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Conserved domains on  [gi|543000764|gb|ERI95740|]
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ATPase/histidine kinase/DNA gyrase B/HSP90 domain protein [Clostridiales bacterium oral taxon 876 str. F0540]

Protein Classification

sensor histidine kinase( domain architecture ID 11459466)

sensor histidine kinase, part of a two-component regulatory system, functions as a protein kinase that phosphorylates a target protein in response to a signal; may contain an N-terminal HAMP signaling domain

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
28-489 4.61e-80

Sensor histidine kinase YesM [Signal transduction mechanisms];


:

Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 256.48  E-value: 4.61e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764  28 ISLVMSKRINDHYNIMLNKMSTTNQIKSYLTDSFNNFNKYIQTNTAQSKKIYEDSYNKAALNLNYLKANSDLDSRYILRD 107
Cdd:COG2972    1 LSKSLSLLSIVLLLLILLLLVLLILLLSLLLIILLLLLLLILLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLALL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 108 LENSLGSYKASADETIKIHDDQNNIDAYYSGYVNTKDIASYCNVFIGKLSDSYLNYNSEI----YNKLKEKEKFIYKVLA 183
Cdd:COG2972   81 LILLLLLLLLLLLILLLSLLLLLALILLLALLLLLSILLLILGLLLIILLLLSLLGWTLVslipKSELFRGLFSLRRLIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 184 AYIGVALLISIFYTLLFLRNILSKLRELVDTSEKVSSGDFTYYEGRKIDiyELDILSAAFSTMISNIKDHINTLKETAEL 263
Cdd:COG2972  161 LIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKVEKGDLVRLEVSGND--EIGILARSFNEMVERIKELIEEVYELELE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 264 QKKIsddemkllkyentlklsQLKVLQSQINPHFLFNTLNCINQTAIKENALSTESLIRSVSGILRYSLSMMNRYATLEQ 343
Cdd:COG2972  239 KKEA-----------------ELKALQAQINPHFLFNTLNSIRWLAELEDPEEAEEMLEALSKLLRYSLSKGDELVTLEE 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 344 EIEIIKQYMFIQQLRYGDRVSFILNINADLSKVKIPGMTLQPFVENAFIHGIEPKEEGGTIIIDIHEEDGSCIIIVEDNG 423
Cdd:COG2972  302 ELELIKSYLEIQKLRFGDRLEVEIEIDEELLDLLIPKLILQPLVENAIEHGIEPKEGGGTIRISIRKEGDRLVITVEDNG 381
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543000764 424 CGIDEETLSKITSEDftqEHNGHTTGMGIKSVVERLELMYEGKNIFEIKSQKRVGTKIYLKIPIKG 489
Cdd:COG2972  382 VGMPEEKLEKLLEEL---SSKGEGRGIGLRNVRERLKLYYGEEYGLEIESEPGEGTTVTIRIPLEE 444
 
Name Accession Description Interval E-value
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
28-489 4.61e-80

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 256.48  E-value: 4.61e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764  28 ISLVMSKRINDHYNIMLNKMSTTNQIKSYLTDSFNNFNKYIQTNTAQSKKIYEDSYNKAALNLNYLKANSDLDSRYILRD 107
Cdd:COG2972    1 LSKSLSLLSIVLLLLILLLLVLLILLLSLLLIILLLLLLLILLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLALL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 108 LENSLGSYKASADETIKIHDDQNNIDAYYSGYVNTKDIASYCNVFIGKLSDSYLNYNSEI----YNKLKEKEKFIYKVLA 183
Cdd:COG2972   81 LILLLLLLLLLLLILLLSLLLLLALILLLALLLLLSILLLILGLLLIILLLLSLLGWTLVslipKSELFRGLFSLRRLIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 184 AYIGVALLISIFYTLLFLRNILSKLRELVDTSEKVSSGDFTYYEGRKIDiyELDILSAAFSTMISNIKDHINTLKETAEL 263
Cdd:COG2972  161 LIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKVEKGDLVRLEVSGND--EIGILARSFNEMVERIKELIEEVYELELE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 264 QKKIsddemkllkyentlklsQLKVLQSQINPHFLFNTLNCINQTAIKENALSTESLIRSVSGILRYSLSMMNRYATLEQ 343
Cdd:COG2972  239 KKEA-----------------ELKALQAQINPHFLFNTLNSIRWLAELEDPEEAEEMLEALSKLLRYSLSKGDELVTLEE 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 344 EIEIIKQYMFIQQLRYGDRVSFILNINADLSKVKIPGMTLQPFVENAFIHGIEPKEEGGTIIIDIHEEDGSCIIIVEDNG 423
Cdd:COG2972  302 ELELIKSYLEIQKLRFGDRLEVEIEIDEELLDLLIPKLILQPLVENAIEHGIEPKEGGGTIRISIRKEGDRLVITVEDNG 381
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543000764 424 CGIDEETLSKITSEDftqEHNGHTTGMGIKSVVERLELMYEGKNIFEIKSQKRVGTKIYLKIPIKG 489
Cdd:COG2972  382 VGMPEEKLEKLLEEL---SSKGEGRGIGLRNVRERLKLYYGEEYGLEIESEPGEGTTVTIRIPLEE 444
His_kinase pfam06580
Histidine kinase; This family represents a region within bacterial histidine kinase enzymes. ...
284-363 1.80e-26

Histidine kinase; This family represents a region within bacterial histidine kinase enzymes. Two-component signal transduction systems such as those mediated by histidine kinase are integral parts of bacterial cellular regulatory processes, and are used to regulate the expression of genes involved in virulence. Members of this family often contain pfam02518 and/or pfam00672.


