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 2049861626   6 TILLAEDSPYDAEMAIDALREANLLNPIVHVTDGVEALDYLFRRGKYADRGegDPSVLLLDIKMPRMDGLEVLEALRQDE 85
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVPNELHVVRDGEEALDFLRGEGEYADAP--RPDLILLDLNMPRMDGFEVLREIKADP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2049861626  86 KLRLLPVVILSSSREEADLVRSWDLGVNAYVVKPVDVDQFFEAVRTLGKFW 136
Cdd:cd17557    79 DLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSLGEYW 129

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 2049861626   6 TILLAEDSPYDAEMAIDALREANLLNPIVHVTDGVEALDYLFRRGKYADRGegDPSVLLLDIKMPRMDGLEVLEALRQDE 85
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVPNELHVVRDGEEALDFLRGEGEYADAP--RPDLILLDLNMPRMDGFEVLREIKADP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2049861626  86 KLRLLPVVILSSSREEADLVRSWDLGVNAYVVKPVDVDQFFEAVRTLGKFW 136
Cdd:cd17557    79 DLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSLGEYW 129

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 2049861626   7 ILLAEDSPydaeMAIDALREA-NLLNPIVHVT-DGVEALDYLfrrgkyadrGEGDPSVLLLDIKMPRMDGLEVLEALRQD 84
Cdd:pfam00072   1 VLIVDDDP----LIRELLRQLlEKEGYVVAEAdDGKEALELL---------KEERPDLILLDINMPGMDGLELLKRIRRR 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2049861626  85 EKlrLLPVVILSSSREEADLVRSWDLGVNAYVVKPVDVDQFFEAVR 130
Cdd:pfam00072  68 DP--TTPVIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111

response regulator PleD; Reviewed

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049861626   6 TILLAEDSPYDAEmaidaLREANLLNPIVHV---TDGVEALDyLFRRGKyadrgegdPSVLLLDIKMPRMDGLEVLEALR 82
Cdd:PRK09581    4 RILVVDDIPANVK-----LLEAKLLAEYYTVltaSSGAEAIA-ICEREQ--------PDIILLDVMMPGMDGFEVCRRLK 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2049861626  83 QDEKLRLLPVVILSSSREEADLVRSWDLGVNAYVVKPVDVDQFFEAVRTLGKFWAVINE 141
Cdd:PRK09581   70 SDPATTHIPVVMVTALDDPEDRVRGLEAGADDFLTKPINDVALFARVKSLTRLKMVIDE 128

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 2049861626   6 TILLAEDSPYDAEMAIDALREANLLNPIVHVTDGVEALDYLFRRGKYADRGegDPSVLLLDIKMPRMDGLEVLEALRQDE 85
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVPNELHVVRDGEEALDFLRGEGEYADAP--RPDLILLDLNMPRMDGFEVLREIKADP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2049861626  86 KLRLLPVVILSSSREEADLVRSWDLGVNAYVVKPVDVDQFFEAVRTLGKFW 136
Cdd:cd17557    79 DLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSLGEYW 129

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049861626   5 RTILLAEDSPYDAEMAIDALREANLLnpIVHVTDGVEALDYLFRRgkyadrgegDPSVLLLDIKMPRMDGLEVLEALRQD 84
Cdd:COG3706     2 ARILVVDDDPTNRKLLRRLLEAAGYE--VVEAADGEEALELLQEH---------RPDLILLDLEMPDMDGLELCRRLRAD 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2049861626  85 EKLRLLPVVILSSSREEADLVRSWDLGVNAYVVKPVDVDQFFEAVRTLGKF 135
Cdd:COG3706    71 PRTADIPIIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVARY 121

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049861626   5 RTILLAEDSPYDAEMAIDALREANLlnPIVHVTDGVEALDYLfrrgkyadrGEGDPSVLLLDIKMPRMDGLEVLEALRQD 84
Cdd:COG3437     7 PTVLIVDDDPENLELLRQLLRTLGY--DVVTAESGEEALELL---------LEAPPDLILLDVRMPGMDGFELLRLLRAD 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2049861626  85 EKLRLLPVVILSSSREEADLVRSWDLGVNAYVVKPVDVDQFFEAVRTL 132
Cdd:COG3437    76 PSTRDIPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNA 123

