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Database: UniProt
Entry: A0A1I1QN90_9FLAO
LinkDB: A0A1I1QN90_9FLAO
Original site: A0A1I1QN90_9FLAO 
ID   A0A1I1QN90_9FLAO        Unreviewed;       454 AA.
AC   A0A1I1QN90;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05216297_105210 {ECO:0000313|EMBL:SFD19530.1};
OS   Flavobacterium phragmitis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=739143 {ECO:0000313|EMBL:SFD19530.1, ECO:0000313|Proteomes:UP000199672};
RN   [1] {ECO:0000313|EMBL:SFD19530.1, ECO:0000313|Proteomes:UP000199672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10370 {ECO:0000313|EMBL:SFD19530.1,
RC   ECO:0000313|Proteomes:UP000199672};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; FOMH01000005; SFD19530.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1QN90; -.
DR   STRING; 739143.SAMN05216297_105210; -.
DR   OrthoDB; 594725at2; -.
DR   Proteomes; UP000199672; 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; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; 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   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SFD19530.1};
KW   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        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        156..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          175..228
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          236..454
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   454 AA;  52579 MW;  D77EF6079FCEAAED CRC64;
     MKLVTRTALT YAILTAFILF VFAYSVYFVS EKNRKDEFFD RLDYKIIWRA EFIFDAQINK
     DLIKFLHTKN KKVLNEADIS VYDSNFNLYF SDNMPPLGNQ KILESIKRNK FLNWADEKYQ
     YRGILYKDNH QEYYIVGRAI DVTGLNHINA FKENVLYVYF ISIVLVFIIG FGFSYYTLKP
     LKDIIFQIRD ISEHNLNKRI VVPKAKDELY ELTQTFNTTF NRLEKSFNNH RNFVTTISHE
     FRTPLSILIA EIELGKELNQ TVDDYKKSLD NALEEANHVS QLSTALLDFA RANYDISQIK
     MSPTRIDEVL VDAKLNLINK KEVKYKIGIS YMNLDNTDSS VYNYTGNPYL LQIAFSNIME
     NACKYSENHS CNVEINASSE KITLTFSDDG IGIPEADLEK IYNLFYRGKN KDHENGYGIG
     LSIVKQIISL HNGSIEVISK VGKGTIFTVI LPLQ
//
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