ID   A0A285ZT64_9SPHI        Unreviewed;       741 AA.
AC   A0A285ZT64;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN06297358_0878 {ECO:0000313|EMBL:SOD12844.1};
OS   Pedobacter xixiisoli.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1476464 {ECO:0000313|EMBL:SOD12844.1, ECO:0000313|Proteomes:UP000219281};
RN   [1] {ECO:0000313|EMBL:SOD12844.1, ECO:0000313|Proteomes:UP000219281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12803 {ECO:0000313|EMBL:SOD12844.1,
RC   ECO:0000313|Proteomes:UP000219281};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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; OCMT01000001; SOD12844.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285ZT64; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000219281; Unassembled WGS sequence.
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; 3.
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; 4.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
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; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF13188; PAS_8; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 4.
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); 4.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          262..333
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          391..461
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          464..516
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          520..736
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   741 AA;  83605 MW;  2FC84177A0165040 CRC64;
     MDSNYSKNRF NDLIDAAPSA TAIYHTRDIV VTAANAQMLA FWGKDETVIG KPLIEAVPEL
     AGQPFIALLQ KVYDTGITHH AERDGAELLV DGKLQISYFN YTYKAILGVN GKTEAIIHSA
     INVTPLVKAQ QELSEMQERL SLALQSAEIG TWELAPVSEE VYWDQRCRAL FGFEGEADIN
     YHQVLDCIVA EDKQMVMDAV AAAVDPKRLA NYDVRFRTLG TASKKIRWVH CKGRAYLNEM
     GVTYRFAGTA RDITAEVNTS LNEQQMLSLV NYNADVMSIA DMQGNLIYMN HAGKKLLGVE
     ENTPMNSMTA RDFYEPEELR RVQETIIPQI DDEKGWTGTL CLKNSKTHEA IPCQVNYILI
     KNPITGEIIG RGATARDLRP ELKAKDKLAQ AMQEMEFLAN SVPTVVWTAT TEGMIDFVNK
     QWYEQSAVAI TDALGTGWTE LVHPDDLERT LVAWKNSLTT GMPYQAEFRL KDKHEKYRWW
     LVRAVALKDN NHNILKWYGS NTDITEQKEL QRQKDDFLGI ASHELKTPVT SIKAYAQIVE
     MMLKRSGDDK NLELIHKMNN QINRLTNLIA DLLDVTKINT GKLAFKPSIF DFDQLVAEVA
     DEIQVTSEQH KIEKKLNSNS LVDLDRDRLS QVISNLITNA IKYSPDAKKI IIQTEVSFNE
     VQFSVQDFGI GIASDKQEKI FEQFYRVSNT NEYAFPGLGL GLYISVEIIK QMNGRIWVNS
     EQDQGASFGF ALPLANGNQK F
//