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Conserved domains on  [gi|1073966954|gb|AOV06673|]
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ATP-binding protein [Sporosarcina ureilytica]

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 ...
 15-131 3.00e-45

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: 143.28  E-value: 3.00e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073966954  15 DIVAARQLGRNEAKKLGFGTVDQARITTAISELARNIYLYAGKGKIEITCIHKDDATGISIIASDEGPGFPDVRKVMDDG 94
Cdd:cd16934     1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVALEILAVDQGPGIADVDEALRDG 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1073966954  95 FTTSGGLGAGMPGVRRLMDDFNIVTKRGVGTTITAIK 131
Cdd:cd16934    81 FSTGGGLGLGLGGVRRLADEFDLHSAPGRGTVVVARK 117
 
Name Accession Description Interval E-value
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
 15-131 3.00e-45

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: 143.28  E-value: 3.00e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073966954  15 DIVAARQLGRNEAKKLGFGTVDQARITTAISELARNIYLYAGKGKIEITCIHKDDATGISIIASDEGPGFPDVRKVMDDG 94
Cdd:cd16934     1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVALEILAVDQGPGIADVDEALRDG 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1073966954  95 FTTSGGLGAGMPGVRRLMDDFNIVTKRGVGTTITAIK 131
Cdd:cd16934    81 FSTGGGLGLGLGGVRRLADEFDLHSAPGRGTVVVARK 117
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
12-133 1.10e-27

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 98.83  E-value: 1.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073966954  12 TEWDIVAARQLGRNEAKKLGFGTVDQARITTAISELARNIYLYAGK----GKIEITCIHKDDatGISIIASDEGPGFPDV 87
Cdd:COG2172     7 DLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGgdpdGPVEVELELDPD--GLEIEVRDEGPGFDPE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1073966954  88 RkvMDDGFTTSGGLGAGMPGVRRLMDDFNIVTKRGvGTTITAIKWI 133
Cdd:COG2172    85 D--LPDPYSTLAEGGRGLFLIRRLMDEVEYESDPG-GTTVRLVKRL 127
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 36-128 9.15e-10

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 52.27  E-value: 9.15e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073966954   36 DQARITTAISELARNIYLYAGK-GKIEITCIHKDDATGISIiaSDEGPGFP--DVRKVMDDGFTTS------GGLGAGMP 106
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHVEITV--EDNGPGIPpeDLEKIFEPFFRTDkrsrkiGGTGLGLS 79

                           90       100
                   ....*....|....*....|....*.
gi 1073966954  107 GVRRLMDDFN----IVTKRGVGTTIT 128
Cdd:smart00387  80 IVKKLVELHGgeisVESEPGGGTTFT 105
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
15-131 1.16e-08

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 49.98  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073966954  15 DIVAARQLGRNEAKKLGFGTVDQARITTAISELARNIYLYAGK----GKIEITCihKDDATGISIIASDEGPGF-----P 85
Cdd:pfam13581   7 QLRAARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHAYRegpeGPVEVRL--TSDGGGLVVTVADSGPPFdpltlP 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1073966954  86 DVRKVMDDGFTTSGGLGAGMpgVRRLMDDFNIvTKRGVGTTITAIK 131
Cdd:pfam13581  85 PPDLEEPDEDRKEGGRGLAL--IRGLMDDVEY-TRGGEGNTVRMRK 127
 
Name Accession Description Interval E-value
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
 15-131 3.00e-45

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: 143.28  E-value: 3.00e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073966954  15 DIVAARQLGRNEAKKLGFGTVDQARITTAISELARNIYLYAGKGKIEITCIHKDDATGISIIASDEGPGFPDVRKVMDDG 94
Cdd:cd16934     1 DVVDARRAARELARRLGLSEVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGRVALEILAVDQGPGIADVDEALRDG 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1073966954  95 FTTSGGLGAGMPGVRRLMDDFNIVTKRGVGTTITAIK 131
Cdd:cd16934    81 FSTGGGLGLGLGGVRRLADEFDLHSAPGRGTVVVARK 117
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
12-133 1.10e-27

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 98.83  E-value: 1.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073966954  12 TEWDIVAARQLGRNEAKKLGFGTVDQARITTAISELARNIYLYAGK----GKIEITCIHKDDatGISIIASDEGPGFPDV 87
Cdd:COG2172     7 DLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGgdpdGPVEVELELDPD--GLEIEVRDEGPGFDPE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1073966954  88 RkvMDDGFTTSGGLGAGMPGVRRLMDDFNIVTKRGvGTTITAIKWI 133
Cdd:COG2172    85 D--LPDPYSTLAEGGRGLFLIRRLMDEVEYESDPG-GTTVRLVKRL 127
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 43-131 6.87e-10

