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Conserved domains on  [gi|1158447249|ref|WP_079022080|]
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MULTISPECIES: ATP-binding protein [Streptomyces]

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];
11-137 1.83e-25

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


:

Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 95.37  E-value: 1.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158447249  11 VELQALPSRIGQIRRIVSAHLRHWQLD-DLVDPVQLGVTELLSNVHRHA---QPDKECTVELELLLDRLTVSVRDNDPRI 86
Cdd:COG2172     2 LSLPADLEDLGLARRAVRALLRELGLDeDDADDLVLAVSEAVTNAVRHAyggDPDGPVEVELELDPDGLEIEVRDEGPGF 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1158447249  87 PVAtesdalDLWDEPDALATSGRGLAIVGALSDSWGVRPRGvSGKTVWFTL 137
Cdd:COG2172    82 DPE------DLPDPYSTLAEGGRGLFLIRRLMDEVEYESDP-GGTTVRLVK 125
 
Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
11-137 1.83e-25

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 95.37  E-value: 1.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158447249  11 VELQALPSRIGQIRRIVSAHLRHWQLD-DLVDPVQLGVTELLSNVHRHA---QPDKECTVELELLLDRLTVSVRDNDPRI 86
Cdd:COG2172     2 LSLPADLEDLGLARRAVRALLRELGLDeDDADDLVLAVSEAVTNAVRHAyggDPDGPVEVELELDPDGLEIEVRDEGPGF 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1158447249  87 PVAtesdalDLWDEPDALATSGRGLAIVGALSDSWGVRPRGvSGKTVWFTL 137
Cdd:COG2172    82 DPE------DLPDPYSTLAEGGRGLFLIRRLMDEVEYESDP-GGTTVRLVK 125
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 43-137 3.94e-20

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: 80.39  E-value: 3.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158447249  43 VQLGVTELLSNVHRHAQ---PDKECTVELELLLDRLTVSVRDNDPRIPVATESDaldlwdePDA-LATSGRGLAIVGALS 118
Cdd:cd16936     1 VELAVSEAVTNAVRHAYrhdGPGPVRLELDLDPDRLRVEVTDSGPGFDPLRPAD-------PDAgLREGGRGLALIRALM 73

                          90
                  ....*....|....*....
gi 1158447249 119 DSWGVRPRGVsGKTVWFTL 137
Cdd:cd16936    74 DEVGYRRTPG-GKTVWLEL 91
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
13-136 1.08e-15

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 70.01  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158447249  13 LQALPSRIGQIRRIVSAHLRHWQLD-DLVDPVQLGVTELLSNVHRHAQ---PDKECTVELELLLDRLTVSVRDNDPRIPV 88
Cdd:pfam13581   1 FPADPEQLRAARRVLEAVLRRAGLPeELLDEVELAVGEACTNAVEHAYregPEGPVEVRLTSDGGGLVVTVADSGPPFDP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1158447249  89 ATESDALDLWDEPDaLATSGRGLAIVGALSDSWGVRPRGVsGKTVWFT 136
Cdd:pfam13581  81 LTLPPPDLEEPDED-RKEGGRGLALIRGLMDDVEYTRGGE-GNTVRMR 126
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 41-137 8.24e-06

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 43.02  E-value: 8.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158447249   41 DPVQLG--VTELLSNVHRHAQPDKECTVELELLLDRLTVSVRDNDPRIPVATESDALD--LWDEPDALATSGR--GLAIV 114
Cdd:smart00387   2 DPDRLRqvLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEpfFRTDKRSRKIGGTglGLSIV 81

                           90       100
                   ....*....|....*....|....*..
gi 1158447249  115 GALSDSWG----VRPRGVSGKTVWFTL 137
Cdd:smart00387  82 KKLVELHGgeisVESEPGGGTTFTITL 108
 
Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
11-137 1.83e-25

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 95.37  E-value: 1.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158447249  11 VELQALPSRIGQIRRIVSAHLRHWQLD-DLVDPVQLGVTELLSNVHRHA---QPDKECTVELELLLDRLTVSVRDNDPRI 86
Cdd:COG2172     2 LSLPADLEDLGLARRAVRALLRELGLDeDDADDLVLAVSEAVTNAVRHAyggDPDGPVEVELELDPDGLEIEVRDEGPGF 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1158447249  87 PVAtesdalDLWDEPDALATSGRGLAIVGALSDSWGVRPRGvSGKTVWFTL 137
Cdd:COG2172    82 DPE------DLPDPYSTLAEGGRGLFLIRRLMDEVEYESDP-GGTTVRLVK 125
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 43-137 3.94e-20

