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 501231534   4 PLKVMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSVFKDTPVIL 83
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIF 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501231534  84 LSSRDGLFDKARGRVVGSDQFLTKPFSKEELLDAI 118
Cdd:COG3706   81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115

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 501231534   4 PLKVMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSVFKDTPVIL 83
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIF 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501231534  84 LSSRDGLFDKARGRVVGSDQFLTKPFSKEELLDAI 118
Cdd:COG3706   81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115

Ycf27; Reviewed

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231534   6 KVMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSvfkDTPVILLS 85
Cdd:CHL00148   8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKES---DVPIIMLT 84

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501231534  86 SRDGLFDKARGRVVGSDQFLTKPFSKEELLDAIRA 120
Cdd:CHL00148  85 ALGDVSDRITGLELGADDYVVKPFSPKELEARIRS 119

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 501231534   4 PLKVMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSVFKDTPVIL 83
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIF 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501231534  84 LSSRDGLFDKARGRVVGSDQFLTKPFSKEELLDAI 118
Cdd:COG3706   81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115

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 501231534   4 PLKVMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSvfKDTPVIL 83
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARP--SDIPIIM 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 501231534  84 LSSRDGLFDKARGRVVGSDQFLTKPFSKEELLDAIRAHV 122
Cdd:COG0745   79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALL 117

phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231534   7 VMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSVFKDTPVILLSS 86
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTG 80

                         90       100
                 ....*....|....*....|..
gi 501231534  87 RDGLFDKARGRVVGSDQFLTKP 108
Cdd:cd17602   81 KDGLVDRIRAKMAGASGYLTKP 102

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 501231534   8 MVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSvfKDTPVILLSSR 87
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKG--SDIPIIMLTAK 78

                         90       100
                 ....*....|....*....|.
gi 501231534  88 DGLFDKARGRVVGSDQFLTKP 108
Cdd:cd17574   79 DEEEDKVLGLELGADDYITKP 99

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 501231534   7 VMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSVFKDTPVILLSS 86
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 501231534  87 RDGLFDKARGRVVGSDQFLTKPFSKEELLDAIR 119
Cdd:cd17598   81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIK 113

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 501231534   7 VMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKI---------VDHQPSIIFVDVLMPRLDGYQTCAVIKHNSVFK 77
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLenlakegndLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 501231534  78 DTPVILLSSRDGLFDKARGRVVGSDQFLTKP 108
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111

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 501231534   7 VMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKhnSVFKDTPVILLSS 86
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLR--AAGNDLPILVLTA 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 501231534  87 RDGLFDKARGRVVGSDQFLTKPFSKEELLDAIRA 120
Cdd:cd17627   79 RDSVSDRVAGLDAGADDYLVKPFALEELLARVRA 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 501231534   6 KVMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSVFKDTPVILLS 85
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILMLT 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 501231534  86 SRDGLFDKARGRVVGSDQFLTKPFSKEELLDAIR 119
Cdd:cd17562   82 TESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVK 115

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 501231534   3 QPLKVMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKhnSVFKDTPVI 82
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELR--ALDPDLPVI 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501231534  83 LLSSRDGLFDKARGRVVGSDQFLTKPFSKEELLDAIRAHVPGFAVPQQHAP 133
Cdd:COG2204   79 LLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAE 129

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 501231534   7 VMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVI-KHNSVFKDTPVILLS 85
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIrELEGGGRRTPIIALT 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 501231534  86 SRDGLFDKARGRVVGSDQFLTKPFSKEELLDAI 118
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113

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 501231534   7 VMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSVFKDTPVILLSS 86
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 501231534  87 RDGLFDKARGRVVGSDQFLTKPFSKEELLDAI 118
Cdd:cd17580   81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. 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 501231534   6 KVMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSVfkDTPVILLS 85
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGP--DVPVLFLT 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501231534  86 SRDGLFDKARGRVVGSDQFLTKPFSKEELLDAIRA 120
Cdd:cd17615   79 AKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRA 113

DNA-binding response regulator HprR;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231534   5 LKVMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQtcaVIKHNSVFKDTPVILL 84
Cdd:PRK11517   1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQ---ILQTLRTAKQTPVICL 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 501231534  85 SSRDGLFDKARGRVVGSDQFLTKPFSKEELLDAIRAHVpgfavpQQHAP 133
Cdd:PRK11517  78 TARDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQL------RQHHA 120