Pssm-ID: 461952 [Multi-domain]  Cd Length: 79  Bit Score: 102.13  E-value: 1.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764  284 SQLKVLQSQINPHFLFNTLNCINQTAIKENALsTESLIRSVSGILRYSLSMMNRYATLEQEIEIIKQYMFIQQLRYGDRV 363
Cdd:pfam06580   1 AELKALQAQINPHFLFNTLNSISSLAIEDPEE-AAEMILKLSDLLRYSLYEGEELVTLEEELEFLENYLEIQKIRFGDRL 79
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
378-486 6.02e-17

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: 76.33  E-value: 6.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 378 IPGMTLQPFVENAFIHGIEPKEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEetlsKITSEDFTQEHNGhtTGMGIKSVVE 457
Cdd:cd16924    1 IPPFTLQPLVENAIQHGLSPLTDKGVVTISALKEDNHVMIEVEDNGRGIDP----KVLNILGKKPKEG--NGIGLYNVHQ 74
                         90       100
                 ....*....|....*....|....*....
gi 543000764 458 RLELMYEGKNIFEIKSQKRVGTKIYLKIP 486
Cdd:cd16924   75 RLILLFGEDYGIHIASEPDKGTRITFTIP 103
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
387-488 1.41e-15

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 72.68  E-value: 1.41e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764   387 VENAFIHGIEPKEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDFT---QEHNGHTTGMGIKSVVERLELMy 463
Cdd:smart00387  10 LSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRtdkRSRKIGGTGLGLSIVKKLVELH- 88
                           90       100
                   ....*....|....*....|....*
gi 543000764   464 EGKniFEIKSQKRVGTKIYLKIPIK 488
Cdd:smart00387  89 GGE--ISVESEPGGGTTFTITLPLE 111
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
353-488 8.92e-12

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 67.30  E-value: 8.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 353 FIQQLRYGDRVSFILNINADLSKVKIPGMTLQPFVENAFIHGIEPKEEGGTIIIDIHEE-DGSCIIIVEDNGCGIDEETL 431
Cdd:PRK11360 471 LFQTAGVQARVDFETELDNELPPIWADPELLKQVLLNILINAVQAISARGKIRIRTWQYsDGQVAVSIEDNGCGIDPELL 550
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 543000764 432 SKITSEDFTQEHNGhtTGMGIkSVVERLELMYEGkNIfEIKSQKRVGTKIYLKIPIK 488
Cdd:PRK11360 551 KKIFDPFFTTKAKG--TGLGL-ALSQRIINAHGG-DI-EVESEPGVGTTFTLYLPIN 602
spIIAB TIGR01925
anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates ...
364-484 5.08e-06

anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates spore development in B subtilis. SpoIIAB binds to sigma F, preventing formation of the transcription complex at the promoter. SpoIIAA (anti-anti-sigma F factor) binds to SpoIIAB to inhibit association with sigma F, however SpoIIAB can phosphorylate SpoIIAA, causing disassociation of the SpoIIAA/B complex. The SpoIIE phosphatase dephosphorylates SpoIIAA. [Regulatory functions, Protein interactions, Cellular processes, Sporulation and germination]


Pssm-ID: 130980 [Multi-domain]  Cd Length: 137  Bit Score: 46.07  E-value: 5.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764  364 SFILNINADLSKVKIPGMTLQPFVENAFIHGIEpKEEGGTIIIDIHEEDGSCIIIVEDNGCGIdeETLSKITSEDFTQEH 443
Cdd:TIGR01925  25 SFIAQLDPTMEELTDIKTAVSEAVTNAIIHGYE-ENCEGVVYISATIEDHEVYITVRDEGIGI--ENLEEAREPLYTSKP 101
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 543000764  444 NGHTTGMGiksvverLELMYEGKNIFEIKSQKRVGTKIYLK 484
Cdd:TIGR01925 102 ELERSGMG-------FTVMENFMDDVSVDSEKEKGTKIIMK 135
 
Name Accession Description Interval E-value
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
28-489 4.61e-80

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 256.48  E-value: 4.61e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764  28 ISLVMSKRINDHYNIMLNKMSTTNQIKSYLTDSFNNFNKYIQTNTAQSKKIYEDSYNKAALNLNYLKANSDLDSRYILRD 107
Cdd:COG2972    1 LSKSLSLLSIVLLLLILLLLVLLILLLSLLLIILLLLLLLILLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLALL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 108 LENSLGSYKASADETIKIHDDQNNIDAYYSGYVNTKDIASYCNVFIGKLSDSYLNYNSEI----YNKLKEKEKFIYKVLA 183
Cdd:COG2972   81 LILLLLLLLLLLLILLLSLLLLLALILLLALLLLLSILLLILGLLLIILLLLSLLGWTLVslipKSELFRGLFSLRRLIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 184 AYIGVALLISIFYTLLFLRNILSKLRELVDTSEKVSSGDFTYYEGRKIDiyELDILSAAFSTMISNIKDHINTLKETAEL 263
Cdd:COG2972  161 LIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKVEKGDLVRLEVSGND--EIGILARSFNEMVERIKELIEEVYELELE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 264 QKKIsddemkllkyentlklsQLKVLQSQINPHFLFNTLNCINQTAIKENALSTESLIRSVSGILRYSLSMMNRYATLEQ 343
Cdd:COG2972  239 KKEA-----------------ELKALQAQINPHFLFNTLNSIRWLAELEDPEEAEEMLEALSKLLRYSLSKGDELVTLEE 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 344 EIEIIKQYMFIQQLRYGDRVSFILNINADLSKVKIPGMTLQPFVENAFIHGIEPKEEGGTIIIDIHEEDGSCIIIVEDNG 423
Cdd:COG2972  302 ELELIKSYLEIQKLRFGDRLEVEIEIDEELLDLLIPKLILQPLVENAIEHGIEPKEGGGTIRISIRKEGDRLVITVEDNG 381
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543000764 424 CGIDEETLSKITSEDftqEHNGHTTGMGIKSVVERLELMYEGKNIFEIKSQKRVGTKIYLKIPIKG 489
Cdd:COG2972  382 VGMPEEKLEKLLEEL---SSKGEGRGIGLRNVRERLKLYYGEEYGLEIESEPGEGTTVTIRIPLEE 444
LytS COG3275
Sensor histidine kinase, LytS/YehU family [Signal transduction mechanisms];
132-488 7.86e-62

