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Conserved domains on  [gi|2041110722|gb|QVL17084|]
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anti-sigma regulatory factor [Pseudomonas qingdaonensis]

Protein Classification

anti-sigma regulatory factor( domain architecture ID 13014755)

anti-sigma regulatory factor similar to RsbT, an ATPase with serine/threonine kinase activity that phosphorylates its antagonist RsbS and stimulates the phosphatase RsbU in a signaling cascade that results in active sigma-B

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
 16-129 1.92e-30

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.


:

Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 105.53  E-value: 1.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041110722  16 DVVRARQLARTLAQGCGMSLINLTKLVTAVSELARNAVVYGGGGHMDWQVVEKDHRKGLRLTFRDEGPGIPDIKLAMTDG 95
Cdd:cd16934     1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVALEILAVDQGPGIADVDEALRDG 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2041110722  96 WTSGGGLGLGLTGAKRLVDEFELDTAPGAGTRVT 129
Cdd:cd16934    81 FSTGGGLGLGLGGVRRLADEFDLHSAPGRGTVVV 114
 
Name Accession Description Interval E-value
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
 16-129 1.92e-30

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.


Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 105.53  E-value: 1.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041110722  16 DVVRARQLARTLAQGCGMSLINLTKLVTAVSELARNAVVYGGGGHMDWQVVEKDHRKGLRLTFRDEGPGIPDIKLAMTDG 95
Cdd:cd16934     1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVALEILAVDQGPGIADVDEALRDG 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2041110722  96 WTSGGGLGLGLTGAKRLVDEFELDTAPGAGTRVT 129
Cdd:cd16934    81 FSTGGGLGLGLGGVRRLADEFDLHSAPGRGTVVV 114
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
14-133 8.77e-18

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 73.41  E-value: 8.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041110722  14 EQDVVRARQLARTLAQGCGMSLINLTKLVTAVSELARNAVVYGGGG------HMDWQVVEkdhrKGLRLTFRDEGPGIPD 87
Cdd:COG2172     8 LEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGdpdgpvEVELELDP----DGLEIEVRDEGPGFDP 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2041110722  88 IKLAmtDGWTSGGGLGLGLTGAKRLVDEFELDTAPGaGTRVTILRW 133
Cdd:COG2172    84 EDLP--DPYSTLAEGGRGLFLIRRLMDEVEYESDPG-GTTVRLVKR 126
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 39-130 3.13e-06

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: 43.13  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041110722  39 TKLVTAVSELARNAVVYGGGGHMDWQVVEKDHRkgLRLTFRDEGPGIP--DIKLAMTDGWTSGGGLGLGL----TGAKRL 112
Cdd:pfam02518   4 LRLRQVLSNLLDNALKHAAKAGEITVTLSEGGE--LTLTVEDNGIGIPpeDLPRIFEPFSTADKRGGGGTglglSIVRKL 81

                          90       100
                  ....*....|....*....|..
gi 2041110722 113 VD----EFELDTAPGAGTRVTI 130
Cdd:pfam02518  82 VEllggTITVESEPGGGTTVTL 103
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 41-130 2.68e-04

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 38.01  E-value: 2.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041110722   41 LVTAVSELARNAVVYGG-GGHMDwqVVEKDHRKGLRLTFRDEGPGIP--DIKLAMTDGWTSGGGLGLGLTG------AKR 111
Cdd:smart00387   6 LRQVLSNLLDNAIKYTPeGGRIT--VTLERDGDHVEITVEDNGPGIPpeDLEKIFEPFFRTDKRSRKIGGTglglsiVKK 83

                           90       100
                   ....*....|....*....|...
gi 2041110722  112 LVDEF----ELDTAPGAGTRVTI 130
Cdd:smart00387  84 LVELHggeiSVESEPGGGTTFTI 106
 
Name Accession Description Interval E-value
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
 16-129 1.92e-30

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.


Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 105.53  E-value: 1.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041110722  16 DVVRARQLARTLAQGCGMSLINLTKLVTAVSELARNAVVYGGGGHMDWQVVEKDHRKGLRLTFRDEGPGIPDIKLAMTDG 95
Cdd:cd16934     1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVALEILAVDQGPGIADVDEALRDG 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2041110722  96 WTSGGGLGLGLTGAKRLVDEFELDTAPGAGTRVT 129
Cdd:cd16934    81 FSTGGGLGLGLGGVRRLADEFDLHSAPGRGTVVV 114
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
14-133 8.77e-18

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 73.41  E-value: 8.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041110722  14 EQDVVRARQLARTLAQGCGMSLINLTKLVTAVSELARNAVVYGGGG------HMDWQVVEkdhrKGLRLTFRDEGPGIPD 87
Cdd:COG2172     8 LEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGdpdgpvEVELELDP----DGLEIEVRDEGPGFDP 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2041110722  88 IKLAmtDGWTSGGGLGLGLTGAKRLVDEFELDTAPGaGTRVTILRW 133
Cdd:COG2172    84 EDLP--DPYSTLAEGGRGLFLIRRLMDEVEYESDPG-GTTVRLVKR 126
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 39-130 3.13e-06

