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Conserved domains on  [gi|759537887|ref|WP_043257900|]
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ATP-binding protein [Streptomyces sp. Tu6071]

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];
6-118 1.67e-14

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


:

Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 64.55  E-value: 1.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759537887   6 SAELTAVDA--RLLAQTYAAAHCPRVDRAAVALVVAELLANAERHT-----AGSWRLVVSHSTRLLSIAVHDLGRLLP-- 76
Cdd:COG2172    5 PADLEDLGLarRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAyggdpDGPVEVELELDPDGLEIEVRDEGPGFDpe 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 759537887  77 -LPGKVAFDGTGQFGLRIIRGLSDHFSVHSGPTGKTVTAQWHL 118
Cdd:COG2172   85 dLPDPYSTLAEGGRGLFLIRRLMDEVEYESDPGGTTVRLVKRL 127
 
Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
6-118 1.67e-14

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 64.55  E-value: 1.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759537887   6 SAELTAVDA--RLLAQTYAAAHCPRVDRAAVALVVAELLANAERHT-----AGSWRLVVSHSTRLLSIAVHDLGRLLP-- 76
Cdd:COG2172    5 PADLEDLGLarRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAyggdpDGPVEVELELDPDGLEIEVRDEGPGFDpe 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 759537887  77 -LPGKVAFDGTGQFGLRIIRGLSDHFSVHSGPTGKTVTAQWHL 118
Cdd:COG2172   85 dLPDPYSTLAEGGRGLFLIRRLMDEVEYESDPGGTTVRLVKRL 127
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 34-116 2.02e-12

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: 58.43  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759537887  34 VALVVAELLANAERHTAGSW-----RLVVSHSTRLLSIAVHDLGRLLPLPGKV---AFDGTGQFGLRIIRGLSDHFSVHS 105
Cdd:cd16936    1 VELAVSEAVTNAVRHAYRHDgpgpvRLELDLDPDRLRVEVTDSGPGFDPLRPAdpdAGLREGGRGLALIRALMDEVGYRR 80

                         90
                 ....*....|.
gi 759537887 106 GPTGKTVTAQW 116
Cdd:cd16936   81 TPGGKTVWLEL 91
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
6-116 7.74e-12

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 57.68  E-value: 7.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759537887    6 SAELTAVD-ARLLAQTYAAAH-CPRVDRAAVALVVAELLANAERH-----TAGSWRLVVSHSTRLLSIAVHDLGR----- 73
Cdd:pfam13581   2 PADPEQLRaARRVLEAVLRRAgLPEELLDEVELAVGEACTNAVEHayregPEGPVEVRLTSDGGGLVVTVADSGPpfdpl 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 759537887   74 ---LLPLPGKVAFDGTGQFGLRIIRGLSDHFSVHSGPTGKTVTAQW 116
Cdd:pfam13581  82 tlpPPDLEEPDEDRKEGGRGLALIRGLMDDVEYTRGGEGNTVRMRK 127
 
Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
6-118 1.67e-14

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 64.55  E-value: 1.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759537887   6 SAELTAVDA--RLLAQTYAAAHCPRVDRAAVALVVAELLANAERHT-----AGSWRLVVSHSTRLLSIAVHDLGRLLP-- 76
Cdd:COG2172    5 PADLEDLGLarRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAyggdpDGPVEVELELDPDGLEIEVRDEGPGFDpe 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 759537887  77 -LPGKVAFDGTGQFGLRIIRGLSDHFSVHSGPTGKTVTAQWHL 118
Cdd:COG2172   85 dLPDPYSTLAEGGRGLFLIRRLMDEVEYESDPGGTTVRLVKRL 127
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 34-116 2.02e-12

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: 58.43  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759537887  34 VALVVAELLANAERHTAGSW-----RLVVSHSTRLLSIAVHDLGRLLPLPGKV---AFDGTGQFGLRIIRGLSDHFSVHS 105
Cdd:cd16936    1 VELAVSEAVTNAVRHAYRHDgpgpvRLELDLDPDRLRVEVTDSGPGFDPLRPAdpdAGLREGGRGLALIRALMDEVGYRR 80

                         90
                 ....*....|.
gi 759537887 106 GPTGKTVTAQW 116
Cdd:cd16936   81 TPGGKTVWLEL 91
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
6-116 7.74e-12

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 57.68  E-value: 7.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759537887    6 SAELTAVD-ARLLAQTYAAAH-CPRVDRAAVALVVAELLANAERH-----TAGSWRLVVSHSTRLLSIAVHDLGR----- 73
Cdd:pfam13581   2 PADPEQLRaARRVLEAVLRRAgLPEELLDEVELAVGEACTNAVEHayregPEGPVEVRLTSDGGGLVVTVADSGPpfdpl 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 759537887   74 ---LLPLPGKVAFDGTGQFGLRIIRGLSDHFSVHSGPTGKTVTAQW 116
Cdd:pfam13581  82 tlpPPDLEEPDEDRKEGGRGLALIRGLMDDVEYTRGGEGNTVRMRK 127
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 29-113 2.24e-05

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.


Pssm-ID: 340427 [Multi-domain]  Cd Length: 131  Bit Score: 40.86  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759537887  29 VDRA-AVALVVAELLANAERHT-----AGSWRLVVSHSTRLLSIAVHDLGRLLPLPGKVAfdGTGQFGLRIIR----GLS 98
Cdd:cd16951   34 SEVAtAIGLVVNELLQNALKHAfsdreGGTITIRSVVDGDYLRITVIDDGVGLPQDEDWP--NKGSLGLQIVRslveGEL 111

                         90
                 ....*....|....*.
gi 759537887  99 DHF-SVHSGPTGKTVT 113
Cdd:cd16951  112 KAFlEVQSAENGTRVN 127
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 30-120 2.42e-03

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: 35.04  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759537887   30 DRAAVALVVAELLANAERHTAGSWRLVVS-HSTRLLSIAVHDLGR-----LLPL-------PGKVAFDGTGqFGLRIIRG 96
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKAGEITVTlSEGGELTLTVEDNGIgippeDLPRifepfstADKRGGGGTG-LGLSIVRK 80

                          90       100
                  ....*....|....*....|....*....
gi 759537887   97 LSD----HFSVHSGP-TGKTVTAQWHLAT 120
Cdd:pfam02518  81 LVEllggTITVESEPgGGTTVTLTLPLAQ 109
 
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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