Sensor histidine kinase, LytS/YehU family [Signal transduction mechanisms];


Pssm-ID: 442506 [Multi-domain]  Cd Length: 352  Bit Score: 205.87  E-value: 7.86e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 132 IDAYYSGYVNTKDIASYCNVFIGKLSDSYLNYNSEIYNKLKEKEKFIYKVLAAYIGVALLISIFYTLLFLRNILSKLREL 211
Cdd:COG3275    7 LLLLLLLLLLLLLLLLSLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 212 VDTSEKVSSGDFTYYEGRKIDIYELDILSAAFSTMISNIKDHINTLKETAELQKKISDDEMKLLKYENTLKLSQLKVLQS 291
Cdd:COG3275   87 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLILILLALLLSLQEEELELEELEKELLEAELKALKA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 292 QINPHFLFNTLNCInQTAIKENALSTESLIRSVSGILRYSLSMMNR-YATLEQEIEIIKQYMFIQQLRYGDRVSFILNIN 370
Cdd:COG3275  167 QINPHFLFNTLNSI-YSLIREDPEKARELLLKLSDLLRYSLYESDKeLVPLEEELEFLENYLELEKLRFGDRLQVEIDID 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 371 ADLSKVKIPGMTLQPFVENAFIHGIEPKEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKitsedftqehnghTTGM 450
Cdd:COG3275  246 EELLDLLIPPLLLQPLVENAIKHGISSKEGGGTISISIEVEGDRLVIEVENNGVGIQPKKKKK-------------GSGI 312
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 543000764 451 GIKSVVERLELMYEGKNIFEIKSQKRVGTKIYLKIPIK 488
Cdd:COG3275  313 GLKNVRERLELLYGDKYSLEIESTDGGGTKVTLKIPLK 350
His_kinase pfam06580
Histidine kinase; This family represents a region within bacterial histidine kinase enzymes. ...
284-363 1.80e-26

Histidine kinase; This family represents a region within bacterial histidine kinase enzymes. Two-component signal transduction systems such as those mediated by histidine kinase are integral parts of bacterial cellular regulatory processes, and are used to regulate the expression of genes involved in virulence. Members of this family often contain pfam02518 and/or pfam00672.


Pssm-ID: 461952 [Multi-domain]  Cd Length: 79  Bit Score: 102.13  E-value: 1.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764  284 SQLKVLQSQINPHFLFNTLNCINQTAIKENALsTESLIRSVSGILRYSLSMMNRYATLEQEIEIIKQYMFIQQLRYGDRV 363
Cdd:pfam06580   1 AELKALQAQINPHFLFNTLNSISSLAIEDPEE-AAEMILKLSDLLRYSLYEGEELVTLEEELEFLENYLEIQKIRFGDRL 79
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
378-486 6.02e-17

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: 76.33  E-value: 6.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 378 IPGMTLQPFVENAFIHGIEPKEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEetlsKITSEDFTQEHNGhtTGMGIKSVVE 457
Cdd:cd16924    1 IPPFTLQPLVENAIQHGLSPLTDKGVVTISALKEDNHVMIEVEDNGRGIDP----KVLNILGKKPKEG--NGIGLYNVHQ 74
                         90       100
                 ....*....|....*....|....*....
gi 543000764 458 RLELMYEGKNIFEIKSQKRVGTKIYLKIP 486
Cdd:cd16924   75 RLILLFGEDYGIHIASEPDKGTRITFTIP 103
HATPase_YpdA-like cd16955
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
378-486 2.63e-16

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli YpdA, a HK of the two-component system (TCS) YpdA-YpdB which is involved in a nutrient sensing regulatory network with YehU-YehT. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and some have a GAF sensor domain; some contain a DUF3816 domain; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340431 [Multi-domain]  Cd Length: 102  Bit Score: 74.42  E-value: 2.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 378 IPGMTLQPFVENAFIHGIEPKEEGGTIIIDIHEEDGSCIII-VEDNGCGIDEETLSKItsedftQEHNGHTTGMGIKSVV 456
Cdd:cd16955    1 IPKLMIQPLVENAIVHGIQEKKGKGVVKISVKKQLKNRLHIaVEDNGIGISPKVIERV------EQDEMPGNKIGLLNVH 74
                         90       100       110
                 ....*....|....*....|....*....|.
gi 543000764 457 ERLELMY-EGKNIFEIKSQkrvGTKIYLKIP 486
Cdd:cd16955   75 QRLKLGYgEGLHIRSRPDP---GTLIAFYIP 102
HATPase_YehU-like cd16956
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
378-486 8.29e-16

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YehU; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) including Escherichia coli YehU, a HK of the two-component system (TCS) YehU-YehT which is involved in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase); some have a GAF sensor domain while some have a cupin domain.


Pssm-ID: 340432 [Multi-domain]  Cd Length: 101  Bit Score: 72.85  E-value: 8.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 378 IPGMTLQPFVENAFIHGIEPKEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDftqehnghTTGMGIKSVVE 457
Cdd:cd16956    1 LPFLTLQPIVENAVKHGLSGLLDGGRVEITARLDGQHLLLEVEDNGGGMDPDTLARILIRS--------SNGLGLNLVDK 72
                         90       100
                 ....*....|....*....|....*....
gi 543000764 458 RLELMYEGKNIFEIKSQKRVGTKIYLKIP 486
Cdd:cd16956   73 RLRQAFGNDYGLDIECAPGEGTRITIRLP 101
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
387-488 1.41e-15

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 72.68  E-value: 1.41e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764   387 VENAFIHGIEPKEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDFT---QEHNGHTTGMGIKSVVERLELMy 463
Cdd:smart00387  10 LSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRtdkRSRKIGGTGLGLSIVKKLVELH- 88
                           90       100
                   ....*....|....*....|....*
gi 543000764   464 EGKniFEIKSQKRVGTKIYLKIPIK 488
Cdd:smart00387  89 GGE--ISVESEPGGGTTFTITLPLE 111
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
378-486 5.76e-14

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis LytS and Staphylococcus aureus LytS; 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. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and a GAF sensor domain; most contain a DUF3816 domain.