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 2049861626   5 RTILLAEDSPYDAEMAIDALREANLlnPIVHVTDGVEALDYLfrrgkyadrGEGDPSVLLLDIKMPRMDGLEVLEALRQD 84
Cdd:COG2204     3 ARILVVDDDPDIRRLLKELLERAGY--EVETAASGEEALALL---------REEPPDLVLLDLRMPGMDGLELLRELRAL 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2049861626  85 EklRLLPVVILSSSREEADLVRSWDLGVNAYVVKPVDVDQFFEAVR 130
Cdd:COG2204    72 D--PDLPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVE 115

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 2049861626   8 LLAEDSPYDAEMAIDALREANLLnpIVHVTDGVEALDYLFrrgkyadrgEGDPSVLLLDIKMPRMDGLEVLEALRQDEkl 87
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYE--VDTAADGEEALELLR---------EERPDLVLLDLMMPGMDGLELLRKLRELP-- 67

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2049861626  88 RLLPVVILSSSREEADLVRSWDLGVNAYVVKP 119
Cdd:cd00156    68 PDIPVIVLTAKADEEDAVRALELGADDYLVKP 99

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 2049861626   7 ILLAEDSPydaeMAIDALREA-NLLNPIVHVT-DGVEALDYLfrrgkyadrGEGDPSVLLLDIKMPRMDGLEVLEALRQD 84
Cdd:pfam00072   1 VLIVDDDP----LIRELLRQLlEKEGYVVAEAdDGKEALELL---------KEERPDLILLDINMPGMDGLELLKRIRRR 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2049861626  85 EKlrLLPVVILSSSREEADLVRSWDLGVNAYVVKPVDVDQFFEAVR 130
Cdd:pfam00072  68 DP--TTPVIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111

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 2049861626   8 LLAEDSPYDAEMAIDALREANLLnpIVHVTDGVEALDYLFrrgkyadrgEGDPSVLLLDIKMPRMDGLEVLEALRqdEKL 87
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYE--VDTAADGEEALELAR---------EEQPDLIILDVMLPGMDGFEVCRRLR--EKG 67

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2049861626  88 RLLPVVILSSSREEADLVRSWDLGVNAYVVKP 119
Cdd:cd17574    68 SDIPIIMLTAKDEEEDKVLGLELGADDYITKP 99

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 2049861626   6 TILLAEDSPYDAEMAIDALREANLLNPIVHvTDGVEALDYLfrrgkyadrGEGDPSVLLLDIKMPRMDGLEVLEALRQDE 85
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSAGYLEVVSF-TDPREALAWC---------RENPPDLILLDYMMPGMDGLEFIRRLRALP 71

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2049861626  86 KLRLLPVVILSSSREEADLVRSWDLGVNAYVVKPVD 121
Cdd:cd17551    72 GLEDVPIVMITADTDREVRLRALEAGATDFLTKPFD 107

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 2049861626   1 MTDIRtILLAEDSPYDAEMAIDALREANLlNPIVHVTDGVEALDYLFRRgkyadrgegDPSVLLLDIKMPRMDGLEVLEA 80
Cdd:COG3707     1 MRGLR-VLVVDDEPLRRADLREGLREAGY-EVVAEAADGEDAVELVREL---------KPDLVIVDIDMPDRDGLEAARQ 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2049861626  81 LRQDeklRLLPVVILSSSREEADLVRSWDLGVNAYVVKPVDVDQFFEAVRT 131
Cdd:COG3707    70 ISEE---RPAPVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALEL 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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049861626   7 ILLAEDSPYDAEMAIDALREANLlnPIVHVTDGVEALDYLFRRgkyadrgegDPSVLLLDIKMPRMDGLEVLEALRQDEK 86
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGY--KVQVARNGREALAMLAEH---------RPTLVISDIVMPEMDGYELCRKIKSDPD 69

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2049861626  87 LRLLPVVILSSSREEADLVRSWDLGVNAYVVKPVD 121
Cdd:cd17598    70 LKDIPVILLTTLSDPRDVIRGLECGADNFITKPYD 104

