phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. 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 494066479   3 RILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLR-EEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFITG 81
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQqGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80

                         90       100
                 ....*....|....*....|...
gi 494066479  82 FAAVALNPDSNAPQDAKVLSKPF 104
Cdd:cd18160   81 GAAAAPELLSDAVGDNATLKKPF 103

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. 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 494066479   3 RILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLR-EEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFITG 81
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQqGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80

                         90       100
                 ....*....|....*....|...
gi 494066479  82 FAAVALNPDSNAPQDAKVLSKPF 104
Cdd:cd18160   81 GAAAAPELLSDAVGDNATLKKPF 103

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 494066479    4 ILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFITGFA 83
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 494066479   84 avalnpDSNAPQDAK------VLSKPFHLRDLVNEVE 114
Cdd:pfam00072  81 ------DEDDAVEALeagaddFLSKPFDPDELLAAIR 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 494066479     3 RILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMP 56
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. 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 494066479   3 RILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLR-EEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFITG 81
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQqGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80

                         90       100
                 ....*....|....*....|...
gi 494066479  82 FAAVALNPDSNAPQDAKVLSKPF 104
Cdd:cd18160   81 GAAAAPELLSDAVGDNATLKKPF 103

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494066479   1 MARILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELAR--RATEIDPDLKVMF 78
Cdd:COG0784    5 GKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRriRALPRLPDIPIIA 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 494066479  79 ITGFAAVALNPDSNAPQDAKVLSKPFHLRDLVNEVEKLLQAA 120
Cdd:COG0784   85 LTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126

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 494066479   3 RILLAEDDNDMRRFLVKALER-AGYEVVDF-DNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFIT 80
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWeAGFEVVGEaENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILS 80

                 ...
gi 494066479  81 GFA 83
Cdd:COG4753   81 GYS 83

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 494066479    4 ILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFITGFA 83
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 494066479   84 avalnpDSNAPQDAK------VLSKPFHLRDLVNEVE 114
Cdd:pfam00072  81 ------DEDDAVEALeagaddFLSKPFDPDELLAAIR 111

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494066479   5 LLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFITGFA 83
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKA 79

Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494066479   1 MARILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFIT 80
Cdd:COG5803    2 MKKILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMMT 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 494066479  81 GFAAVALNPDSNAPQDAKVLSKPFHLRDLVNEVEKLL 117
Cdd:COG5803   82 AYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLL 118

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 494066479   4 ILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFITGFA 83
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRRTPIIALT 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 494066479  84 AVALNPDSNAPQDA---KVLSKPFHLRDLVNEV 113
Cdd:cd17546   81 ANALEEDREKCLEAgmdDYLSKPVKLDQLKEVL 113

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators similar to Pseudomonas savastanoi blue-light-activated histidine kinase; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase (HK)/response regulators contain all the elements of a classical TCS in a single polypeptide chain. Pseudomonas savastanoi blue-light-activated histidine kinase is a photosensitive HK and RR that is involved in increased bacterial virulence upon exposure to light. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic 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 494066479   4 ILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEP-FSLLLTDIVMP-EMDGIELARRATEIDPDLKVMFITG 81
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPdIDLLVTDVIMPgGMNGSQLAEEARRRRPDLKVLLTSG 80

                         90       100
                 ....*....|....*....|...
gi 494066479  82 FAAVALNPDSNAPQdAKVLSKPF 104
Cdd:cd18161   81 YAENAIEGGDLAPG-VDVLSKPF 102

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494066479   1 MARILLAEDDNDMRRFLVKALER-AGYEVVD-FDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMF 78
Cdd:COG4565    3 MIRVLIVEDDPMVAELLRRYLERlPGFEVVGvASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDVIV 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494066479  79 ITGFAAVALNPDSNAPQDAKVLSKPFHLRDLVNEVEKLLQ 118
Cdd:COG4565   83 ITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLE 122

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. 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 494066479   4 ILLAEDDNDMRRFLVKALERA-GYEVV-DFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFITG 81
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESEpDIEVVgEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80

                 .
gi 494066479  82 F 82
Cdd:cd17535   81 H 81

histidine kinase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494066479   3 RILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEP-FSLLLTDIVMP-EMDGIELARRATEIDPDLKVMFIT 80
Cdd:PRK13557 417 TILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPeVDLLFTDLIMPgGMNGVMLAREARRRQPKIKVLLTT 496