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 501231534   6 KVMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSVFKDTPVILLS 85
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 501231534  86 SRDGLFDKARGRVVGSDQFLTKPFSKEELLDAIR 119
Cdd:cd17548   81 AYAMKGDREKILEAGCDGYISKPIDTREFLETVA 114

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the 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 501231534   7 VMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNsvFKDTPVILLS- 85
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEK--YPDLPVIMISg 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 501231534  86 ----------SRDGLFDkargrvvgsdqFLTKPFSKEELLDAIR 119
Cdd:cd17550   79 hgtietavkaTKLGAYD-----------FIEKPLSLDRLLLTIE 111

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 501231534   6 KVMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKhnSVFKDTPVILLS 85
Cdd:cd17554    2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIR--EKKPDLPVIICT 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 501231534  86 SRDGLFDKArgRVVGSDQFLTKPFSKEELLDAIRAH 121
Cdd:cd17554   80 AYSEYKSDF--SSWAADAYVVKSSDLTELKETIKRL 113

envelope stress response regulator transcription factor CpxR;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231534   6 KVMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIvDHQPSIIFVDVLMPRLDGYQTCAVIKHNsvfKDTPVILLS 85
Cdd:PRK10955   3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLL-DDSIDLLLLDVMMPKKNGIDTLKELRQT---HQTPVIMLT 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501231534  86 SRDGLFDKARGRVVGSDQFLTKPFSKEELLDAIRA 120
Cdd:PRK10955  79 ARGSELDRVLGLELGADDYLPKPFNDRELVARIRA 113

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that 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 501231534   7 VMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSvfkDTPVILLSS 86
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS---QVPVLMLTA 77

                         90       100       110
                 ....*....|....*....|....*....|....
gi 501231534  87 RDGLFDKARGRVVGSDQFLTKPFSKEELLDAIRA 120
Cdd:cd17623   78 RGDDIDRILGLELGADDYLPKPFNPRELVARIRA 111

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 501231534   6 KVMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSvfkDTPVILLS 85
Cdd:cd19939    1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHS---HVPILMLT 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 501231534  86 SRDGLFDKARGRVVGSDQFLTKPFSKEELLDAIRA 120
Cdd:cd19939   78 ARTEEMDRVLGLEMGADDYLCKPFSPRELLARVRA 112

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, 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 501231534   7 VMVIDDSRTIRRTAQMLLGEAGCEVITAS---DGFDaLAKIVDHqpSIIFVDVLMPRLDGYQTCAVIKHNSVfkDTPVIL 83
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDlgeEGLD-LGKLYDY--DIILLDLNLPDMSGYEVLRTLRLAKV--KTPILI 75

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 501231534  84 LSSRDGLFDKARGRVVGSDQFLTKPFSKEELLDAIRAHV 122
Cdd:cd17616   76 LSGLADIEDKVKGLGFGADDYMTKPFHKDELVARIHAIV 114

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 501231534   5 LKVMVIDDSRTIRRTAQMLLGEAGCEVI-TASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSVfkdTPVIL 83
Cdd:cd19932    1 VRVLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENI---APIVL 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 501231534  84 LS--SRDGLFDKARGrvVGSDQFLTKPFSKEELLDAI 118
Cdd:cd19932   78 LTaySQQDLVERAKE--AGAMAYLVKPFSESDLIPAI 112

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI belongs to the OmpR family of DNA-binding response regulators that 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 501231534   7 VMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSvfkDTPVILLSS 86
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKS---TLPVIFLTS 77

                         90       100
                 ....*....|....*....|..
gi 501231534  87 RDGLFDKARGRVVGSDQFLTKP 108
Cdd:cd19936   78 KDDEIDEVFGLRMGADDYITKP 99

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501231534   7 VMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSvfKDTPVILLSS 86
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAG--KQTPVLMLTA 78

                         90       100
                 ....*....|....*....|..
gi 501231534  87 RDGLFDKARGRVVGSDQFLTKP 108
Cdd:cd19935   79 RDSVEDRVKGLDLGADDYLVKP 100

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 501231534   7 VMVIDDSRTIRRTAQMLLGEAGCEVITASDGFDALAKIVDHQPSIIFVDVLMPRLDGYQTCAVIKHNSvfkDTPVILLSS 86
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWS---AVPVIVLSA 77

                         90       100
                 ....*....|....*....|..
gi 501231534  87 RDGLFDKARGRVVGSDQFLTKP 108
Cdd:cd17620   78 RDEESDKIAALDAGADDYLTKP 99