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Database: UniProt
Entry: A0A1F7W8Y8_9BACT
LinkDB: A0A1F7W8Y8_9BACT
Original site: A0A1F7W8Y8_9BACT 
ID   A0A1F7W8Y8_9BACT        Unreviewed;       693 AA.
AC   A0A1F7W8Y8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 22.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A2304_05150 {ECO:0000313|EMBL:OGL98848.1};
OS   Candidatus Uhrbacteria bacterium RIFOXYB2_FULL_57_15.
OC   Bacteria; Candidatus Uhrbacteria.
OX   NCBI_TaxID=1802422 {ECO:0000313|EMBL:OGL98848.1, ECO:0000313|Proteomes:UP000176501};
RN   [1] {ECO:0000313|EMBL:OGL98848.1, ECO:0000313|Proteomes:UP000176501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {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:OGL98848.1}.
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DR   EMBL; MGFE01000014; OGL98848.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F7W8Y8; -.
DR   Proteomes; UP000176501; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; 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   CDD; cd12914; PDC1_DGC_like; 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; 2.
DR   InterPro; IPR033479; dCache_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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02743; dCache_1; 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; 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   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        286..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          336..387
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          473..692
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   693 AA;  77339 MW;  8BE581685EE68B70 CRC64;
     MEVEQGRNFR WLAKLVYITV IFFVTLAVCF SIWRIYQSTT EATVERRQAI VSLAAASTEL
     RFEYLKDLGV SFATRVRFRE FISTNDWDGA IGILSDVTEN FPYIDRIFIT DPSGMLMADV
     PALSDVRGKN FAFRDWYIGV SDGWKPYVSD VYQRTAEPRY NVVAISVPIV ADTGEILGIL
     VLQIRADQLV NWMRSAVEGT NMVAYLVDPK GHPVGNPLVD PQESLLDFSD QPFVAAVLNN
     ERGLGIYSGI NGGNESLVVY EPISLFGWGV VVSEEIDSAF ATRNEILSIA VLIFLIAVGI
     VVFLVSLLYL MLMRLQRMSL ELDARVESRA RAFGEEHAKI QAIIESMIDG VIVSDLRGRV
     VLANQEIRRL LGYVPSELQG KKIFSSLEMR DRTGKIIPES RRPMLQALHG KITRIPTVTD
     ANFYVRKDGT LFPALVTCAP VLVDGKVAGA VSVLRDATKE YAVDRAKNEF VRLASHQLRT
     PLTAILWYVQ NMIEGSVGRL SKPQTEHLKI IEYSTRRMIR LVNDLLRVSQ IDLSQIPSRI
     HGMELQPVVG SVVEELFEVA SERNVSVTVS SPRSLPLVRA DELLVRQSLL ILVGNAIAFT
     PAKGRIKIIL ERVTNDVRIS VRDTGIGIPK DEQGRVFQRF FRASNAQKYT GEGTGLGLFI
     AKEIVNLSKG KIGFSSEEGR GSTFWISFPI VRS
//
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