Pssm-ID: 340433 [Multi-domain]  Cd Length: 106  Bit Score: 67.84  E-value: 5.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 378 IPGMTLQPFVENAFIHGIEPKEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDFTQEHNghtTGMGIKSVVE 457
Cdd:cd16957    1 VPPFALQVLVENAIRHAFPKRKENNEVRVVVKKDQHKVHVSVSDNGQGIPEERLDLLGKTTVTSEKG---TGTALENLNR 77
                         90       100
                 ....*....|....*....|....*....
gi 543000764 458 RLELMYEGKNIFEIKSQKRVGTKIYLKIP 486
Cdd:cd16957   78 RLIGLFGSEACLHIESEVHGGTEVWFVIP 106
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
176-492 7.74e-13

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: 69.99  E-value: 7.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 176 KFIYKVLAAYIGVALLISIFYTLLFLRNILSKLRELVDTSEKVSSGDFTyyegRKIDIY---ELDILSAAFSTMISNIKD 252
Cdd:COG5000    5 ILFLLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDLS----VRLPVTgddEIGELARAFNRMTDQLKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 253 HINTLKETAELQKKI----------SDDEMKLLKY----ENTLKLSQLKVLQ---SQINPHFLF---------------- 299
Cdd:COG5000   81 QREELEERRRYLETIlenlpagvivLDADGRITLAnpaaERLLGIPLEELIGkplEELLPELDLaellrealergwqeei 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 300 -------NTLNC----------------INQ-------------------------TAIKenaLSTESLIRSVSGILRYS 331
Cdd:COG5000  161 eltrdgrRTLLVrasplrddgyvivfddITEllraerlaawgelarriaheiknplTPIQ---LSAERLRRKLADKLEED 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 332 LSMMNRY-ATLEQEIEIIKQymFIQQLR------------------------------YGDRVSFILNINADLSKVKI-P 379
Cdd:COG5000  238 REDLERAlDTIIRQVDRLKR--IVDEFLdfarlpepqlepvdlnellrevlalyepalKEKDIRLELDLDPDLPEVLAdR 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 380 GMTLQPF---VENAfihgIEPKEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDFTQEHNGhtTGMG---IK 453
Cdd:COG5000  316 DQLEQVLinlLKNA----IEAIEEGGEIEVSTRREDGRVRIEVSDNGPGIPEEVLERIFEPFFTTKPKG--TGLGlaiVK 389
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 543000764 454 SVVErlelMYEGKniFEIKSQKRVGTKIYLKIPIKGLGE 492
Cdd:COG5000  390 KIVE----EHGGT--IELESRPGGGTTFTIRLPLAEEAE 422
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
177-487 9.30e-13

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 69.17  E-value: 9.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 177 FIYKVLAAYIGVALLISIFYTLLFLRNILSKLRELVDTSEKVSSGDFTYYEGRKIDIYELDILSAAFSTMIS-NIKDHIN 255
Cdd:COG0642   47 LLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVShELRTPLT 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 256 TLKETAELQKKISDDEMKllKYENTLkLSQLKVLQSQINpHFLFntlncinqtaikenalstesLIRSVSGILRYSLSMM 335
Cdd:COG0642  127 AIRGYLELLLEELDEEQR--EYLETI-LRSADRLLRLIN-DLLD--------------------LSRLEAGKLELEPEPV 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 336 NRYATLEQEIEIIkqymfiQQLRYGDRVSFILNINADLSKVKIPGMTLQP----FVENAFIHGiepkEEGGTIIIDIHEE 411
Cdd:COG0642  183 DLAELLEEVVELF------RPLAEEKGIELELDLPDDLPTVRGDPDRLRQvllnLLSNAIKYT----PEGGTVTVSVRRE 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 412 DGSCIIIVEDNGCGIDEETLSKITsEDFTQEHNGHT---TGMGIkSVVERL-ELMyEGKniFEIKSQKRVGTKIYLKIPI 487
Cdd:COG0642  253 GDRVRISVEDTGPGIPPEDLERIF-EPFFRTDPSRRgggTGLGL-AIVKRIvELH-GGT--IEVESEPGKGTTFTVTLPL 327
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
387-488 1.80e-12

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: 63.54  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764  387 VENAFIHGIEPKEEGGTIIIDIHEEDGsCIIIVEDNGCGIDEETLSKITsEDFTQEHNGHT--TGMGIkSVVERLELMYE 464
Cdd:pfam02518  10 LSNLLDNALKHAAKAGEITVTLSEGGE-LTLTVEDNGIGIPPEDLPRIF-EPFSTADKRGGggTGLGL-SIVRKLVELLG 86
                          90       100
                  ....*....|....*....|....
gi 543000764  465 GKniFEIKSQKRVGTKIYLKIPIK 488
Cdd:pfam02518  87 GT--ITVESEPGGGTTVTLTLPLA 108
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
353-488 8.92e-12

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 67.30  E-value: 8.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 353 FIQQLRYGDRVSFILNINADLSKVKIPGMTLQPFVENAFIHGIEPKEEGGTIIIDIHEE-DGSCIIIVEDNGCGIDEETL 431
Cdd:PRK11360 471 LFQTAGVQARVDFETELDNELPPIWADPELLKQVLLNILINAVQAISARGKIRIRTWQYsDGQVAVSIEDNGCGIDPELL 550
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 543000764 432 SKITSEDFTQEHNGhtTGMGIkSVVERLELMYEGkNIfEIKSQKRVGTKIYLKIPIK 488
Cdd:PRK11360 551 KKIFDPFFTTKAKG--TGLGL-ALSQRIINAHGG-DI-EVESEPGVGTTFTLYLPIN 602
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
387-487 1.67e-11