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494066479  81 GFAAVALNPDSNAPQDAKVLSKPFHLRDLVNEVEKLLQAA 120
Cdd:PRK13557 497 GYAEASIERTDAGGSEFDILNKPYRRAELARRVRMVLDGP 536

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). 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 494066479   3 RILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFITGF 82
Cdd:cd17553    2 KILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTAY 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 494066479  83 AAVALNPDSNAPQDAKVLSKPFHLRDLVNEVEKLLQ 118
Cdd:cd17553   82 GELDMIQESKELGALTHFAKPFDIDEIRDAVKKYLP 117

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494066479   1 MARILLAEDDNDMRRFLVKALER-AGYEVVD-FDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMF 78
Cdd:COG3279    1 MMKILIVDDEPLARERLERLLEKyPDLEVVGeASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 494066479  79 ITGFAAVALnpdsnapqDA-KV-----LSKPFHLRDLVNEVEKLLQ 118
Cdd:COG3279   81 TTAYDEYAL--------EAfEVnavdyLLKPIDEERLAKALEKAKE 118

acetoacetate metabolism transcriptional regulator AtoC;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494066479   3 RILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFITGF 82
Cdd:PRK11361   6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAY 85

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 494066479  83 AAVALNPDSNAPQDAKVLSKPFHLRDLVNEVEKLLQ 118
Cdd:PRK11361  86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQ 121

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494066479   2 ARILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARR 66
Cdd:cd17562    1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKE 65

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494066479   4 ILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFIT 80
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLT 77

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. 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 494066479   2 ARILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFITG 81
Cdd:cd17555    1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSG 80

DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494066479   4 ILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFITGFA 83
Cdd:COG4566    2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 494066479  84 AVALnpdsnAPQDAK-----VLSKPFHLRDLVNEVEKLLQAA 120
Cdd:COG4566   82 DVPM-----AVRAMKagavdFLEKPFDDQALLDAVRRALARD 118

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily 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 494066479   4 ILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFITgfa 83
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILT--- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494066479  84 AVALNPDSNAPQDAKV---LSKPFHLRDLVNEVEKLLQAA 120
Cdd:cd19934   78 ARDSWQDKVEGLDAGAddyLTKPFHIEELLARLRALIRRA 117

phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase/response regulators; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase/response regulators contain all the elements of a classical TCS in a single polypeptide chain. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494066479   4 ILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEiDPDLK 75
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKS-DPDLK 71

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase 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 494066479   2 ARILLAEDDNDMRRFLVKALERAGY-EVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELAR--RATEIDPDLKVMF 78
Cdd:cd17551    1 MRILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRrlRALPGLEDVPIVM 80

                 ..
gi 494066479  79 IT 80
Cdd:cd17551   81 IT 82

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 494066479   4 ILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARR--ATEIDPDLKVMFITG 81
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRlkADPATRHIPVIFLTA 80

                 ....
gi 494066479  82 FAAV 85
Cdd:cd19920   81 LTDT 84

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 494066479   3 RILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEID--PDLKVMFIT 80
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPetRHIPVIMIT 80

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 494066479     3 RILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMP 56
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55

phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. 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 494066479   4 ILLAEDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRL---------REEPFSLLLTDIVMPEMDGIELARRATEiDP-- 72
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLenlakegndLSKELDLIITDIEMPKMDGYELTFELRD-DPrl 79

                 ....*....
gi 494066479  73 -DLKVMFIT 80
Cdd:cd19924   80 aNIPVILNS 88

response regulator FixJ; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494066479   8 EDDNDMRRFLVKALERAGYEVVDFDNGAGAYDRLREEPFSLLLTDIVMPEMDGIELARRATEIDPDLKVMFITGFAAVAL 87
Cdd:PRK09390  10 DDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHGDVPL 89

                         90       100       110
                 ....*....|....*....|....*....|...
gi 494066479  88 NPDSNAPQDAKVLSKPFHLRDLVNEVEKLLQAA 120
Cdd:PRK09390  90 AVEAMKLGAVDFIEKPFEDERLIGAIERALAQA 122