ID A0A080M1V1_9PROT Unreviewed; 832 AA.
AC A0A080M1V1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=luxQ_7 {ECO:0000313|EMBL:KFB75267.1};
GN ORFNames=AW06_003639 {ECO:0000313|EMBL:KFB75267.1};
OS Candidatus Accumulibacter cognatus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=2954383 {ECO:0000313|EMBL:KFB75267.1, ECO:0000313|Proteomes:UP000021315};
RN [1] {ECO:0000313|EMBL:KFB75267.1, ECO:0000313|Proteomes:UP000021315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-02 {ECO:0000313|Proteomes:UP000021315};
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 -!- 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:KFB75267.1}.
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DR EMBL; JDST02000096; KFB75267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A080M1V1; -.
DR STRING; 1453999.AW06_003639; -.
DR Proteomes; UP000021315; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KFB75267.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000021315};
KW Transferase {ECO:0000313|EMBL:KFB75267.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 54..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 272..324
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 401..454
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 472..689
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 709..828
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 758
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 832 AA; 91480 MW; 16A1A3CB8BD707FB CRC64;
MSSRRVIDWL VPPRADARVA ARARIVARSL LTISAVVSLL LVAFFAVRSR PSTLELTLFA
VAIMTPVGAA VALRFVSRPT EVLLLTNLLG SAYVAVWAFA TGGVLSAAVP WLIALLATLG
TFGRARLLLA AFAIDILLLV ALYWATVREL LPPNLVPAEE AALLAFIGQL SSLVVVAMAA
RIVLRARVAA SASIQRGEQR LHRIVNGMPA AIAHIDYTES TPHYSFVNRR YAERFGRTDE
AVGGMGVPEL LGDEAYRRIE PHLQQVRRGE AAEYDLALPM PDGSTRYDRS YLLPDRAEDG
SVQGAYIFAI DDSERKRALL ALELSQTRLA EAQAMAQVGN WEFDLQTERL EWSDEVYHIC
GHRPRSFAPF FTAHYMAATH VDDRPRLAAA LEQILATSAP QQLEHRIQRS DGVERTVEVR
AEVLRTDSAG RIVKLVGIIQ DVSERKLIEQ QLIAAKEAAE SASRAKSVFL ANMSHEIRTP
MNGVIGMADL LLQEPLAERA RHYARTIQRS GRALLGVLDD ILDLSKIEAG RLDLESASFN
LQVMLRELQD LFGEAARLKN VTLRVTVAAD LPRWVTGDVV RLRQVLLNLV SNAVKFTTHG
TIDVDACRES DGALRFSVRD TGIGIAADKQ TQIFEAFAQA EQGTTRRFGG TGLGLSIARE
LVRLMGGEIG LQSSPGEGSC FWFQVRLPEA TAPAEARRRA VAGSFAGRRV LIAEDDPVNA
EVTRATLEHY GIDVVLVPDG EQAVTEQARQ PFDLVLMDCQ MLQMDGLEAT RLIREAEKLR
GTQRTPVVAL TAHAMAGYRD ECLQAGMDDY LVKPFKAEAL RQMLGRWLND QP
//
