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Database: UniProt
Entry: A0A1G1WH80_9BACT
LinkDB: A0A1G1WH80_9BACT
Original site: A0A1G1WH80_9BACT 
ID   A0A1G1WH80_9BACT        Unreviewed;       493 AA.
AC   A0A1G1WH80;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   22-FEB-2023, entry version 14.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE   Flags: Fragment;
GN   ORFNames=A2Z42_01750 {ECO:0000313|EMBL:OGY27078.1};
OS   Candidatus Woykebacteria bacterium RBG_19FT_COMBO_43_10.
OC   Bacteria; Candidatus Woykebacteria.
OX   NCBI_TaxID=1802598 {ECO:0000313|EMBL:OGY27078.1, ECO:0000313|Proteomes:UP000176645};
RN   [1] {ECO:0000313|EMBL:OGY27078.1, ECO:0000313|Proteomes:UP000176645}
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:OGY27078.1}.
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DR   EMBL; MHCU01000049; OGY27078.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1WH80; -.
DR   Proteomes; UP000176645; 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; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
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        181..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          206..258
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          273..491
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          236..266
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         493
FT                   /evidence="ECO:0000313|EMBL:OGY27078.1"
SQ   SEQUENCE   493 AA;  55905 MW;  23CB9C26A2BB313B CRC64;
     MKIRGDPLSF RYSLRVKFSL ITAAIFLIIF GIVSFVLIRQ NIDFQKQSLL ARANTFSNLG
     TKPIGDAYNS YFQAGFLRFR EQLIDTLVLN EDIFRLQIIS VEGEILFDTI NLDRQNGETV
     EKMEDPEILQ AVSARQPTQL TGQNGDVDEI IVPYSDDFGA RPFSVRYFIS YESIYKEVDR
     IILTIGLLTV AVLVVTLVAM TVFVYLLILK PLGRIIDAAG EITRGNLRQK IDLATRDELA
     ELANSLNQMT ERLKKNIEDL KQLDKLKNEF VYLASHNLRS PLTAIKGYID ILLKNKSLDR
     EAKEASGKIA VSSARLEELT ESLLNLVALE ENKQPLLMKS VDLEELLEAL AEKFAASISE
     KRISLIFEFS PGEIPKIDLD EPRISQALES LLENAIKFNR EEGKIIVGLK RIKDYLRLSI
     KDTGIGIPKK ERERVFQKFH RATDILTYDY EGIGLGLYVT KLIIEAHQGR IWFESEAGAG
     TTFYVELPLK EVD
//
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