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Conserved domains on  [gi|2155128114|ref|WP_229822942|]
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ATP-binding protein [Streptomyces netropsis]

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];
25-143 9.73e-21

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


:

Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 81.88  E-value: 9.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155128114  25 FHFPALNTSVAEARRRVLARLREWGIDEVACDDAQLVVSELFTNAVRHTDSD----KVSCQLRISGARLRIEIADQGHT- 99
Cdd:COG2172     2 LSLPADLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGdpdgPVEVELELDPDGLEIEVRDEGPGf 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2155128114 100 PTEPRARCSGADEESGRGLLLVGAVSEAWGVRPDDSgrGRVVWA 143
Cdd:COG2172    82 DPEDLPDPYSTLAEGGRGLFLIRRLMDEVEYESDPG--GTTVRL 123
 
Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
25-143 9.73e-21

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 81.88  E-value: 9.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155128114  25 FHFPALNTSVAEARRRVLARLREWGIDEVACDDAQLVVSELFTNAVRHTDSD----KVSCQLRISGARLRIEIADQGHT- 99
Cdd:COG2172     2 LSLPADLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGdpdgPVEVELELDPDGLEIEVRDEGPGf 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2155128114 100 PTEPRARCSGADEESGRGLLLVGAVSEAWGVRPDDSgrGRVVWA 143
Cdd:COG2172    82 DPEDLPDPYSTLAEGGRGLFLIRRLMDEVEYESDPG--GTTVRL 123
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 58-145 2.86e-19

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: 76.92  E-value: 2.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155128114  58 AQLVVSELFTNAVRHTDSDKVSCQLRI----SGARLRIEIADQGHTPTEPRARC-SGADEESGRGLLLVGAVSEAWGVRP 132
Cdd:cd16936     1 VELAVSEAVTNAVRHAYRHDGPGPVRLeldlDPDRLRVEVTDSGPGFDPLRPADpDAGLREGGRGLALIRALMDEVGYRR 80

                          90
                  ....*....|...
gi 2155128114 133 DDsgRGRVVWADL 145
Cdd:cd16936    81 TP--GGKTVWLEL 91
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
27-142 1.97e-11

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 57.68  E-value: 1.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155128114  27 FPALNTSVAEARRRVLARLREWGIDEVACDDAQLVVSELFTNAVRH----TDSDKVSCQLRISGARLRIEIADQGH---- 98
Cdd:pfam13581   1 FPADPEQLRAARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHayreGPEGPVEVRLTSDGGGLVVTVADSGPpfdp 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2155128114  99 --TPTEPRARCSGADEESGRGLLLVGAVSEAwgVRPDDSGRGRVVW 142
Cdd:pfam13581  81 ltLPPPDLEEPDEDRKEGGRGLALIRGLMDD--VEYTRGGEGNTVR 124
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 59-97 4.39e-05

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 40.32  E-value: 4.39e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2155128114   59 QLVVSELFTNAVRHTDSD-KVSCQLRISGARLRIEIADQG 97
Cdd:smart00387   7 RQVLSNLLDNAIKYTPEGgRITVTLERDGDHVEITVEDNG 46
 
Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
25-143 9.73e-21

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 81.88  E-value: 9.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155128114  25 FHFPALNTSVAEARRRVLARLREWGIDEVACDDAQLVVSELFTNAVRHTDSD----KVSCQLRISGARLRIEIADQGHT- 99
Cdd:COG2172     2 LSLPADLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGdpdgPVEVELELDPDGLEIEVRDEGPGf 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2155128114 100 PTEPRARCSGADEESGRGLLLVGAVSEAWGVRPDDSgrGRVVWA 143
Cdd:COG2172    82 DPEDLPDPYSTLAEGGRGLFLIRRLMDEVEYESDPG--GTTVRL 123
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 58-145 2.86e-19

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: 76.92  E-value: 2.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155128114  58 AQLVVSELFTNAVRHTDSDKVSCQLRI----SGARLRIEIADQGHTPTEPRARC-SGADEESGRGLLLVGAVSEAWGVRP 132
Cdd:cd16936     1 VELAVSEAVTNAVRHAYRHDGPGPVRLeldlDPDRLRVEVTDSGPGFDPLRPADpDAGLREGGRGLALIRALMDEVGYRR 80

                          90
                  ....*....|...
gi 2155128114 133 DDsgRGRVVWADL 145
Cdd:cd16936    81 TP--GGKTVWLEL 91
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
27-142 1.97e-11

