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Database: UniProt
Entry: A0A1G3PRK6_9SPIR
LinkDB: A0A1G3PRK6_9SPIR
Original site: A0A1G3PRK6_9SPIR 
ID   A0A1G3PRK6_9SPIR        Unreviewed;       614 AA.
AC   A0A1G3PRK6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A2Y33_08395 {ECO:0000313|EMBL:OHD56970.1};
OS   Spirochaetes bacterium GWF1_51_8.
OC   Bacteria; Spirochaetota.
OX   NCBI_TaxID=1802190 {ECO:0000313|EMBL:OHD56970.1, ECO:0000313|Proteomes:UP000177109};
RN   [1] {ECO:0000313|EMBL:OHD56970.1, ECO:0000313|Proteomes:UP000177109}
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:OHD56970.1}.
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DR   EMBL; MIBE01000011; OHD56970.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G3PRK6; -.
DR   STRING; 1802190.A2Y33_08395; -.
DR   Proteomes; UP000177109; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; 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   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 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; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          397..607
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   614 AA;  70095 MW;  F3CB46A2C534EA18 CRC64;
     MFLIDDAPLK SFLIDLISSL SPKYVLLFRD EVFSSVITES DLKRSGKLQV SDQIAEILKD
     SPHRLALLLD DEHLKVWSEE NPELRRLLPH FNKLFDSSYK EMQAKSDEQS MIESAFSDLY
     NAFAVNIGDE FLFSYLIGTI VKFLNAEVGL LQIFNENETL NFSMGFKAES LKNIKMDGKE
     FRDYLYNTKE ILLIDSVVRE NRLSVADSDR QHLKTILAVP IFNKGVLVAI IYLVNKSYSA
     VNESFTGADK RFIANLSIQI GAIITNALLY KKTIELKEFN EEVLENIPVG ILNSSTDGTT
     LFTNRYMREL VYSMNMSIEA VIGLIESYNL PEFFGKELHI QRAERDFYLS VSKRILNIGF
     KPVVNLYTVF DITDEKEIEG QLRKSEKLAS AGELISSIAH EIKNPLTSIK GFADLLWQRI
     HDEEFVLKFA NIVSREINRL NNIIERFLSF AKPQIGVLAT IDLNAIIHEV SEVIAYSLKE
     SDVSLVMNMK EDIIVYGNRE LLSQVFMNIV LNSIQALREI KRKKKTIRID EEIVSGFAEI
     VIEDNGEGIK KEDLDKVFNP FYTTKSKGSG LGLSISHRIV TEHKGTLLID SKEGEYTRLI
     IRLPVFEKSR IEEK
//
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