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Database: UniProt
Entry: A0A023DC72_9BACI
LinkDB: A0A023DC72_9BACI
Original site: A0A023DC72_9BACI 
ID   A0A023DC72_9BACI        Unreviewed;       740 AA.
AC   A0A023DC72;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=kinE {ECO:0000313|EMBL:GAJ38903.1};
GN   ORFNames=GCA01S_010_00300 {ECO:0000313|EMBL:GAJ38903.1};
OS   Parageobacillus caldoxylosilyticus NBRC 107762.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX   NCBI_TaxID=1220594 {ECO:0000313|EMBL:GAJ38903.1, ECO:0000313|Proteomes:UP000023561};
RN   [1] {ECO:0000313|EMBL:GAJ38903.1, ECO:0000313|Proteomes:UP000023561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 107762 {ECO:0000313|EMBL:GAJ38903.1,
RC   ECO:0000313|Proteomes:UP000023561};
RA   Hosoyama A., Hosoyama Y., Katano-Makiyama Y., Tsuchikane K., Ohji S.,
RA   Ichikawa N., Yamazoe A., Fujita N.;
RT   "Whole genome shotgun sequence of Geobacillus caldoxylosilyticus NBRC
RT   107762.";
RL   Submitted (APR-2014) 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};
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:GAJ38903.1}.
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DR   EMBL; BAWO01000010; GAJ38903.1; -; Genomic_DNA.
DR   RefSeq; WP_042407478.1; NZ_BAWO01000010.1.
DR   AlphaFoldDB; A0A023DC72; -.
DR   OrthoDB; 9815750at2; -.
DR   Proteomes; UP000023561; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 4.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 4.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065:SF57; SPORULATION KINASE E; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 2.
DR   Pfam; PF13426; PAS_9; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
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; PS50112; PAS; 4.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:GAJ38903.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023561};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          30..87
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          151..221
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          272..327
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          392..462
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          524..730
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          10..37
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   740 AA;  85832 MW;  1DF40FD87AED2BEF CRC64;
     MSRNLSPREE KNVVVDVRLL EEENRRLKER LNSYSIIFER SLDAIVIFNK HGEFVDVNEA
     ACKLFEMDKC ELIGKKLSMF LELVPPDILM FQQSMLHKFG SFSDELLIKL ANGKVKHIEF
     SMKKDAFNEY DLVIMRDISA HKALERERIM HEFLFKDVFN RAVDSIVIFD EFGRFIDVNP
     AFCMSLNLEK AKLLNLSFQQ FIAKEDVDDF VRLLAELKEK GTAKGELSLV RLDGTVKMFE
     LTTTSNVYSG FYMAIMRDVT DRKNMEIKLQ KSEERFRAIF EQAHEAILIW DDYGYILNAN
     RAASRTFELP LNLLVRKNLL DFLDHNDEKV KRIFAEFRKK GEIRDELTFH MPNGEDKQLE
     FTMKKGAIDG YHLTIFRNVT ERRKIERELR ESEQKFRSIF DHAMDGILLW GQGYRILDVN
     PIACEIFQAG KEQLLHRPIT EFIPEKARKH FRKLIQQSER VGEAYAEVDF SNDGKQKIIE
     FALKKEIIPG VGMMMLRDIT ERKEMELQLR KSDTLNVVGE LAAGIAHEIR NPMTALKGFI
     QLLQGSIKED YSMYFNVIMS ELKRIESIIT EFLVLAKPQA IQYQQNDICK IMQDTIDLIN
     VQAMMHSVQI IADFAPQLPP IYCEPNQLKQ VFINILKNAI EVMPKGGDVT VRIRQSDDNH
     IRISITDQGC GIPKDKIKKL GEPFYTTKER GTGLGLMVSY KIIEEHQGKI DVESEVGVGT
     TFHITLPIKR VEKEDDHDEI
//
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