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 64.16  E-value: 1.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 387 VENAFIHGiepkEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDFTQEHNGHTTGMGI-----KSVVERlel 461
Cdd:COG2205  141 LDNAIKYS----PPGGTITISARREGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRGEGGTGLglaivKRIVEA--- 213
                         90       100
                 ....*....|....*....|....*.
gi 543000764 462 mYEGKniFEIKSQKRVGTKIYLKIPI 487
Cdd:COG2205  214 -HGGT--IWVESEPGGGTTFTVTLPL 236
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
387-489 2.48e-11

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 65.26  E-value: 2.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 387 VENAFIHGIEPKEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDF-TQEHNGHttGMG---IKSVVERlelm 462
Cdd:COG3290  290 LDNAIEAVEKLPEEERRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFERGFsTKLGEGR--GLGlalVKQIVEK---- 363
                         90       100
                 ....*....|....*....|....*..
gi 543000764 463 YEGKniFEIKSQKRVGTKIYLKIPIKG 489
Cdd:COG3290  364 YGGT--IEVESEEGEGTVFTVRLPKEG 388
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
182-488 2.09e-10

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 62.12  E-value: 2.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 182 LAAYIGVALLISIFYTLLFLRNILSKLRELVDTSEKVSSGDFTYYEGRKIDIYELDILSAAFSTMISNIKDHINTLKETA 261
Cdd:COG4191   27 LLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALLLLLLAALDAEEN 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 262 ELQKKISDDEMKLLKYENTLKLSQLKVLQSQ---------------INphflfNTLNCI---------------NQTAIK 311
Cdd:COG4191  107 AELEELERDITELERAEEELRELQEQLVQSEklaalgelaagiaheIN-----NPLAAIlgnaellrrrledepDPEELR 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 312 ENALSTESLIRSVSGILRySLSMMNRYATLEQEI----EIIKQYMFI--QQLRYGdRVSFILNINADLSKVKI-PGMTLQ 384
Cdd:COG4191  182 EALERILEGAERAAEIVR-SLRAFSRRDEEEREPvdlnELIDEALELlrPRLKAR-GIEVELDLPPDLPPVLGdPGQLEQ 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 385 PF---VENAfIHGIEPKEEGgTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDFTQEHNGHTTGMG---IKSVVER 458
Cdd:COG4191  260 VLlnlLINA-IDAMEEGEGG-RITISTRREGDYVVISVRDNGPGIPPEVLERIFEPFFTTKPVGKGTGLGlsiSYGIVEK 337
                        330       340       350
                 ....*....|....*....|....*....|
gi 543000764 459 lelmYEGKniFEIKSQKRVGTKIYLKIPIK 488
Cdd:COG4191  338 ----HGGR--IEVESEPGGGTTFTITLPLA 361
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
362-488 3.19e-10

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 61.88  E-value: 3.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 362 RVSFILNINADLSKVKI-PGMTLQPF---VENAFIHGiepkEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITsE 437
Cdd:COG5002  261 GIELELDLPEDPLLVLGdPDRLEQVLtnlLDNAIKYT----PEGGTITVSLREEDDQVRISVRDTGIGIPEEDLPRIF-E 335
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 543000764 438 DFTQEHNGHT-----TGMG--I-KSVVERlelmYEGKniFEIKSQKRVGTKIYLKIPIK 488
Cdd:COG5002  336 RFYRVDKSRSretggTGLGlaIvKHIVEA----HGGR--IWVESEPGKGTTFTITLPLA 388
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
363-488 3.70e-10

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 62.06  E-value: 3.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 363 VSFILNINADLSKVKIPGMTLQPFVENAFIHGIEPKEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDFTQE 442
Cdd:COG5805  376 IQIRLELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNGGTITIHTEEEDNSVIIRVIDEGIGIPEERLKKLGEPFFTTK 455
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 543000764 443 HNGhtTGMGI---KSVVERlelmyeGKNIFEIKSQKRVGTKIYLKIPIK 488
Cdd:COG5805  456 EKG--TGLGLmvsYKIIEN------HNGTIDIDSKVGKGTTFTITLPLS 496
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
186-461 1.61e-09

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 60.51  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 186 IGVALLISIFYTLLFLRNILSKLRELVDTSEKVSSGDFTyyegRKIDIY---ELDILSAAFSTMISNIKDHINTLKETAE 262
Cdd:COG2770  218 ALLALLLALLLALLLARRITRPLRRLAEAARRIAAGDLD----VRIPVSrkdEIGELARAFNRMADSLRESIEEAEEEEE 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 263 LQKKISDDEMKLLKYENTLKLSQLKVLQSQINPHFLFNTLNCINQTAIKENALSTESLIRSVSGILRYSLSMMNRYATLE 342
Cdd:COG2770  294 LAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAEL 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 343 QEIEIIKQYMFIQQLRYGDRVSFILNINADLSKVKIPGMTLQPFVENAFIHGIEPKEEGGTIIIDIHEEDGSCIIIVEDN 422
Cdd:COG2770  374 LVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEA 453
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 543000764 423 GCGIDEETLSKITSEDFTQEHNGHTTGMGIKSVVERLEL 461
Cdd:COG2770  454 EGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLL 492
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
394-488 6.85e-09

