Inhibitor of the pro-sigma(K) processing machinery; Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB- processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K.

Swarming motility protein; Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro- sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation. Belongs to the peptidase S41A family.

Inhibitor of the pro-sigma(K) processing machinery; Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB- processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K.

Regulatory membrane-associated serine protease; Plays a central role in the sigma-K checkpoint which coordinates gene expression during the later stages of spore formation. The protease is activated by trans cleavage of the zymogen precursor producing SpoIVB-45 kDa. This undergoes further trimming by cis cleavage to form SpoIVB-43 kDa and SpoIVB-42 kDa. The protease then cleaves the C-terminus of the SpoIVFA metalloprotease activating the latter.

Inhibitor of the pro-sigma(K) processing machinery; Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB- processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K.

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.

Inhibitor of the pro-sigma(K) processing machinery; Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB- processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K.

Membrane metalloprotease; Implicated in the coupling of mother cell to forespore gene expression. Required for spore formation. Processes the pro-sigma K factor.

Swarming motility protein; Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro- sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation. Belongs to the peptidase S41A family.

Inhibitor of the pro-sigma(K) processing machinery; Involved in the mediation of the intercompartmental coupling of pro-sigma K processing to events in the forespore. Inhibits SpoIVFB- processing activity until a signal has been received from the forespore. Could inhibit SpoIVFB metalloprotease activity by coordinating a zinc in the SpoIVFB active site, preventing access of a water molecule and the sequence of pro-sigma K, which are necessary for peptide bond hydrolysis to produce sigma-K.

Swarming motility protein; Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro- sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation. Belongs to the peptidase S41A family.

Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane.

Swarming motility protein; Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro- sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation. Belongs to the peptidase S41A family.

Regulatory membrane-associated serine protease; Plays a central role in the sigma-K checkpoint which coordinates gene expression during the later stages of spore formation. The protease is activated by trans cleavage of the zymogen precursor producing SpoIVB-45 kDa. This undergoes further trimming by cis cleavage to form SpoIVB-43 kDa and SpoIVB-42 kDa. The protease then cleaves the C-terminus of the SpoIVFA metalloprotease activating the latter.

Swarming motility protein; Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro- sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation. Belongs to the peptidase S41A 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.

Swarming motility protein; Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro- sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation. Belongs to the peptidase S41A family.

Membrane metalloprotease; Implicated in the coupling of mother cell to forespore gene expression. Required for spore formation. Processes the pro-sigma K factor.

Peptidoglycan O-acetyltransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; enzyme.

Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane.

Protease required for RsiW anti-sigma(W) degradation; Involved in the degradation of anti-sigma-W factor RsiW. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Seems to be responsible for sensing antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. Therefore it is a protease governing regulated intramembrane proteolysis and r [...]

Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane.

Protease required for RsiW anti-sigma(W) degradation; Involved in the degradation of anti-sigma-W factor RsiW. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Seems to be responsible for sensing antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. Therefore it is a protease governing regulated intramembrane proteolysis and r [...]

anti-sigma(W) factor; The anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-W (SigW). Holds SigW, its cognate ECF sigma factor, in an inactive form until released by regulated intramembrane proteolysis (RIP). SigW and RsiW mediate cell response to cell wall stress. RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, PrsW) , then within the membrane itself (site-2 protease, S2P [...]

Protease required for RsiW anti-sigma(W) degradation; Involved in the degradation of anti-sigma-W factor RsiW. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Seems to be responsible for sensing antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. Therefore it is a protease governing regulated intramembrane proteolysis and r [...]

Type I signal peptidase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the peptidase S26 family.

Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane.

Swarming motility protein; Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro- sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation. Belongs to the peptidase S41A family.

Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane.

Peptidoglycan O-acetyltransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; enzyme.

Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane.

Protease required for RsiW anti-sigma(W) degradation; Involved in the degradation of anti-sigma-W factor RsiW. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Seems to be responsible for sensing antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. Therefore it is a protease governing regulated intramembrane proteolysis and r [...]

Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane.

anti-sigma(W) factor; The anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-W (SigW). Holds SigW, its cognate ECF sigma factor, in an inactive form until released by regulated intramembrane proteolysis (RIP). SigW and RsiW mediate cell response to cell wall stress. RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, PrsW) , then within the membrane itself (site-2 protease, S2P [...]

Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane.

Type I signal peptidase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the peptidase S26 family.

Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane.

Regulatory membrane-associated serine protease; Plays a central role in the sigma-K checkpoint which coordinates gene expression during the later stages of spore formation. The protease is activated by trans cleavage of the zymogen precursor producing SpoIVB-45 kDa. This undergoes further trimming by cis cleavage to form SpoIVB-43 kDa and SpoIVB-42 kDa. The protease then cleaves the C-terminus of the SpoIVFA metalloprotease activating the latter.

Regulator of sigma-W protease RasP; Is responsible for site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Can also cleave liberated signal peptides of PenP and Mpr, probably within in the cell membrane.

Membrane metalloprotease; Implicated in the coupling of mother cell to forespore gene expression. Required for spore formation. Processes the pro-sigma K factor.