ID   A0A1G1ZRD4_9BACT        Unreviewed;       442 AA.
AC   A0A1G1ZRD4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A3H63_01180 {ECO:0000313|EMBL:OGY67021.1};
OS   Candidatus Harrisonbacteria bacterium RIFCSPLOWO2_02_FULL_45_10c.
OC   Bacteria; Candidatus Harrisonbacteria.
OX   NCBI_TaxID=1798410 {ECO:0000313|EMBL:OGY67021.1, ECO:0000313|Proteomes:UP000176284};
RN   [1] {ECO:0000313|EMBL:OGY67021.1, ECO:0000313|Proteomes:UP000176284}
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   -!- 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:OGY67021.1}.
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DR   EMBL; MHJM01000034; OGY67021.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1ZRD4; -.
DR   STRING; 1798410.A3H63_01180; -.
DR   Proteomes; UP000176284; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd00075; HATPase; 1.
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; IPR000014; PAS.
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; PTHR43711:SF32; DRUG SENSORY PROTEIN A; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT 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; 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; PS50112; PAS; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        44..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          75..146
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          211..430
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   442 AA;  49326 MW;  3C6CD84C10BF6834 CRC64;
     MSDFFKKIKQ YLAYPEMKIL WLFLFLVSLI VIIDVIYLEE IFWILVSIII LASIGTVIAV
     NSIRTARLTE RLRLEKARLD TIISSMDDGV LVYDQDFRIL LFNPAAASIF GIPAQEAIGQ
     QLSPESVKNE KLKELAMTVF QSLAPQVVRQ TAEGVYPQIV DLSFTDPEQE LRVTTDRVLN
     SQGQVTGFLK IIRDRTREIG LLKSKSEFIA VAAHQLRTPL SAVSWTFESL KKDTLNDNQK
     ELADTGIAAS NNLLKIVEDL LNVSTIEEGK FGYNFQEIGL IGFIQGAVDS VSPVAREYQV
     KVFMEPFPEG EVAVTMDPEK IGLVMANLLE NAIKYNVANG QVVVSIERRN DGPFMQINVA
     DTGMGISEEA RQKLFTKFFR AGNAVTKETV GSGLGLYIVK NIIKRHGGQI WVDSEVGRGT
     TFHFTIPTDS RLIPPKEIGF VE
//