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 58.06  E-value: 6.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 394 GIEPKEEGGTIIIDIHEEDGSCIII-VEDNGCGIDEETLSKITSEDFTQEHNGhtTGMGIkSVVERLELMYEGKniFEIK 472
Cdd:COG5809  391 AIEAMPEGGNITIETKAEDDDKVVIsVTDEGCGIPEERLKKLGEPFYTTKEKG--TGLGL-MVSYKIIEEHGGK--ITVE 465
                         90
                 ....*....|....*.
gi 543000764 473 SQKRVGTKIYLKIPIK 488
Cdd:COG5809  466 SEVGKGTTFSITLPIK 481
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
387-486 5.58e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 50.75  E-value: 5.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 387 VENAFIHGIEPKEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDF-TQEHNGHTTGMG-IKSVVERLelmyE 464
Cdd:cd16915    9 IDNALDALAATGAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFERGVsTKGQGERGIGLAlVRQSVERL----G 84
                         90       100
                 ....*....|....*....|..
gi 543000764 465 GKniFEIKSQKRVGTKIYLKIP 486
Cdd:cd16915   85 GS--ITVESEPGGGTTFSIRIP 104
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
389-487 2.47e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; 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 AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 48.96  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 389 NAFIHGIEPKEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDFTQEHNGHTTGMGIkSVVERLELMYEGKni 468
Cdd:cd16943   10 NLLVNAAQAMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFFTTKPVGEGTGLGL-SLSYRIIQKHGGT-- 86
                         90
                 ....*....|....*....
gi 543000764 469 FEIKSQKRVGTKIYLKIPI 487
Cdd:cd16943   87 IRVASVPGGGTRFTIILPI 105
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
308-489 4.37e-07

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 51.16  E-value: 4.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 308 TAIKENALSTESLIRSVSGILRYS-LSMMNRYATLEQEIEIIKQymfiqqlRYGDRVSFILNINADlskvkipgmTLQPF 386
Cdd:COG4585   95 EEIRELAREALAELRRLVRGLRPPaLDDLGLAAALEELAERLLR-------AAGIRVELDVDGDPD---------RLPPE 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 387 VE------------NAFIHGiepkeEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKitsedftqehnghtTGMGIKS 454
Cdd:COG4585  159 VElalyrivqealtNALKHA-----GATRVTVTLEVDDGELTLTVRDDGVGFDPEAAPG--------------GGLGLRG 219
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 543000764 455 VVERLELMyEGKniFEIKSQKRVGTKIYLKIPIKG 489
Cdd:COG4585  220 MRERAEAL-GGT--LTIGSAPGGGTRVRATLPLAA 251
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
42-262 3.11e-06

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 49.63  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764  42 IMLNKMSTTNQIKSYLTDSFNNFNKYIQTNTAQSKKIYEDSYNKAALNLNYLKANSDLDSRYILRDLENSLGSYKASADE 121
Cdd:COG0840   44 ALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLALLALALAALALLAALAALLALLELLLAAL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 122 TIKIHDDQNNIDAYYSGYVNTKDIASYCNVFIGKLSDSYLNYNSEIYNKLKEKEKFIYKVLAAYIGVALLISIFYTLLFL 201
Cdd:COG0840  124 LAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALALLAAALLALVALAIILALLLS 203
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543000764 202 RNILSKLRELVDTSEKVSSGDFTyyegRKIDIY---ELDILSAAFSTMISNIKDHINTLKETAE 262
Cdd:COG0840  204 RSITRPLRELLEVLERIAEGDLT----VRIDVDskdEIGQLADAFNRMIENLRELVGQVRESAE 263
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
381-466 3.11e-06

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 49.20  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 381 MTLQPFVENAfiHGIEPkeEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITsEDFT---QEHNGhtTGMGIkSVVE 457
Cdd:PRK10755 250 LLLRNLVENA--HRYSP--EGSTITIKLSQEDGGAVLAVEDEGPGIDESKCGELS-KAFVrmdSRYGG--IGLGL-SIVS 321

                 ....*....
gi 543000764 458 RLELMYEGK 466
Cdd:PRK10755 322 RITQLHHGQ 330
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
387-486 3.13e-06

Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some hybrid sensor histidine kinases; This family includes the cytoplasmic histidine kinase (HK) CheA, a transmembrane receptor which, together with cytoplasmic adaptor protein (CheW), forms the lattice at the core of the chemosensory array that controls the cellular chemotaxis of motile bacteria and archaea. CheA forms a two-component signal transduction system (TCS) with the response regulator CheY. Proteins having this CheA-like HATPase domain generally also have a histidine-phosphotransfer domain, a histidine kinase homodimeric domain, and a regulatory domain; some are hybrid sensor histidine kinases as they contain a REC signal receiver domain.


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 47.58  E-value: 3.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 387 VENAFIHGIEP--------KEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSK------ITSEDFTQE---------- 442
Cdd:cd16916   47 LRNAVDHGIEApeerlaagKPPEGTITLRAEHQGNQVVIEVSDDGRGIDREKIREkaiergLITADEAATlsddevlnli 126
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 543000764 443 -HNGHTT------------GMGI-KSVVERLelmyeGKNIfEIKSQKRVGTKIYLKIP 486
Cdd:cd16916  127 fAPGFSTaeqvtdvsgrgvGMDVvKRSIESL-----GGTI-EVESEPGQGTTFTIRLP 178
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
387-484 4.73e-06

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: 45.99  E-value: 4.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 387 VENAFIHGIEpKEEGGTIIIDIHEEDGSCIIIVEDNGCGIdeETLSKITSEDFTQEHNGHTTGMGiksvverLELMYEGK 466
Cdd:cd16942   47 VTNAIIHGYN-NDPNGIVSISVIIEDGVVHLTVRDEGVGI--PDIEEARQPLFTTKPELERSGMG-------FTIMENFM 116
                         90
                 ....*....|....*...
gi 543000764 467 NIFEIKSQKRVGTKIYLK 484
Cdd:cd16942  117 DEVIVESEVNKGTTVYLK 134
spIIAB TIGR01925
anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates ...
364-484 5.08e-06

anti-sigma F factor; This model describes the SpoIIAB anti-sigma F factor. Sigma F regulates spore development in B subtilis. SpoIIAB binds to sigma F, preventing formation of the transcription complex at the promoter. SpoIIAA (anti-anti-sigma F factor) binds to SpoIIAB to inhibit association with sigma F, however SpoIIAB can phosphorylate SpoIIAA, causing disassociation of the SpoIIAA/B complex. The SpoIIE phosphatase dephosphorylates SpoIIAA. [Regulatory functions, Protein interactions, Cellular processes, Sporulation and germination]