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: 80.39  E-value: 3.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158447249  43 VQLGVTELLSNVHRHAQ---PDKECTVELELLLDRLTVSVRDNDPRIPVATESDaldlwdePDA-LATSGRGLAIVGALS 118
Cdd:cd16936     1 VELAVSEAVTNAVRHAYrhdGPGPVRLELDLDPDRLRVEVTDSGPGFDPLRPAD-------PDAgLREGGRGLALIRALM 73

                          90
                  ....*....|....*....
gi 1158447249 119 DSWGVRPRGVsGKTVWFTL 137
Cdd:cd16936    74 DEVGYRRTPG-GKTVWLEL 91
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
13-136 1.08e-15

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 70.01  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158447249  13 LQALPSRIGQIRRIVSAHLRHWQLD-DLVDPVQLGVTELLSNVHRHAQ---PDKECTVELELLLDRLTVSVRDNDPRIPV 88
Cdd:pfam13581   1 FPADPEQLRAARRVLEAVLRRAGLPeELLDEVELAVGEACTNAVEHAYregPEGPVEVRLTSDGGGLVVTVADSGPPFDP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1158447249  89 ATESDALDLWDEPDaLATSGRGLAIVGALSDSWGVRPRGVsGKTVWFT 136
Cdd:pfam13581  81 LTLPPPDLEEPDED-RKEGGRGLALIRGLMDDVEYTRGGE-GNTVRMR 126
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 41-137 4.11e-10

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: 54.68  E-value: 4.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158447249  41 DPVQLG--VTELLSNVHRHAQPDKECTVELELLlDRLTVSVRDNDPRIPVATESDALDLWDEPDALATSGRG--LAIVGA 116
Cdd:pfam02518   2 DELRLRqvLSNLLDNALKHAAKAGEITVTLSEG-GELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGGGTGlgLSIVRK 80

                          90       100
                  ....*....|....*....|....*
gi 1158447249 117 LSDSWG----VRPRGVSGKTVWFTL 137
Cdd:pfam02518  81 LVELLGgtitVESEPGGGTTVTLTL 105
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 41-137 8.24e-06

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 43.02  E-value: 8.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158447249   41 DPVQLG--VTELLSNVHRHAQPDKECTVELELLLDRLTVSVRDNDPRIPVATESDALD--LWDEPDALATSGR--GLAIV 114
Cdd:smart00387   2 DPDRLRqvLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEpfFRTDKRSRKIGGTglGLSIV 81

                           90       100
                   ....*....|....*....|....*..
gi 1158447249  115 GALSDSWG----VRPRGVSGKTVWFTL 137
Cdd:smart00387  82 KKLVELHGgeisVESEPGGGTTFTITL 108
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 47-92 1.13e-05

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.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 42.16  E-value: 1.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1158447249  47 VTELLSNVHRHAQPDKeCTVELELLLDRLTVSVRDNDPRIPVATES 92
Cdd:cd16917     5 VQEALTNALKHAGASR-VRVTLSYTADELTLTVVDDGVGFDGPAPP 49
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
40-137 8.95e-05

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 41.82  E-value: 8.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158447249  40 VDPVQLG--VTELLSNVHRHAQPDKECTVELELLLDRLTVSVRDNDPRIPvatESDALDLWD----EPDALATSGR--GL 111
Cdd:COG2205   128 ADPELLEqvLANLLDNAIKYSPPGGTITISARREGDGVRISVSDNGPGIP---EEELERIFErfyrGDNSRGEGGTglGL 204

                          90       100       110
                  ....*....|....*....|....*....|
gi 1158447249 112 AIVGALSDSWG----VRPRGVSGKTVWFTL 137
Cdd:COG2205   205 AIVKRIVEAHGgtiwVESEPGGGTTFTVTL 234
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
47-112 1.77e-04

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 40.76  E-value: 1.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1158447249  47 VTELLSNVHRHAQPdKECTVELELLLDRLTVSVRDNDPRIPvatesdaldlwdePDALATSGRGLA 112
Cdd:COG4585   167 VQEALTNALKHAGA-TRVTVTLEVDDGELTLTVRDDGVGFD-------------PEAAPGGGLGLR 218
 
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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