Class III stress response-related ATPase, AAA+ superfamily; Competence gene repressor; required for cell growth at high temperature. Negative regulator of comK expression. May interact with MecA to negatively regulate comK; Belongs to the ClpA/ClpB family. ClpC subfamily.

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP 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 transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...]

Class III stress response-related ATPase, AAA+ superfamily; Competence gene repressor; required for cell growth at high temperature. Negative regulator of comK expression. May interact with MecA to negatively regulate comK; Belongs to the ClpA/ClpB family. ClpC subfamily.

Transcriptional regulator; Controls the expression of the cellular protein quality control genes clpC, clpE and clpP, as well as mcsA and mcsB. Acts as a repressor of these class III stress genes by binding to a directly repeated heptanucleotide operator sequence (A/GGTCAAA NAN A/GGTCAAA). After heat shock, CtsR is degraded by the ClpCP and ClpEP proteolytic systems, ensuring the derepression of clpE, clpP and the clpC operon. CtsR negatively autoregulates its own synthesis.

Class III stress response-related ATPase, AAA+ superfamily; Competence gene repressor; required for cell growth at high temperature. Negative regulator of comK expression. May interact with MecA to negatively regulate comK; Belongs to the ClpA/ClpB family. ClpC subfamily.

Activator of protein kinase McsB; Activates the phosphorylation activity of the protein- arginine kinase McsB. Is required for the delocalization of competence proteins from the cell poles.

Class III stress response-related ATPase, AAA+ superfamily; Competence gene repressor; required for cell growth at high temperature. Negative regulator of comK expression. May interact with MecA to negatively regulate comK; Belongs to the ClpA/ClpB family. ClpC subfamily.

Protein tyrosine kinase; Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix- turn-helix domain of CtsR, thereby preventing its binding to DNA and consequently inducing the expression of repressed genes. The transcriptional repressor HrcA, the chaperone GroEL, the unfoldase ClpC, together with several ribosomal subunits, represent other physiological targets of McsB under str [...]

Class III stress response-related ATPase, AAA+ superfamily; Competence gene repressor; required for cell growth at high temperature. Negative regulator of comK expression. May interact with MecA to negatively regulate comK; Belongs to the ClpA/ClpB family. ClpC subfamily.

Protein-tyrosine-phosphatase; Catalyzes the specific dephosphorylation of phosphoarginine residues in a large number of proteins. Counteracts the protein arginine kinase McsB in vivo. Can dephosphorylate CtsR-P; thus, can restore the DNA-binding ability of the CtsR repressor by reversing the McsB-mediated phosphorylation. Is the only active pArg phosphatase present in B.subtilis. Exhibits almost no activity against pSer, pThr, or pTyr peptides. Appears to play a role in B.subtilis stress resistance. Protein arginine phosphorylation has a physiologically important role and is involved i [...]

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP 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 transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...]

Class III stress response-related ATPase, AAA+ superfamily; Competence gene repressor; required for cell growth at high temperature. Negative regulator of comK expression. May interact with MecA to negatively regulate comK; Belongs to the ClpA/ClpB family. ClpC subfamily.

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP 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 transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...]

Transcriptional regulator; Controls the expression of the cellular protein quality control genes clpC, clpE and clpP, as well as mcsA and mcsB. Acts as a repressor of these class III stress genes by binding to a directly repeated heptanucleotide operator sequence (A/GGTCAAA NAN A/GGTCAAA). After heat shock, CtsR is degraded by the ClpCP and ClpEP proteolytic systems, ensuring the derepression of clpE, clpP and the clpC operon. CtsR negatively autoregulates its own synthesis.

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP 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 transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...]

Activator of protein kinase McsB; Activates the phosphorylation activity of the protein- arginine kinase McsB. Is required for the delocalization of competence proteins from the cell poles.

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP 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 transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...]

Protein tyrosine kinase; Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix- turn-helix domain of CtsR, thereby preventing its binding to DNA and consequently inducing the expression of repressed genes. The transcriptional repressor HrcA, the chaperone GroEL, the unfoldase ClpC, together with several ribosomal subunits, represent other physiological targets of McsB under str [...]

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP 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 transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...]

Protein-tyrosine-phosphatase; Catalyzes the specific dephosphorylation of phosphoarginine residues in a large number of proteins. Counteracts the protein arginine kinase McsB in vivo. Can dephosphorylate CtsR-P; thus, can restore the DNA-binding ability of the CtsR repressor by reversing the McsB-mediated phosphorylation. Is the only active pArg phosphatase present in B.subtilis. Exhibits almost no activity against pSer, pThr, or pTyr peptides. Appears to play a role in B.subtilis stress resistance. Protein arginine phosphorylation has a physiologically important role and is involved i [...]

Transcriptional regulator; Controls the expression of the cellular protein quality control genes clpC, clpE and clpP, as well as mcsA and mcsB. Acts as a repressor of these class III stress genes by binding to a directly repeated heptanucleotide operator sequence (A/GGTCAAA NAN A/GGTCAAA). After heat shock, CtsR is degraded by the ClpCP and ClpEP proteolytic systems, ensuring the derepression of clpE, clpP and the clpC operon. CtsR negatively autoregulates its own synthesis.

