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Conserved domains on  [gi|1912961173|ref|WP_191851947|]
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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];
30-149 1.87e-17

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


:

Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 74.18  E-value: 1.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912961173  30 ASDLRSVPEVRRELRELLDGRA-ERDRCAVAELLTSELVANALVHTDREA-----VVTAVVSGRGLRVEVRDfaeRGPVP 103
Cdd:COG2172     5 PADLEDLGLARRAVRALLRELGlDEDDADDLVLAVSEAVTNAVRHAYGGDpdgpvEVELELDPDGLEIEVRD---EGPGF 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1912961173 104 RSSPVREETETDRErtHGRGLLLVRALADAWGVRAHEVGKSVWFEL 149
Cdd:COG2172    82 DPEDLPDPYSTLAE--GGRGLFLIRRLMDEVEYESDPGGTTVRLVK 125
 
Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
30-149 1.87e-17

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 74.18  E-value: 1.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912961173  30 ASDLRSVPEVRRELRELLDGRA-ERDRCAVAELLTSELVANALVHTDREA-----VVTAVVSGRGLRVEVRDfaeRGPVP 103
Cdd:COG2172     5 PADLEDLGLARRAVRALLRELGlDEDDADDLVLAVSEAVTNAVRHAYGGDpdgpvEVELELDPDGLEIEVRD---EGPGF 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1912961173 104 RSSPVREETETDRErtHGRGLLLVRALADAWGVRAHEVGKSVWFEL 149
Cdd:COG2172    82 DPEDLPDPYSTLAE--GGRGLFLIRRLMDEVEYESDPGGTTVRLVK 125
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 59-149 2.01e-16

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: 70.37  E-value: 2.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912961173  59 AELLTSELVANALVHTDREA-----VVTAVVSGRGLRVEVRDFAERGPVPRSSPVREEtetdrERTHGRGLLLVRALADA 133
Cdd:cd16936     1 VELAVSEAVTNAVRHAYRHDgpgpvRLELDLDPDRLRVEVTDSGPGFDPLRPADPDAG-----LREGGRGLALIRALMDE 75

                          90
                  ....*....|....*.
gi 1912961173 134 WGVRAHEVGKSVWFEL 149
Cdd:cd16936    76 VGYRRTPGGKTVWLEL 91
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
30-147 6.74e-09

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 51.52  E-value: 6.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912961173  30 ASDLRSVPEVRRELRELLD----GRAERDRCAVAellTSELVANALVHTDREAV-----VTAVVSGRGLRVEVRDFAERG 100
Cdd:pfam13581   2 PADPEQLRAARRVLEAVLRraglPEELLDEVELA---VGEACTNAVEHAYREGPegpveVRLTSDGGGLVVTVADSGPPF 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1912961173 101 PVPRSSPVREETETDRERTHGRGLLLVRALADAWGVRAHEVGKSVWF 147
Cdd:pfam13581  79 DPLTLPPPDLEEPDEDRKEGGRGLALIRGLMDDVEYTRGGEGNTVRM 125
 
Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
30-149 1.87e-17

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 74.18  E-value: 1.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912961173  30 ASDLRSVPEVRRELRELLDGRA-ERDRCAVAELLTSELVANALVHTDREA-----VVTAVVSGRGLRVEVRDfaeRGPVP 103
Cdd:COG2172     5 PADLEDLGLARRAVRALLRELGlDEDDADDLVLAVSEAVTNAVRHAYGGDpdgpvEVELELDPDGLEIEVRD---EGPGF 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1912961173 104 RSSPVREETETDRErtHGRGLLLVRALADAWGVRAHEVGKSVWFEL 149
Cdd:COG2172    82 DPEDLPDPYSTLAE--GGRGLFLIRRLMDEVEYESDPGGTTVRLVK 125
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 59-149 2.01e-16

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: 70.37  E-value: 2.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912961173  59 AELLTSELVANALVHTDREA-----VVTAVVSGRGLRVEVRDFAERGPVPRSSPVREEtetdrERTHGRGLLLVRALADA 133
Cdd:cd16936     1 VELAVSEAVTNAVRHAYRHDgpgpvRLELDLDPDRLRVEVTDSGPGFDPLRPADPDAG-----LREGGRGLALIRALMDE 75

                          90
                  ....*....|....*.
gi 1912961173 134 WGVRAHEVGKSVWFEL 149
Cdd:cd16936    76 VGYRRTPGGKTVWLEL 91
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
30-147 6.74e-09

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 51.52  E-value: 6.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912961173  30 ASDLRSVPEVRRELRELLD----GRAERDRCAVAellTSELVANALVHTDREAV-----VTAVVSGRGLRVEVRDFAERG 100
Cdd:pfam13581   2 PADPEQLRAARRVLEAVLRraglPEELLDEVELA---VGEACTNAVEHAYREGPegpveVRLTSDGGGLVVTVADSGPPF 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1912961173 101 PVPRSSPVREETETDRERTHGRGLLLVRALADAWGVRAHEVGKSVWF 147
Cdd:pfam13581  79 DPLTLPPPDLEEPDEDRKEGGRGLALIRGLMDDVEYTRGGEGNTVRM 125
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 64-149 2.00e-04

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: 39.27  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912961173  64 SELVANALVHTDREAVVT-AVVSGRGLRVEVRDfaeRGP------VPRSSPVREETETDRERTHGRGLLLVRALADAWGV 136
Cdd:pfam02518  11 SNLLDNALKHAAKAGEITvTLSEGGELTLTVED---NGIgippedLPRIFEPFSTADKRGGGGTGLGLSIVRKLVELLGG 87

                          90
                  ....*....|....*...
gi 1912961173 137 RAH-----EVGKSVWFEL 149
Cdd:pfam02518  88 TITvesepGGGTTVTLTL 105
 
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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