ID A0A011QSQ0_9PROT Unreviewed; 698 AA.
AC A0A011QSQ0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=fixL_1 {ECO:0000313|EMBL:EXI92160.1};
GN ORFNames=AW12_00778 {ECO:0000313|EMBL:EXI92160.1};
OS Candidatus Accumulibacter sp. BA-94.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454005 {ECO:0000313|EMBL:EXI92160.1, ECO:0000313|Proteomes:UP000020878};
RN [1] {ECO:0000313|EMBL:EXI92160.1, ECO:0000313|Proteomes:UP000020878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA-94 {ECO:0000313|Proteomes:UP000020878};
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:EXI92160.1}.
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DR EMBL; JEMZ01000036; EXI92160.1; -; Genomic_DNA.
DR STRING; 1454005.AW12_00778; -.
DR PATRIC; fig|1454005.3.peg.741; -.
DR Proteomes; UP000020878; 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 GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000020878};
KW Transferase {ECO:0000313|EMBL:EXI92160.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 47..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 328..400
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 404..456
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 482..697
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 698 AA; 78280 MW; 3BC6CD87F40EDD6C CRC64;
MLAKDRRQEA NLGKMSADEA GPPTLPVRPA APTYDRRRPP PLRWSTWYLF ALKLATGLLL
ILLIALLWLL HRNEIDEQRS ALIADVLWLE QTLRFHLEGN AEQFQQLALD LTRAQRPAEL
FDLRARHLLR NSPELRQVLW LDATAKVLHG MPTLTLPRVI DEAFGDNPVS RSLELARLGK
PIYSDAFRTI EFRTIEAAQF EVYVPIFADG AYRGALLAVY SLNGLLKHQI PWWFAERYQV
RAVDGNGSLL ASKSRIDASP TTLTHPISLD PPGYGVTLQV TAYRSPGNLA QTLIATLVII
LAAAVFWSLW AVRGLVQRRI SAEQALRTEY AFRKAMEDSL MVGMRARDLE GRVTYANPSF
LRMVGFSAEE LIGRAPPMPY WAPEEMERTL QVHNHILQGN APHEGFEIRL MRKDGSRFDA
LIYEAPLIDA DGRQTGWMGS IIDVTARKXV TARKQAEEVA RQQQEKLQVT ARLVTMGEMA
STLAHELNQP LAAITSYNAG CLNKLDSGNF NPLQIREALG KLAVQAQRAG QIIRRVHDFV
RKSEPKLTPC DLAEVIDDSV GFIEAAARNR GVRIVREIQG MRPELLADPV MLEQVLLNLM
RNGIEAMAGL PAERRRLTVR LGQVDAQMEI RVIDRGPGIP PEALEKLFTP LFSTKADGMG
MGLNICRSII EFHHGRLWVE ANPEGGSIFV ITLPIHRQ
//