Pssm-ID: 130980 [Multi-domain]  Cd Length: 137  Bit Score: 46.07  E-value: 5.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764  364 SFILNINADLSKVKIPGMTLQPFVENAFIHGIEpKEEGGTIIIDIHEEDGSCIIIVEDNGCGIdeETLSKITSEDFTQEH 443
Cdd:TIGR01925  25 SFIAQLDPTMEELTDIKTAVSEAVTNAIIHGYE-ENCEGVVYISATIEDHEVYITVRDEGIGI--ENLEEAREPLYTSKP 101
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 543000764  444 NGHTTGMGiksvverLELMYEGKNIFEIKSQKRVGTKIYLK 484
Cdd:TIGR01925 102 ELERSGMG-------FTVMENFMDDVSVDSEKEKGTKIIMK 135
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
369-492 5.81e-06

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 48.75  E-value: 5.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 369 INADLSKVKIPGMTLQPF-------VENAFIHGIePKEEGGTIIIDIHEEDGSCIIIVEDNGCGIDeetlskitsEDFTQ 441
Cdd:COG3920  383 IELDGPDVELPADAAVPLglilnelVTNALKHAF-LSGEGGRIRVSWRREDGRLRLTVSDNGVGLP---------EDVDP 452
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 543000764 442 EhngHTTGMG---IKSVVERLelmyEGKniFEIKSQKrvGTKIYLKIPIKGLGE 492
Cdd:COG3920  453 P---ARKGLGlrlIRALVRQL----GGT--LELDRPE--GTRVRITFPLAELAA 495
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
400-480 2.10e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 43.43  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 400 EGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDFTQEhNGHT----TGMGI---KSVVERLelmyeGKNIfEIK 472
Cdd:cd16948   23 QGGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGFTGE-NGRNfqesTGMGLylvKKLCDKL-----GHKI-DVE 95

                 ....*...
gi 543000764 473 SQKRVGTK 480
Cdd:cd16948   96 SEVGEGTT 103
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
346-488 2.75e-05

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 46.38  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 346 EIIKQYMFIQQLRYGDRVSFILNINADLSKVKI-PGMTLQPFVeNAFIHGIEPKEEGGTIIIDIHEEDGSCI-------- 416
Cdd:COG3852  208 EVLERVLELLRAEAPKNIRIVRDYDPSLPEVLGdPDQLIQVLL-NLVRNAAEAMPEGGTITIRTRVERQVTLgglrprly 286
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543000764 417 --IIVEDNGCGIDEETLSKITseD--FTQEHNGhtTGMGI---KSVVERlelmYEGKnIfEIKSQKRVGTKIYLKIPIK 488
Cdd:COG3852  287 vrIEVIDNGPGIPEEILDRIF--EpfFTTKEKG--TGLGLaivQKIVEQ----HGGT-I-EVESEPGKGTTFRIYLPLE 355
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
389-487 3.26e-05

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 46.33  E-value: 3.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 389 NAFIHGIEPKEE----G----GTIIIDIHEEDGSCIIIVEDNGCGID---------------EETLSKITSED-----Ft 440
Cdd:COG0643  288 NAVDHGIETPEErlaaGkpetGTITLSAYHEGGRVVIEVSDDGRGLDlekirakaiekglitAEEAAALSDEElleliF- 366
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 441 qeHNGHTT----------GMG---IKSVVERLelmyeGKNIfEIKSQKRVGTKIYLKIPI 487
Cdd:COG0643  367 --APGFSTaeevtdlsgrGVGmdvVKTNIEAL-----GGTI-EIESEPGKGTTFTLRLPL 418
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
387-459 4.17e-05

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 42.98  E-value: 4.17e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543000764 387 VENAFIHGiEPKEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDFtqehnghTTGMGIkSVVERL 459
Cdd:COG2172   43 VTNAVRHA-YGGDPDGPVEVELELDPDGLEIEVRDEGPGFDPEDLPDPYSTLA-------EGGRGL-FLIRRL 106
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
402-486 4.31e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 42.48  E-value: 4.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 402 GTIIIDIH---EEDGSCIII--VEDNGCGIDEETLSKITsEDFTQEHNGHT-----TGMGIkSVVERL-ELMyeGKNIfE 470
Cdd:cd16922   19 GEVTLRVSleeEEEDGVQLRfsVEDTGIGIPEEQQARLF-EPFSQADSSTTrkyggTGLGL-AISKKLvELM--GGDI-S 93
                         90
                 ....*....|....*.
gi 543000764 471 IKSQKRVGTKIYLKIP 486
Cdd:cd16922   94 VESEPGQGSTFTFTLP 109
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
387-488 5.31e-05

Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 45.55  E-value: 5.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 387 VENAFIHGiePKEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKI--------TSEDFTqehnGhtTGMG---IKSV 455
Cdd:COG4251  403 ISNAIKYS--RPGEPPRIEIGAEREGGEWVFSVRDNGIGIDPEYAEKIfeifqrlhSRDEYE----G--TGIGlaiVKKI 474
                         90       100       110
                 ....*....|....*....|....*....|...
gi 543000764 456 VERlelmYEGKniFEIKSQKRVGTKIYLKIPIK 488
Cdd:COG4251  475 VER----HGGR--IWVESEPGEGATFYFTLPKA 501
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
202-255 7.22e-05

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 40.31  E-value: 7.22e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 543000764   202 RNILSKLRELVDTSEKVSSGDFTyyegRKIDIY---ELDILSAAFSTMISNIKDHIN 255
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLT----VRLPVDgrdEIGELARAFNEMADRLEETIA 53
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
381-483 7.95e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 42.01  E-value: 7.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 381 MTLQPFVENAfiHGIEPkeEGGTIIIDIHEEDGScIIIVEDNGCGIDEETLSKItSEDFTQEHNGHTTGMGIK-SVVERL 459
Cdd:cd16940   16 LLLRNLVDNA--VRYSP--QGSRVEIKLSADDGA-VIRVEDNGPGIDEEELEAL-FERFYRSDGQNYGGSGLGlSIVKRI 89
                         90       100
                 ....*....|....*....|....
gi 543000764 460 ELMYEGKNIFEIKSQKRVGTKIYL 483
Cdd:cd16940   90 VELHGGQIFLGNAQGGGLEAWVRL 113
PRK10935 PRK10935
nitrate/nitrite two-component system sensor histidine kinase NarQ;
180-303 1.56e-04

nitrate/nitrite two-component system sensor histidine kinase NarQ;


