phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    5 VMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDELHVIPVIAVTA 84
Cdd:cd17548   2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALTA 81

                        90       100       110
                ....*....|....*....|....*....|...
gi 4732057   85 FAMKGDEERIRQGGCEAYVSKPISVPKFIETIK 117
Cdd:cd17548  82 YAMKGDREKILEAGCDGYISKPIDTREFLETVA 114

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    5 VMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDELHVIPVIAVTA 84
Cdd:cd17548   2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALTA 81

                        90       100       110
                ....*....|....*....|....*....|...
gi 4732057   85 FAMKGDEERIRQGGCEAYVSKPISVPKFIETIK 117
Cdd:cd17548  82 YAMKGDREKILEAGCDGYISKPIDTREFLETVA 114

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057      5 VMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDelHVIPVIAVTA 84
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRD--PTTPVIILTA 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 4732057     85 FAMKGDEERIRQGGCEAYVSKPISVPKFIETIK 117
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 4732057       5 VMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLP 57
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    5 VMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDELHVIPVIAVTA 84
Cdd:cd17548   2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALTA 81

                        90       100       110
                ....*....|....*....|....*....|...
gi 4732057   85 FAMKGDEERIRQGGCEAYVSKPISVPKFIETIK 117
Cdd:cd17548  82 YAMKGDREKILEAGCDGYISKPIDTREFLETVA 114

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    5 VMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDELHV-IPVIAVT 83
Cdd:cd17546   1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRrTPIIALT 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 4732057   84 AFAMKGDEERIRQGGCEAYVSKPISVPKFIETI 116
Cdd:cd17546  81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    2 PKQVMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDelHVIPVIA 81
Cdd:COG0745   1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARP--SDIPIIM 78

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 4732057   82 VTAFAMKGDEERIRQGGCEAYVSKPISVPKFIETIKTYL 120
Cdd:COG0745  79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALL 117

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    5 VMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDELHVIPVIAVTA 84
Cdd:cd17580   1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 4732057   85 FAMKGDEERIRQGGCEAYVSKPISVPKFIETI 116
Cdd:cd17580  81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    5 VMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDELHVIPVIAVTa 84
Cdd:cd17538   2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT- 80

                        90       100
                ....*....|....*....|....*..
gi 4732057   85 fAMKGDEERIRqgGCEA----YVSKPI 107
Cdd:cd17538  81 -ALDDREDRIR--GLEAgaddFLSKPI 104

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    4 QVMIVEDNELNMKLFRDLIEASGYTT--IQTRNGMEALDLARKH-------RPDLILMDIQLPEVSGLEVTKWLKEDDEL 74
Cdd:cd17557   1 TILLVEDNPGDAELIQEAFKEAGVPNelHVVRDGEEALDFLRGEgeyadapRPDLILLDLNMPRMDGFEVLREIKADPDL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 4732057   75 HVIPVIAVTAfamKGDEERIRQG---GCEAYVSKPISVPKFIETIKT 118
Cdd:cd17557  81 RRIPVVVLTT---SDAEEDIERAyelGANSYIVKPVDFEEFVEAIRS 124

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    5 VMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDELHVIPVIAVTA 84
Cdd:cd19920   1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80

                        90       100
                ....*....|....*....|....
gi 4732057   85 FAMKGDEER-IRQGGCEaYVSKPI 107
Cdd:cd19920  81 LTDTEDKVKgFELGAVD-YITKPF 103

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    6 MIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDelHVIPVIAVTAf 85
Cdd:cd17574   1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKG--SDIPIIMLTA- 77

                        90       100
                ....*....|....*....|....
gi 4732057   86 amKGDEERIRQG---GCEAYVSKP 106
Cdd:cd17574  78 --KDEEEDKVLGlelGADDYITKP 99

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    1 MPKQVMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDELhvIPVI 80
Cdd:COG2204   1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPD--LPVI 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 4732057   81 AVTAFAMKGDEERIRQGGCEAYVSKPISVPKFIETIKTYLGDA 123
Cdd:COG2204  79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERR 121

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    5 VMIVEDNELNMKLFRDLIE-ASGYTTIQT-RNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDelHVIPVIAV 82
Cdd:COG4753   2 VLIVDDEPLIREGLKRILEwEAGFEVVGEaENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELD--PDTKIIIL 79

                        90       100
                ....*....|....*....|....
gi 4732057   83 TAFAMKGDEERIRQGGCEAYVSKP 106
Cdd:COG4753  80 SGYSDFEYAQEAIKLGADDYLLKP 103

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    5 VMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDELHVIPVIAVTA 84
Cdd:cd19927   1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80

                        90       100
                ....*....|....*....|....
gi 4732057   85 FAMKGDeeRIR--QGGCEAYVSKP 106
Cdd:cd19927  81 KGMTSD--RIKgyNAGCDGYLSKP 102

phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes Mycobacterium tuberculosis PdtaR, also called Rv1626, and similar proteins containing a REC domain and an ANTAR (AmiR and NasR transcription antitermination regulators) RNA-binding output domain. PdtaR is a response regulator that acts at the level of transcriptional antitermination and is a member of the PdtaR/PdtaS two-component regulatory system. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    3 KQVMIVEDNELNMKLFRDLIEASGYTTI-QTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDdelHVIPVIA 81
Cdd:cd19932   1 VRVLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSE---NIAPIVL 77

