ID A0A080LYX1_9PROT Unreviewed; 1505 AA.
AC A0A080LYX1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=rpfC_1 {ECO:0000313|EMBL:KFB73976.1};
GN ORFNames=AW09_000747 {ECO:0000313|EMBL:KFB73976.1};
OS Candidatus Accumulibacter phosphatis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=327160 {ECO:0000313|EMBL:KFB73976.1, ECO:0000313|Proteomes:UP000020077};
RN [1] {ECO:0000313|EMBL:KFB73976.1, ECO:0000313|Proteomes:UP000020077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA-91 {ECO:0000313|Proteomes:UP000020077};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFB73976.1}.
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DR EMBL; JDVG02000127; KFB73976.1; -; Genomic_DNA.
DR Proteomes; UP000020077; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 3.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFB73976.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 176..246
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 557..609
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 610..654
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 679..732
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 729..775
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 802..854
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 890..1110
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1138..1254
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1305..1400
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 1258..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 863..890
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1187
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1344
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1505 AA; 164918 MW; 03649DE468081FA1 CRC64;
MTPMRSDGRA AMLRVVLIYA FVATLWILFS DTLIGHLGVQ PETLVMLGML KGLAFVGLTS
MLLYALLRRL PEGAAATPAG GGSRRLLLSV AALALLILIV GAAAMRQVAE RQETRPADLF
WITLSIAAAL FAVVFLGIML HQQQRLRLAE SLRQAQAEAL RRQQLVDQQR AEHLALASHY
QTMIGEARDI ILLLDENGQI VEANAAAVAA YGCSADELRG MHIRDLRGEE TRSTLGEQWQ
ASARPDGVLF ETVHRRRDGT CFPVEVSSRA FSVEGKLYHQ SFVRDISERR KADEALRRSH
RALRTLSECN QALVRASDEA TLLSDICRLL VDFGCYRLAW VAYTDGDDDP CRIRPVAAAG
CEDGSGATVR IHSDDVDCGH GPTGTAIRER RLVLAQNLQS DPAFEPWREA AQRQGHAASI
ALPLLAGDAA CLGALNLYAG EAEAFDADET QLLVELADDL AYGIRALRDR AARNAAEATL
RATAQQLEHL LEASPTILYA LRFIDGVPRA QQVSANVERI SGYTVAEALQ DGWWEAGLHP
DDRAAVLRFS ASCGGITVHE YRFAHKQGHY LWIRDELRLI RDAAGQAVEI VGAWTDISIA
RQAMLALQES ERRYREIFVA NPQPMWVYDR ETLAFLDVNA AAIRRYGYRR EEFLAMTIKD
IRPAEEIPHL LTRVAQVEVN VDAGVWRHRR RDGSELLVEI TSHALDFGGR RAHVVLAHDI
TQRVQAEAEL RKLSLAVEQS PESIIITDID ARIEYVNEAA VRSSGYLRVE LIGENPRILQ
SGKTPSRTYR ALWAALSAGQ VWRGELHNRR KDGVEYVEFA IVTPIRQANG RITHYVAVKE
DITEKKRIGA ELDRYRHHLE EMVQERTVQL AEARARAEAA NRAKSDFLAN MSHEIRTPMN
AIIGLTHLLQ SSAPTPQQSE RLDKINAATR HLLAIINDIL DLSKIEAGKL ALEQDDFPLA
AILDSVLSLI AEPARTKGLT VEIVEPQEPL WLRGDATRLR QALLNYASNA VKFTECGRVI
LRTRLLEEAG DTLQLLFEVE DTGIGIAAEK LPQIFEAFEQ ADASTTRKYG GTGLGLAITR
RLARLMGGDA GADSVPGQGS RFWFTACLQR GRGVMAAPLV EPAVDAEDTL RRCHAGARLL
LAEDNEINRE VALELLHGVG LAVDSVADGR AALRMATARD YALILMDVQM PMMDGLEASR
AIRALPGRAA LPIVAMTANI FEDDRRACVA AGMNDFVAKP VEPEQLFATL LRWLTPAQPG
RRTASTPAPS GERLATRPEK SETLARLTSI AGLDAVAGVQ LLNGNVASYC RLLRLYVDSY
GETIVSMPQQ LRSGEHDEVQ RRAHAIKGVS ANLRVAGVQQ ACIALEAALR AGDAAADDLE
GLVMTLAERY TAVCAAIRKA LDAAPDAAGA GTVILAPDWD GVRSVLAELE ALLASDNLRA
NQLVDENAAL LHTALGHFAG EIEGHLRQFR YPDALDVLQR ARRAYPQAQT LAAAPAVLAS
TGLTR
//
