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Database: UniProt
Entry: A0A150MZL5_9BACI
LinkDB: A0A150MZL5_9BACI
Original site: A0A150MZL5_9BACI 
ID   A0A150MZL5_9BACI        Unreviewed;       551 AA.
AC   A0A150MZL5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=B4110_3427 {ECO:0000313|EMBL:KYD29870.1};
OS   Parageobacillus toebii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Parageobacillus.
OX   NCBI_TaxID=153151 {ECO:0000313|EMBL:KYD29870.1, ECO:0000313|Proteomes:UP000075324};
RN   [1] {ECO:0000313|EMBL:KYD29870.1, ECO:0000313|Proteomes:UP000075324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4110 {ECO:0000313|EMBL:KYD29870.1,
RC   ECO:0000313|Proteomes:UP000075324};
RA   Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA   Eijlander R.T., Kuipers O.P.;
RT   "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT   Foods.";
RL   Submitted (JAN-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};
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:KYD29870.1}.
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DR   EMBL; LQYW01000061; KYD29870.1; -; Genomic_DNA.
DR   RefSeq; WP_062678139.1; NZ_LQYW01000061.1.
DR   AlphaFoldDB; A0A150MZL5; -.
DR   PATRIC; fig|153151.4.peg.3391; -.
DR   Proteomes; UP000075324; 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   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 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   Gene3D; 3.30.450.20; PAS 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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          336..551
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   551 AA;  63166 MW;  3269A53E5943FED0 CRC64;
     MEVKDRQQMI NLLTGVQSSK KSYYNELKKT VIELKKKNMQ LEIINDVTKS FNVDMSIDEM
     LKNVFDKLQT IFPIERISLS MYENEKLILT NVYPPHSLYF PIGFELSKEH SLYWKAVESL
     EKIFYQVDSN KENYEDYIEN KVYESLGIRS VLLVPLIHKG KVIGVFSIGS KEMMEYDEDD
     LTFFQQFCDQ LAVCIENARL YNEVLTSKKE WEETFRAVSE MILVVDLEGN ILKYNDAAKD
     FFQLHYKSEK RNFHQLLSLD IHNSPVLKMV QTKKPVYQEI HFQKRVCELR AYPVFNESQH
     IYAIIIYIND ITEKLRIEAQ LVQSGKLAAI GEMAAGIAHE LNNPLTAILG NAQLLLRTAD
     DRSYKLLSDI YSCGKRCKTI IQNLLTFSRQ DEYMFEDCSV NEAVEQVLGL IGDQIKKQNI
     TIQKKLDHSL ELIEGNIQQI GQIVLNLLIN AKDALEEMDI PKKVISIETK SVTEDGKKWI
     LLSVQDNGKG IEEQYLQEIF NPFFTTKRPG KGTGLGLSVS LGIAQAHGGT IEVISHPGKG
     STFMLKLPAK Q
//
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