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 4732057   82 VTAFAMKGDEERIRQGGCEAYVSKPISVPKFIETIKT 118
Cdd:cd19932  78 LTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEM 114

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    3 KQVMIVEDNELNMKLFRDLIEASGYTTIQT-RNGMEALDLARKHRPDLILMDIQLP-EVSGLEVTKWLKeddELHVIPVI 80
Cdd:cd17534   1 KKILIVEDEAIIALDLKEILESLGYEVVGIaDSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIR---EKFDIPVI 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 4732057   81 AVTAFAmkgDE---ERIRQGGCEAYVSKPISVPKFIETIKTYL 120
Cdd:cd17534  78 FLTAYS---DEetlERAKETNPYGYLVKPFNERELKAAIELAL 117

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    1 MPKQVMIVEDNELNMKLFRDLIEASGYTTI-QTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDElhvIPV 79
Cdd:COG3707   2 RGLRVLVVDDEPLRRADLREGLREAGYEVVaEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP---APV 78

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 4732057   80 IAVTAFAMKGDEERIRQGGCEAYVSKPISVPKFIETI 116
Cdd:COG3707  79 ILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPAL 115

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    6 MIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDELHVIPVIAVTAf 85
Cdd:cd19937   1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTA- 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 4732057   86 amKGDE-ERI--RQGGCEAYVSKPISVPKFIETIKTYL 120
Cdd:cd19937  80 --KGEEfDKVlgLELGADDYITKPFSPRELLARVKAVL 115

two component system sensor kinase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057     4 QVMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTK-WLKEDDELHV-IPVIA 81
Cdd:PRK15347 692 QILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQlWRDDPNNLDPdCMIVA 771

                         90       100
                 ....*....|....*....|....*..
gi 4732057    82 VTAFAMKGDEERIRQGGCEAYVSKPIS 108
Cdd:PRK15347 772 LTANAAPEEIHRCKKAGMNHYLTKPVT 798

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    3 KQVMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDELHVIPVIAV 82
Cdd:cd17618   1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIML 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 4732057   83 TAfamKGDEERIRQG---GCEAYVSKPISVPKFIETIKTYL 120
Cdd:cd17618  81 TA---RGEEEDKVRGleaGADDYITKPFSPRELVARIKAVL 118

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    5 VMIVEDNELNMKLFRDLIEASGYTTI--QTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEddELHVIPVIAV 82
Cdd:cd19930   1 VLIAEDQEMVRGALAALLELEDDLEVvaQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELRE--ELPDTKVLIV 78

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 4732057   83 TAFAMKGDEERIRQGGCEAYVSKPISVPKFIETIKT 118
Cdd:cd19930  79 TTFGRPGYFRRALAAGVDGYVLKDRPIEELADAIRT 114

DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    5 VMIVEDNELNMKLFRDLIEASGYTTI--QTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDelHVIPVIAV 82
Cdd:COG3279   4 ILIVDDEPLARERLERLLEKYPDLEVvgEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELD--PPPPIIFT 81

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 4732057   83 TAF---AMKGdeerIRQGGCeAYVSKPISVPKFIETIK 117
Cdd:COG3279  82 TAYdeyALEA----FEVNAV-DYLLKPIDEERLAKALE 114

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    3 KQVMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDElhVIPVIAV 82
Cdd:cd17554   1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKP--DLPVIIC 78

                ...
gi 4732057   83 TAF 85
Cdd:cd17554  79 TAY 81

acetoacetate metabolism transcriptional regulator AtoC;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057     5 VMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDElhVIPVIAVTA 84
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHET--RTPVILMTA 84

                         90       100
                 ....*....|....*....|...
gi 4732057    85 FA-MKGDEERIRQGGCEaYVSKP 106
Cdd:PRK11361  85 YAeVETAVEALRCGAFD-YVIKP 106

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    5 VMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDElhvIPVIAVTA 84
Cdd:cd17620   1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSA---VPVIVLSA 77

                        90       100
                ....*....|....*....|..
gi 4732057   85 FAMKGDEERIRQGGCEAYVSKP 106
Cdd:cd17620  78 RDEESDKIAALDAGADDYLTKP 99

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    5 VMIVEDNELNMKLFRDLIEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDELhvIPVIAVTA 84
Cdd:cd17627   1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGND--LPILVLTA 78

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 4732057   85 FAMKGDEERIRQGGCEAYVSKPISVPKFIETIKTYL 120
Cdd:cd17627  79 RDSVSDRVAGLDAGADDYLVKPFALEELLARVRALL 114

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    5 VMIVEDNELNMKLFRDLIEASGYTTI--QTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDelHVIPVIAV 82
Cdd:cd17532   1 ALIVDDEPLAREELRYLLEEHPDIEIvgEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLA--KPPLIVFV 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 4732057   83 TA---FAMKGDEErirqggcEA--YVSKPISVPKFIETIK 117
Cdd:cd17532  79 TAydeYAVEAFEL-------NAvdYLLKPFSEERLAEALA 111

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4732057    6 MIVEDN-ELNMKLFRDLiEASGYTTIQTRNGMEALDLARKHRPDLILMDIQLPEVSGLEVTKWLKEDDElhVIPVIAVTA 84
Cdd:cd17625   1 LVVEDEkDLSEAITKHL-KKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGI--ETPVLLLTA 77