Class III stress response-related ATPase, AAA+ superfamily; Competence gene repressor; required for cell growth at high temperature. Negative regulator of comK expression. May interact with MecA to negatively regulate comK; Belongs to the ClpA/ClpB family. ClpC subfamily.

Transcriptional regulator; Controls the expression of the cellular protein quality control genes clpC, clpE and clpP, as well as mcsA and mcsB. Acts as a repressor of these class III stress genes by binding to a directly repeated heptanucleotide operator sequence (A/GGTCAAA NAN A/GGTCAAA). After heat shock, CtsR is degraded by the ClpCP and ClpEP proteolytic systems, ensuring the derepression of clpE, clpP and the clpC operon. CtsR negatively autoregulates its own synthesis.

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP 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 transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...]

Transcriptional regulator; Controls the expression of the cellular protein quality control genes clpC, clpE and clpP, as well as mcsA and mcsB. Acts as a repressor of these class III stress genes by binding to a directly repeated heptanucleotide operator sequence (A/GGTCAAA NAN A/GGTCAAA). After heat shock, CtsR is degraded by the ClpCP and ClpEP proteolytic systems, ensuring the derepression of clpE, clpP and the clpC operon. CtsR negatively autoregulates its own synthesis.

Activator of protein kinase McsB; Activates the phosphorylation activity of the protein- arginine kinase McsB. Is required for the delocalization of competence proteins from the cell poles.

Transcriptional regulator; Controls the expression of the cellular protein quality control genes clpC, clpE and clpP, as well as mcsA and mcsB. Acts as a repressor of these class III stress genes by binding to a directly repeated heptanucleotide operator sequence (A/GGTCAAA NAN A/GGTCAAA). After heat shock, CtsR is degraded by the ClpCP and ClpEP proteolytic systems, ensuring the derepression of clpE, clpP and the clpC operon. CtsR negatively autoregulates its own synthesis.

Protein tyrosine kinase; Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix- turn-helix domain of CtsR, thereby preventing its binding to DNA and consequently inducing the expression of repressed genes. The transcriptional repressor HrcA, the chaperone GroEL, the unfoldase ClpC, together with several ribosomal subunits, represent other physiological targets of McsB under str [...]

Transcriptional regulator; Controls the expression of the cellular protein quality control genes clpC, clpE and clpP, as well as mcsA and mcsB. Acts as a repressor of these class III stress genes by binding to a directly repeated heptanucleotide operator sequence (A/GGTCAAA NAN A/GGTCAAA). After heat shock, CtsR is degraded by the ClpCP and ClpEP proteolytic systems, ensuring the derepression of clpE, clpP and the clpC operon. CtsR negatively autoregulates its own synthesis.

Protein-tyrosine-phosphatase; Catalyzes the specific dephosphorylation of phosphoarginine residues in a large number of proteins. Counteracts the protein arginine kinase McsB in vivo. Can dephosphorylate CtsR-P; thus, can restore the DNA-binding ability of the CtsR repressor by reversing the McsB-mediated phosphorylation. Is the only active pArg phosphatase present in B.subtilis. Exhibits almost no activity against pSer, pThr, or pTyr peptides. Appears to play a role in B.subtilis stress resistance. Protein arginine phosphorylation has a physiologically important role and is involved i [...]

Cryptic glutamate dehydrogenase; GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon [...]

Glutamate dehydrogenase; Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression [...]

Activator of protein kinase McsB; Activates the phosphorylation activity of the protein- arginine kinase McsB. Is required for the delocalization of competence proteins from the cell poles.

Class III stress response-related ATPase, AAA+ superfamily; Competence gene repressor; required for cell growth at high temperature. Negative regulator of comK expression. May interact with MecA to negatively regulate comK; Belongs to the ClpA/ClpB family. ClpC subfamily.

Activator of protein kinase McsB; Activates the phosphorylation activity of the protein- arginine kinase McsB. Is required for the delocalization of competence proteins from the cell poles.

ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP 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 transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...]

Activator of protein kinase McsB; Activates the phosphorylation activity of the protein- arginine kinase McsB. Is required for the delocalization of competence proteins from the cell poles.

Transcriptional regulator; Controls the expression of the cellular protein quality control genes clpC, clpE and clpP, as well as mcsA and mcsB. Acts as a repressor of these class III stress genes by binding to a directly repeated heptanucleotide operator sequence (A/GGTCAAA NAN A/GGTCAAA). After heat shock, CtsR is degraded by the ClpCP and ClpEP proteolytic systems, ensuring the derepression of clpE, clpP and the clpC operon. CtsR negatively autoregulates its own synthesis.

Activator of protein kinase McsB; Activates the phosphorylation activity of the protein- arginine kinase McsB. Is required for the delocalization of competence proteins from the cell poles.

Protein tyrosine kinase; Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix- turn-helix domain of CtsR, thereby preventing its binding to DNA and consequently inducing the expression of repressed genes. The transcriptional repressor HrcA, the chaperone GroEL, the unfoldase ClpC, together with several ribosomal subunits, represent other physiological targets of McsB under str [...]