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 57.68  E-value: 1.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155128114  27 FPALNTSVAEARRRVLARLREWGIDEVACDDAQLVVSELFTNAVRH----TDSDKVSCQLRISGARLRIEIADQGH---- 98
Cdd:pfam13581   1 FPADPEQLRAARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHayreGPEGPVEVRLTSDGGGLVVTVADSGPpfdp 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2155128114  99 --TPTEPRARCSGADEESGRGLLLVGAVSEAwgVRPDDSGRGRVVW 142
Cdd:pfam13581  81 ltLPPPDLEEPDEDRKEGGRGLALIRGLMDD--VEYTRGGEGNTVR 124
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 56-145 9.96e-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: 41.97  E-value: 9.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155128114  56 DDAQLVVSELFTNAVRHT-DSDKVSCQLRiSGARLRIEIADQG-----------HTPTEPRARCSGadEESGRGLLLVGA 123
Cdd:pfam02518   4 LRLRQVLSNLLDNALKHAaKAGEITVTLS-EGGELTLTVEDNGigippedlpriFEPFSTADKRGG--GGTGLGLSIVRK 80

                          90       100
                  ....*....|....*....|....*
gi 2155128114 124 VSEAWGVR---PDDSGRGRVVWADL 145
Cdd:pfam02518  81 LVELLGGTitvESEPGGGTTVTLTL 105
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
52-118 1.21e-05

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 43.36  E-value: 1.21e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2155128114  52 EVACDDAQL--VVSELFTNAVRHTDSD-KVSCQLRISGARLRIEIADQG--------HTPTEPRARCSGADEESGRGL 118
Cdd:COG2205   125 LVYADPELLeqVLANLLDNAIKYSPPGgTITISARREGDGVRISVSDNGpgipeeelERIFERFYRGDNSRGEGGTGL 202
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 59-97 4.39e-05

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 40.32  E-value: 4.39e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2155128114   59 QLVVSELFTNAVRHTDSD-KVSCQLRISGARLRIEIADQG 97
Cdd:smart00387   7 RQVLSNLLDNAIKYTPEGgRITVTLERDGDHVEITVEDNG 46
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
53-118 4.25e-04

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 39.15  E-value: 4.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2155128114  53 VACDDAQL--VVSELFTNAVRHTDSD-KVSCQLRISGARLRIEIADQG------HTP--TEP--RARCSGADEESGRGL 118
Cdd:COG5002   275 VLGDPDRLeqVLTNLLDNAIKYTPEGgTITVSLREEDDQVRISVRDTGigipeeDLPriFERfyRVDKSRSRETGGTGL 353
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
49-97 7.51e-04

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 38.35  E-value: 7.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2155128114  49 GIDEVACDDAQL--VVSELFTNAVRHTDSD-KVSCQLRISGARLRIEIADQG 97
Cdd:COG0642   213 DLPTVRGDPDRLrqVLLNLLSNAIKYTPEGgTVTVSVRREGDRVRISVEDTG 264
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 61-119 1.08e-03

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: 35.99  E-value: 1.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2155128114  61 VVSELFTNAVRHTDSDKVSCQLRISGARLRIEIADQGHTPTEPrarcsGADEESGRGLL 119
Cdd:cd16917     4 IVQEALTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGP-----APPGGGGFGLL 57
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 60-121 2.75e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA, YehU, Bacillus subtilis LytS, and some hybrid sensor histidine kinases; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. It also includes the HATPase domains of Escherichia coli YpdA and YehU, HKs of YpdA-YpdB and YehU-YehTCSs, which are involved together in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), some having accessory sensor domain(s) such as Cache, HAMP or GAF; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340401 [Multi-domain]  Cd Length: 103  Bit Score: 35.50  E-value: 2.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2155128114  60 LVVSELFTNAVRH-----TDSDKVSCQLRISGARLRIEIADQGHTPTEPRARCSGADEESGRGLLLV 121
Cdd:cd16924     4 FTLQPLVENAIQHglsplTDKGVVTISALKEDNHVMIEVEDNGRGIDPKVLNILGKKPKEGNGIGLY 70
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 60-97 3.02e-03

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: 35.86  E-value: 3.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2155128114  60 LVVSELFTNAVRH--TDSDKVSCQLRIS--GARLRIEIADQG 97
Cdd:cd16951    42 LVVNELLQNALKHafSDREGGTITIRSVvdGDYLRITVIDDG 83
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
 60-118 7.86e-03

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 35.65  E-value: 7.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2155128114  60 LVVSELFTNAVRH----TDSDKVSCQLRISGARLRIEIADQGHTPTEprarcsGADEESGRGL 118
Cdd:COG3920   402 LILNELVTNALKHaflsGEGGRIRVSWRREDGRLRLTVSDNGVGLPE------DVDPPARKGL 458
 
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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