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Database: UniProt
Entry: A0A1F3NUT3_9BACT
LinkDB: A0A1F3NUT3_9BACT
Original site: A0A1F3NUT3_9BACT 
ID   A0A1F3NUT3_9BACT        Unreviewed;      1075 AA.
AC   A0A1F3NUT3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Histidine kinase domain-containing protein {ECO:0000259|PROSITE:PS50109};
GN   ORFNames=A3G23_06480 {ECO:0000313|EMBL:OFY69189.1};
OS   Bacteroidetes bacterium RIFCSPLOWO2_12_FULL_37_12.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1797365 {ECO:0000313|EMBL:OFY69189.1, ECO:0000313|Proteomes:UP000176497};
RN   [1] {ECO:0000313|EMBL:OFY69189.1, ECO:0000313|Proteomes:UP000176497}
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   -!- 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:OFY69189.1}.
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DR   EMBL; MEPC01000038; OFY69189.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F3NUT3; -.
DR   STRING; 1797365.A3G23_06480; -.
DR   Proteomes; UP000176497; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   Gene3D; 1.20.5.1930; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011110; Reg_prop.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR011123; Y_Y_Y.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF07494; Reg_prop; 4.
DR   Pfam; PF07495; Y_Y_Y; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
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};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        59..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        830..855
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          883..1075
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   1075 AA;  123181 MW;  5D7082C583638B29 CRC64;
     MLYNKAFVVF SLSISALGMK INIFQKVKSM LHPLTAGIIK QSPSIHRLTG SCFLHTKKFF
     FKFFFSIIFF LLSLSLFSQY RIKHIGLEQG LSQSSVHCIF KDTDGLMWFG TQDGLNRFDG
     YSFKIFHHDK NDSTTISDDF VLEIIEDNTN NLWVCTRNGL NRFDKKTETF TRIFLEGMDK
     NYYHNIFRSF FKDNNGDLVF HSVGKTGIAL IGDDGNFQIK SEPSQFWKHD IFCYDSNGNI
     FISDSLGIWF YEYKNNSYAK PKELFLPAIT NLHVTAMTVS NKNQLWVGEK NKLHVINIEN
     KKHQTLSLPL ELIQRISESH DGNYWVGGEN GICVLDSQLN SITLLKNSPE DEKDLTSYSF
     TQIYHDRNGL VWLGTSDNGL SVFNPQKIFT TFKMKKNDKN SLSDNSVWSI FQNGKRLFIG
     TNSGLNVFFL NSENFFNYKK FEDNILSKQI LPYELLAFNT RAITIDKSEN IWIGGSKGIM
     VLDLSGKILK TFTTENSGLS HNNIFHLLTT KDGSIWISTP FCLNRYNPKT NSFEIYKNDS
     SNNSLPVNYI ISTMEDQGGI LWISTSNGLS LFNPNTKVFK NHLSEYNSKK SLSYNIVSSV
     LEDKRGRIWV STLGGGINFF DREKEIFTSY TTADGLLNNV IYGIVEDEKG TLWMSSNRGI
     SSFNPDTKVF SNYNVNDGIV SNEFSQNSFF KNDNGEIFFG SPEGLLIFNP DELIEQNILP
     KLVLTGVSVN YRKIIPYEIA RKKSIDLFYG DKTISFEFAE PDFINAEKIS YSFLLEGFNK
     KWVEVNSGQR IATFTNLPYR KFKFKVRTKK NNNRWSEPAL NITVNVIPPF WMRGWFITTG
     AFFFLLILIF TVKFFSQRKL RKKLREIELQ RKIQMERERI SRDLHDNVGS HLTYIVTSLD
     NISHKLEKGE KGISEEKISS LSDFSRETIQ QLRETIWAIN KESILLSELK DKVNDHFLKI
     HDLTEHINFS VEMESENNNE LKPSTAIHLF RIVQEAVNNC VKHSGAKTIS VKISTMGNYL
     TIIIADDGKG IVQTENGNNH CGLENMKIRM KEIGGVFALN SKDGVGTEVI ISLCL
//
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