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 2049861626   8 LLAEDSPYDAEMAIDALREANLLnpIVHVTDGVEALDYlfrrgkyADRGEGDpsVLLLDIKMPRMDGLEVLEALRQDEKl 87
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYT--VDVCFDGEEGLEY-------ALSGIYD--LIILDIMLPGMDGLEVLKSLREEGI- 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2049861626  88 rLLPVVILSSSREEADLVRSWDLGVNAYVVKPVDVDQFFEAVRTL 132
Cdd:cd17625    69 -ETPVLLLTALDAVEDRVKGLDLGADDYLPKPFSLAELLARIRAL 112

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049861626   5 RTILLAEDSPYDAEMAIDALREANLlnPIVHVTDGVEALDylfrrgkyadRGEGDP-SVLLLDIKMPRMDGLEVLEALRQ 83
Cdd:cd17562     1 KKILAVDDSASIRQMVSFTLRGAGY--EVVEAADGRDALS----------KAQSKKfDLIITDQNMPNMDGIELIKELRK 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2049861626  84 DEKLRLLPVVILSSSREEADLVRSWDLGVNAYVVKPVDVDQFFEAVRTL 132
Cdd:cd17562    69 LPAYKFTPILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKV 117

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 2049861626   6 TILLAEDSPYDAEmaidaLREANLLN---PIVHVTDGVEALDyLFRRGKyadrgegdPSVLLLDIKMPRMDGLEVLEALR 82
Cdd:cd17538     1 KILVVDDEPANRE-----LLEALLSAegyEVLTADSGQEALA-LAEEEL--------PDLILLDVMMPGMDGFEVCRRLK 66

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2049861626  83 QDEKLRLLPVVILSSSREEADLVRSWDLGVNAYVVKPV 120
Cdd:cd17538    67 EDPETRHIPVIMITALDDREDRIRGLEAGADDFLSKPI 104

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049861626   6 TILLAEDSPYDAEMAIDALREANLLNPIVHVTDGVEALDYLFrrgkyadrgEGDPSVLLLDIKMPRMDGLEVLEALRQDE 85
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKYPDLEVVGEASNGEEALELLE---------EHKPDLVFLDIQMPGLDGFELARQLRELD 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2049861626  86 klRLLPVVILSSSREEAdlVRSWDLGVNAYVVKPVDVDQFFEAVR 130
Cdd:COG3279    74 --PPPPIIFTTAYDEYA--LEAFEVNAVDYLLKPIDEERLAKALE 114

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. 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 2049861626  37 TDGVEALDYLfrrgkyadrGEGDPSVLLLDIKMPRMDGLEVLEALRqdEKLRLLPVVILSSSRE-----EAdlVRswdLG 111
Cdd:cd17536    32 ENGEEALELI---------EEHKPDIVITDIRMPGMDGLELIEKIR--ELYPDIKIIILSGYDDfeyaqKA--IR---LG 95

                          90
                  ....*....|....*....
gi 2049861626 112 VNAYVVKPVDVDQFFEAVR 130
Cdd:cd17536    96 VVDYLLKPVDEEELEEALE 114

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 2049861626   7 ILLAEDSPYDAEMAIDALREANLlnPIVHVTDGVEALDYLFRRgkyadrgegDPSVLLLDIKMPRMDGLEVLEALRQDEK 86
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGF--TVIAASNGLEALDLLNQY---------IPDLIISDIIMPGVDGYSLLGKLRKNAD 69

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2049861626  87 LRLLPVVILSSSREEADLVRSWDLGVNAYVVKP 119
Cdd:cd19927    70 FDTIPVIFLTAKGMTSDRIKGYNAGCDGYLSKP 102

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. 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 2049861626  33 IVHVTDGVEALDYLfrrgkyadrGEGDPSVLLLDIKMPRMDGLEVLEALRQdEKLRLLPVVILSSSREEAdLVRSWDLGV 112
Cdd:cd17593    28 ITFAENGEEALEIL---------REGRIDVLFLDLTMPVMDGYEVLEALPV-EQLETKVIVVSGDVQPEA-KERVLELGA 96