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: 43.13  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041110722  39 TKLVTAVSELARNAVVYGGGGHMDWQVVEKDHRkgLRLTFRDEGPGIP--DIKLAMTDGWTSGGGLGLGL----TGAKRL 112
Cdd:pfam02518   4 LRLRQVLSNLLDNALKHAAKAGEITVTLSEGGE--LTLTVEDNGIGIPpeDLPRIFEPFSTADKRGGGGTglglSIVRKL 81

                          90       100
                  ....*....|....*....|..
gi 2041110722 113 VD----EFELDTAPGAGTRVTI 130
Cdd:pfam02518  82 VEllggTITVESEPGGGTTVTL 103
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 41-130 2.68e-04

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 38.01  E-value: 2.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041110722   41 LVTAVSELARNAVVYGG-GGHMDwqVVEKDHRKGLRLTFRDEGPGIP--DIKLAMTDGWTSGGGLGLGLTG------AKR 111
Cdd:smart00387   6 LRQVLSNLLDNAIKYTPeGGRIT--VTLERDGDHVEITVEDNGPGIPpeDLEKIFEPFFRTDKRSRKIGGTglglsiVKK 83

                           90       100
                   ....*....|....*....|...
gi 2041110722  112 LVDEF----ELDTAPGAGTRVTI 130
Cdd:smart00387  84 LVELHggeiSVESEPGGGTTFTI 106
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
 38-132 3.55e-04

Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of SpoIIAB, an anti sigma-F factor and a serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli where, early in sporulation, the cell divides into two unequal compartments: a larger mother cell and a smaller forespore. Sigma-F transcription factor is activated in the forespore directly after the asymmetric septum forms, and its spatial and temporal activation is required for sporulation. Free sigma-F can associate with the RNA polymerase core and activate transcription of the sigma-F regulon, its regulation may comprise a partner-switching mechanism involving SpoIIAB, SpoIIAA, and sigma-F as follows: SpoIIAB can form alternative complexes with either: i) sigma-F, holding it in an inactive form and preventing its association with RNA polymerase, or ii) unphosphorylated SpoIIAA and a nucleotide, either ATP or ADP. In the presence of ATP, SpoIIAB acts as a kinase to specifically phosphorylate a serine residue of SpoIIAA; this phosphorylated form has low affinity for SpoIIAB and dissociates, making SpoIIAB available to capture sigma-F. SpoIIAA may then be dephosphorylated by a SpoIIE serine phosphatase and be free to attack the SpoIIAB sigma-F complex to induce the release of sigma-F.


Pssm-ID: 340418 [Multi-domain]  Cd Length: 135  Bit Score: 37.90  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041110722  38 LTKLVTAVSELARNAVVYG----GGGHMDWQVVEKDHRkgLRLTFRDEGPGIPDIKLAMTDGWTSGGGLGLGL---TGAK 110
Cdd:cd16942    36 LTEIKTVVSEAVTNAIIHGynndPNGIVSISVIIEDGV--VHLTVRDEGVGIPDIEEARQPLFTTKPELERSGmgfTIME 113

                          90       100
                  ....*....|....*....|..
gi 2041110722 111 RLVDEFELDTAPGAGTRVTILR 132
Cdd:cd16942   114 NFMDEVIVESEVNKGTTVYLKK 135
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
9-130 1.13e-03

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 37.19  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041110722   9 QPILLEQDVVRARQLARTLAQGCGMSL------------INLTKLVTAVSELARNAVVYGG-GGHMDWQVVEKDHRkgLR 75
Cdd:COG2205    89 EPVDLAELLEEAVEELRPLAEEKGIRLeldlppelplvyADPELLEQVLANLLDNAIKYSPpGGTITISARREGDG--VR 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2041110722  76 LTFRDEGPGIPDIKLA-MTDGWTSGGGLGLGLTG------AKRLVD----EFELDTAPGAGTRVTI 130
Cdd:COG2205   167 ISVSDNGPGIPEEELErIFERFYRGDNSRGEGGTglglaiVKRIVEahggTIWVESEPGGGTTFTV 232
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
16-133 2.44e-03

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 35.73  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041110722  16 DVVRARQLARTLAQ--GCGMSLINltKLVTAVSELARNAVVYGGGGHMDwQVVE---KDHRKGLRLTFRDEGPGIPDIKL 90
Cdd:pfam13581   7 QLRAARRVLEAVLRraGLPEELLD--EVELAVGEACTNAVEHAYREGPE-GPVEvrlTSDGGGLVVTVADSGPPFDPLTL 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2041110722  91 AMTDGWTSGGGLGLG---LTGAKRLVDEFELDTAPGaGTRVTiLRW 133
Cdd:pfam13581  84 PPPDLEEPDEDRKEGgrgLALIRGLMDDVEYTRGGE-GNTVR-MRK 127
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 41-91 5.64e-03

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: 33.78  E-value: 5.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2041110722  41 LVTAVSELARNAVVYGGGGHMDWQV-VEKDHRKG-LRLTFRDEGPGIPDIKLA 91
Cdd:cd16936     1 VELAVSEAVTNAVRHAYRHDGPGPVrLELDLDPDrLRVEVTDSGPGFDPLRPA 53
 
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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