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Conserved domains on  [gi|1903075913|dbj|GGY34358|]
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ATPase [Streptomyces djakartensis]

Protein Classification

ATP-binding protein( domain architecture ID 10005496)

ATP-binding protein with a histidine kinase-like ATPase domain, similar to serine/threonine-protein kinase BtrW, which phosphorylates and inactivates its specific antagonist protein BtrV and may function as a negative regulator of sigma-B activity

Gene Ontology:  GO:0005524|GO:0016787
PubMed:  16077112|12354223

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
20-143 3.30e-16

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


:

Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 69.94  E-value: 3.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903075913  20 RPRKPAEARRAVERAvaercrATHTPCDVNALSDALLVASELTTNAILHGG-----GVTDFQVDIDGPGVRVSVSDRSDE 94
Cdd:COG2172     7 DLEDLGLARRAVRAL------LRELGLDEDDADDLVLAVSEAVTNAVRHAYggdpdGPVEVELELDPDGLEIEVRDEGPG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1903075913  95 LPVTAPRaDPHGRLRHGGHGWPIVCRLARDVRVSDLPaGGKCITAVVPL 143
Cdd:COG2172    81 FDPEDLP-DPYSTLAEGGRGLFLIRRLMDEVEYESDP-GGTTVRLVKRL 127
 
Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
20-143 3.30e-16

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 69.94  E-value: 3.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903075913  20 RPRKPAEARRAVERAvaercrATHTPCDVNALSDALLVASELTTNAILHGG-----GVTDFQVDIDGPGVRVSVSDRSDE 94
Cdd:COG2172     7 DLEDLGLARRAVRAL------LRELGLDEDDADDLVLAVSEAVTNAVRHAYggdpdGPVEVELELDPDGLEIEVRDEGPG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1903075913  95 LPVTAPRaDPHGRLRHGGHGWPIVCRLARDVRVSDLPaGGKCITAVVPL 143
Cdd:COG2172    81 FDPEDLP-DPYSTLAEGGRGLFLIRRLMDEVEYESDP-GGTTVRLVKRL 127
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 54-141 1.88e-13

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.


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 61.52  E-value: 1.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903075913  54 ALLVASELTTNAILHGGGVT-----DFQVDIDGPGVRVSVSDRSDELPVTAPRaDPHGRLRHGGHGWPIVCRLARDVRVS 128
Cdd:cd16936     1 VELAVSEAVTNAVRHAYRHDgpgpvRLELDLDPDRLRVEVTDSGPGFDPLRPA-DPDAGLREGGRGLALIRALMDEVGYR 79

                          90
                  ....*....|...
gi 1903075913 129 DLPaGGKCITAVV 141
Cdd:cd16936    80 RTP-GGKTVWLEL 91
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 57-143 3.53e-05

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 40.43  E-value: 3.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903075913  57 VASELTTNAILHGGGVTDFQVDIDGPG-VRVSVSDRS-----DELPVTAPRADPHGRLRHGGHGW--PIVCRLAR----D 124
Cdd:pfam02518   9 VLSNLLDNALKHAAKAGEITVTLSEGGeLTLTVEDNGigippEDLPRIFEPFSTADKRGGGGTGLglSIVRKLVEllggT 88

                          90
                  ....*....|....*....
gi 1903075913 125 VRVSDLPAGGKCITAVVPL 143
Cdd:pfam02518  89 ITVESEPGGGTTVTLTLPL 107
 
Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
20-143 3.30e-16

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 69.94  E-value: 3.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903075913  20 RPRKPAEARRAVERAvaercrATHTPCDVNALSDALLVASELTTNAILHGG-----GVTDFQVDIDGPGVRVSVSDRSDE 94
Cdd:COG2172     7 DLEDLGLARRAVRAL------LRELGLDEDDADDLVLAVSEAVTNAVRHAYggdpdGPVEVELELDPDGLEIEVRDEGPG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1903075913  95 LPVTAPRaDPHGRLRHGGHGWPIVCRLARDVRVSDLPaGGKCITAVVPL 143
Cdd:COG2172    81 FDPEDLP-DPYSTLAEGGRGLFLIRRLMDEVEYESDP-GGTTVRLVKRL 127
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 54-141 1.88e-13

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.


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 61.52  E-value: 1.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903075913  54 ALLVASELTTNAILHGGGVT-----DFQVDIDGPGVRVSVSDRSDELPVTAPRaDPHGRLRHGGHGWPIVCRLARDVRVS 128
Cdd:cd16936     1 VELAVSEAVTNAVRHAYRHDgpgpvRLELDLDPDRLRVEVTDSGPGFDPLRPA-DPDAGLREGGRGLALIRALMDEVGYR 79

                          90
                  ....*....|...
gi 1903075913 129 DLPaGGKCITAVV 141
Cdd:cd16936    80 RTP-GGKTVWLEL 91
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 57-143 3.53e-05

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 40.43  E-value: 3.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903075913  57 VASELTTNAILHGGGVTDFQVDIDGPG-VRVSVSDRS-----DELPVTAPRADPHGRLRHGGHGW--PIVCRLAR----D 124
Cdd:pfam02518   9 VLSNLLDNALKHAAKAGEITVTLSEGGeLTLTVEDNGigippEDLPRIFEPFSTADKRGGGGTGLglSIVRKLVEllggT 88

                          90
                  ....*....|....*....
gi 1903075913 125 VRVSDLPAGGKCITAVVPL 143
Cdd:pfam02518  89 ITVESEPGGGTTVTLTLPL 107
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
25-140 7.85e-04

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 37.27  E-value: 7.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903075913  25 AEARRAVERAvaercrATHTPCDVNALSDALLVASELTTNAILHG-----GGVTDFQVDIDGPGVRVSVSDRS---DELP 96
Cdd:pfam13581   9 RAARRVLEAV------LRRAGLPEELLDEVELAVGEACTNAVEHAyregpEGPVEVRLTSDGGGLVVTVADSGppfDPLT 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1903075913  97 VTAPRAD-PHGRLRHGGHGWPIVCRLARDVRVSDLPaGGKCITAV 140
Cdd:pfam13581  83 LPPPDLEePDEDRKEGGRGLALIRGLMDDVEYTRGG-EGNTVRMR 126
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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