoglycan. This is a step in the formation of muramic delta-lactam residues in spore cortex.