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: 52.27  E-value: 6.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073966954  43 AISELARNIYLYAGK--GKIEITCIHKDDATGISIIASDEGPGFPDVRKVMDDGFTTSGGLgaGMPGVRRLMDDFnIVTK 120
Cdd:cd16936     4 AVSEAVTNAVRHAYRhdGPGPVRLELDLDPDRLRVEVTDSGPGFDPLRPADPDAGLREGGR--GLALIRALMDEV-GYRR 80

                          90
                  ....*....|.
gi 1073966954 121 RGVGTTITAIK 131
Cdd:cd16936    81 TPGGKTVWLEL 91
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 36-128 9.15e-10

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 52.27  E-value: 9.15e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073966954   36 DQARITTAISELARNIYLYAGK-GKIEITCIHKDDATGISIiaSDEGPGFP--DVRKVMDDGFTTS------GGLGAGMP 106
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHVEITV--EDNGPGIPpeDLEKIFEPFFRTDkrsrkiGGTGLGLS 79

                           90       100
                   ....*....|....*....|....*.
gi 1073966954  107 GVRRLMDDFN----IVTKRGVGTTIT 128
Cdd:smart00387  80 IVKKLVELHGgeisVESEPGGGTTFT 105
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
15-131 1.16e-08

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 49.98  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073966954  15 DIVAARQLGRNEAKKLGFGTVDQARITTAISELARNIYLYAGK----GKIEITCihKDDATGISIIASDEGPGF-----P 85
Cdd:pfam13581   7 QLRAARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHAYRegpeGPVEVRL--TSDGGGLVVTVADSGPPFdpltlP 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1073966954  86 DVRKVMDDGFTTSGGLGAGMpgVRRLMDDFNIvTKRGVGTTITAIK 131
Cdd:pfam13581  85 PPDLEEPDEDRKEGGRGLAL--IRGLMDDVEY-TRGGEGNTVRMRK 127
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
 40-131 2.34e-05

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: 41.37  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073966954  40 ITTAISELARNIYLYA----GKGKIEITCIHKDDAtgISIIASDEGPGFPDVRKVMDDGFTTSGGL---GAGMPGVRRLM 112
Cdd:cd16942    39 IKTVVSEAVTNAIIHGynndPNGIVSISVIIEDGV--VHLTVRDEGVGIPDIEEARQPLFTTKPELersGMGFTIMENFM 116

                          90
                  ....*....|....*....
gi 1073966954 113 DDFNIVTKRGVGTTITAIK 131
Cdd:cd16942   117 DEVIVESEVNKGTTVYLKK 135
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
35-128 4.31e-05

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 41.43  E-value: 4.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073966954  35 VDQARITTAISELARNIYLYAGKG-KIEITCIHKDDATGISIIasDEGPGFP--DVRKVMD-----DGFTTSGGLGAGMP 106
Cdd:COG2205   128 ADPELLEQVLANLLDNAIKYSPPGgTITISARREGDGVRISVS--DNGPGIPeeELERIFErfyrgDNSRGEGGTGLGLA 205

                          90       100
                  ....*....|....*....|....*.
gi 1073966954 107 GVRRLMD----DFNIVTKRGVGTTIT 128
Cdd:COG2205   206 IVKRIVEahggTIWVESEPGGGTTFT 231
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
 53-116 1.60e-04

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 40.05  E-value: 1.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1073966954  53 LYAGKGKIEITCIHKDDATGISIIASDEGPGFPDVRKVMDDgFTTSG--GLGAGMPGVRRLMDDFN 116
Cdd:COG4192   556 LDAVATQPQISVDLLSNAENLRVAISDNGNGWPLVDKLFTP-FTTTKevGLGLGLSICRSIMQQFG 620
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 55-128 5.45e-04

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 38.40  E-value: 5.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073966954  55 AGKGKIEITCIHKDDATGISIIasDEGPGFP-DVR-KVMDDGFTT-SGGLGAGMPGVRRLMDD----FNIVTKRGVGTTI 127
Cdd:COG5000   334 EEGGEIEVSTRREDGRVRIEVS--DNGPGIPeEVLeRIFEPFFTTkPKGTGLGLAIVKKIVEEhggtIELESRPGGGTTF 411


                  .
gi 1073966954 128 T 128
Cdd:COG5000   412 T 412
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
55-128 4.59e-03

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 35.76  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1073966954  55 AGKGKIEITCIHKDDATGISIiaSDEGPGFP--DVRKVMDDGFTTSGGLGAGMPGVR-RLM------DDFNIVTKRGVGT 125
Cdd:COG2972   357 EGGGTIRISIRKEGDRLVITV--EDNGVGMPeeKLEKLLEELSSKGEGRGIGLRNVReRLKlyygeeYGLEIESEPGEGT 434


                  ...
gi 1073966954 126 TIT 128
Cdd:COG2972   435 TVT 437
 
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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