Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125512211  64 LLLLVSELVTNADRHSH-----GPYVLDLEGSKDQVSVTVYDSSDAVPRRFVKDP---ARIGGHGLEIVHALATEVIVER 135
Cdd:cd16936     1 VELAVSEAVTNAVRHAYrhdgpGPVRLELDLDPDRLRVEVTDSGPGFDPLRPADPdagLREGGRGLALIRALMDEVGYRR 80

                  ....*
gi 2125512211 136 VPVGK 140
Cdd:cd16936    81 TPGGK 85

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125512211  64 LLLLVSELVTNADRHSH-----GPYVLDLEGSKDQVSVTVYDSSDAVPRRFVKDP---ARIGGHGLEIVHALATEVIVER 135
Cdd:cd16936     1 VELAVSEAVTNAVRHAYrhdgpGPVRLELDLDPDRLRVEVTDSGPGFDPLRPADPdagLREGGRGLALIRALMDEVGYRR 80

                  ....*
gi 2125512211 136 VPVGK 140
Cdd:cd16936    81 TPGGK 85

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Erythrobacter litoralis blue light-activated histidine kinase 2; This domain family includes the histidine kinase-like ATPase (HATPase) domain of blue light-activated histidine kinase 2 of Erythrobacter litoralis (EL346). Signaling commonly occurs within HK dimers, however EL346 functions as a monomer. Also included in this family are the HATPase domains of ethanolamine utilization sensory transduction histidine kinase (EutW), whereby regulation of ethanolamine, a carbon and nitrogen source for gut bacteria, results in autophosphorylation and subsequent phosphoryl transfer to a response regulator (EutV) containing an RNA-binding domain. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory PAS sensor domain, while some have an N-terminal histidine kinase domain.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2125512211  56 IDARSRGDLLLLVSELVTNADRHS-----HGPYVLDLEGSKDQVSVTVYDSSDAVPRRFvkDPARIGGHGLEIVHALAT 129
Cdd:cd16951    32 VSSEVATAIGLVVNELLQNALKHAfsdreGGTITIRSVVDGDYLRITVIDDGVGLPQDE--DWPNKGSLGLQIVRSLVE 108

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.

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                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2125512211  64 LLLLVSELVTNADRHSHGPYV-LDLEGSKDQVSVTVYDssDAVPRRfVKDPARIGGHGL 121
Cdd:cd16917     1 LYRIVQEALTNALKHAGASRVrVTLSYTADELTLTVVD--DGVGFD-GPAPPGGGGFGL 56