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 44.07  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 180 KVLAAYIGVAL---LISIFYTLLFLR-NILSKLRELVDTSEKVSSGDFTYYEGRKIDIYELDILSAAFSTMisnikdhin 255
Cdd:PRK10935 148 ILLAAISLLGLiliLTLVFFTVRFTRrQVVAPLNQLVTASQQIEKGQFDHIPLDTTLPNELGLLAKAFNQM--------- 218
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 256 tlkeTAELQKKISDDEMKLlkYENTLKLSQ----LKVL--------QSQINPHFLFNTLN 303
Cdd:PRK10935 219 ----SSELHKLYRSLEASV--EEKTRKLTQanrsLEVLyqcsqalnASQIDVHCFRHILQ 272
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
398-489 3.01e-04

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 43.36  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 398 KEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDFTQEHNGHTTGMG-IKSVVERLelmyEGKNIFEikSQKR 476
Cdd:PRK11086 451 GEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFDKGYSTKGSNRGVGLYlVKQSVENL----GGSIAVE--SEPG 524
                         90
                 ....*....|...
gi 543000764 477 VGTKIYLKIPIKG 489
Cdd:PRK11086 525 VGTQFFVQIPWDG 537
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
208-250 1.48e-03

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 36.27  E-value: 1.48e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 543000764 208 LRELVDTSEKVSSGDFTYyegrKIDIY---ELDILSAAFSTMISNI 250
Cdd:cd06225    4 LRRLTEAARRIAEGDLDV----RVPVRskdEIGELARAFNQMAERL 45
PRK15347 PRK15347
two component system sensor kinase;
400-495 1.54e-03

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 41.17  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 400 EGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDFTQEHNGHTTGMGIkSVVERLELMYEGKniFEIKSQKRVGT 479
Cdd:PRK15347 530 ETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQADTHSQGTGLGL-TIASSLAKMMGGE--LTLFSTPGVGS 606
                         90
                 ....*....|....*.
gi 543000764 480 KIYLKIPikgLGEYAE 495
Cdd:PRK15347 607 CFSLVLP---LNEYAP 619
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
403-438 1.56e-03

Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.


Pssm-ID: 340403 [Multi-domain]  Cd Length: 188  Bit Score: 39.73  E-value: 1.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 543000764 403 TIIIDIhEEDGSCIIIVEDNGCGIDEETL---------SKITSED 438
Cdd:cd16926   32 RIDVEI-EEGGLKLIRVTDNGSGISREDLelaferhatSKISSFE 75
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
380-486 1.89e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 37.69  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 380 GMTLQPFVENA--FIHGIEPKEeggtiiIDIHEED--GSCIIIVEDNGCGIDEETLSKItsedFT------QEHNGHTTG 449
Cdd:cd16921    2 GQVLTNLLGNAikFRRPRRPPR------IEVGAEDvgEEWTFYVRDNGIGIDPEYAEKV----FGifqrlhSREEYEGTG 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 543000764 450 MGI---KSVVERlelmyEGKNIFeIKSQKRVGTKIYLKIP 486
Cdd:cd16921   72 VGLaivRKIIER-----HGGRIW-LESEPGEGTTFYFTLP 105
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
367-486 4.59e-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: 37.40  E-value: 4.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 367 LNINADLSKVKIP-----GMTLQPFVENAFIHGIEPKEEGgTIIIDIHEEDGSCIIIVEDNGCGIDeetlskitsEDFTQ 441
Cdd:cd16951   23 INITGDTGPVSSEvataiGLVVNELLQNALKHAFSDREGG-TITIRSVVDGDYLRITVIDDGVGLP---------QDEDW 92
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 543000764 442 EHNGHTTGMGIKSVVERlelmyEGKNIFEIKSQKRvGTKIYLKIP 486
Cdd:cd16951   93 PNKGSLGLQIVRSLVEG-----ELKAFLEVQSAEN-GTRVNIDIP 131
mutL PRK00095
DNA mismatch repair endonuclease MutL;
404-438 4.91e-03

DNA mismatch repair endonuclease MutL;


Pssm-ID: 234630 [Multi-domain]  Cd Length: 617  Bit Score: 39.43  E-value: 4.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 543000764 404 IIIDIhEEDGSCIIIVEDNGCGIDEETL---------SKITSED 438
Cdd:PRK00095  42 IDIEI-EEGGLKLIRVRDNGCGISKEDLalalarhatSKIASLD 84
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
389-489 5.05e-03

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 39.38  E-value: 5.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543000764 389 NAFIHGIEPKEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDFTQEHNGhtTGMGIKSVVERLElmYEGKNI 468
Cdd:PRK10364 355 NLYLNAIQAIGQHGVISVTASESGAGVKISVTDSGKGIAADQLEAIFTPYFTTKAEG--TGLGLAVVHNIVE--QHGGTI 430
                         90       100
                 ....*....|....*....|.
gi 543000764 469 fEIKSQKRVGTKIYLKIPIKG 489
Cdd:PRK10364 431 -QVASQEGKGATFTLWLPVNI 450
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
398-459 7.00e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 36.28  E-value: 7.00e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543000764 398 KEEGGTIIIDIHEEDGSCIIIVEDNGCGIDEETLSKITSEDFTQEHNGHTTGMGIK---SVVERL 459
Cdd:cd16976   18 KVENPRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFFTTKPVGKGTGLGLSisyGIVEEH 82
 
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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