                          90       100
                  ....*....|....*....|.
gi 2049861626 113 NAYVVKPVDVDQFFEAVRTLG 133
Cdd:cd17593    97 LAFLKKPFDPEKLAQLLEELG 117

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 2049861626  33 IVHVTDGVEALDYLFrrgkyadrgEGDPSVLLLDIKMPRMDGLEVLEALRqdEKLRLLPVVILSSSREEADLVRSWdlGV 112
Cdd:cd17554    27 VVTAGNGEEALEKLE---------SEDPDLVILDIKMPGMDGLETLRKIR--EKKPDLPVIICTAYSEYKSDFSSW--AA 93

                          90       100
                  ....*....|....*....|
gi 2049861626 113 NAYVVKPVDVDQFFEAVRTL 132
Cdd:cd17554    94 DAYVVKSSDLTELKETIKRL 113

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. 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 2049861626   7 ILLAEDSPYDAEMAIDALREANLlnPIVHVTDGVEALDYLFRRgkyadrgegDPSVLLLDIKMPRMDGLEVLEALRQDEK 86
Cdd:cd19939     2 ILIVEDELELARLTRDYLIKAGL--EVSVFTDGQRAVRRIIDE---------QPSLVVLDIMLPGMDGLTVCREVREHSH 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2049861626  87 lrlLPVVILSSSREEADLVRSWDLGVNAYVVKPV 120
Cdd:cd19939    71 ---VPILMLTARTEEMDRVLGLEMGADDYLCKPF 101

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains; Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2049861626  60 PSVLLLDIKMPRMDGLEVLEALRQDEKLRLLPVVILSSSREEADLVRSWDLGVNAYVVKPVDVDQFFEAVRTL 132
Cdd:cd17552    47 PDAILLDVMMPDMDGLATLKKLQANPETQSIPVILLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKL 119

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) 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 2049861626   4 IRtILLAEDSPYDAEMAIDALREANLLNPIVHVTDGVEALDYLfrrgkyadrGEGDPSVLLLDIKMPRMDGLEVLEALRq 83
Cdd:cd17541     1 IR-VLIVDDSAVMRKLLSRILESDPDIEVVGTARDGEEALEKI---------KELKPDVITLDIEMPVMDGLEALRRIM- 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2049861626  84 deKLRLLPVVILSSS-REEADLV-RSWDLGVNAYVVKPV-DVDQFFEAVR 130
Cdd:cd17541    70 --AERPTPVVMVSSLtEEGAEITlEALELGAVDFIAKPSgGISLDLEEIA 117

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 2049861626  36 VTDGVEALdylfrRGKYADRgegdPSVLLLDIKMPRMDGLEVLEALRQDEklRLLPVVILSSSREEADLVRSWDLGVNAY 115
Cdd:cd17627    28 AVDGAEAL-----RVISGNR----PDAVVLDVMMPRLDGLEVCRRLRAAG--NDLPILVLTARDSVSDRVAGLDAGADDY 96

                          90
                  ....*....|....*..
gi 2049861626 116 VVKPVDVDQFFEAVRTL 132
Cdd:cd17627    97 LVKPFALEELLARVRAL 113

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 2049861626  33 IVHVTDGVEALdYLFRRGKyadrgegdPSVLLLDIKMPRMDGLEVLEALRQDEKLRLLPVVILSSSREEADLVRSWDLGV 112
Cdd:cd19937    24 VVTAYDGEEAL-KRAKDEK--------PDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAKGEEFDKVLGLELGA 94

                  ....*..
gi 2049861626 113 NAYVVKP 119
Cdd:cd19937    95 DDYITKP 101

DNA-binding response regulator HprR;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049861626   7 ILLAEDSPYDAEMAIDALREANLLnpIVHVTDGVEALdYLFRRGKYAdrgegdpsVLLLDIKMPRMDGLEVLEALRQDEK 86
Cdd:PRK11517    3 ILLIEDNQRTQEWVTQGLSEAGYV--IDAVSDGRDGL-YLALKDDYA--------LIILDIMLPGMDGWQILQTLRTAKQ 71