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Database: UniProt
Entry: A0A433HB87_9BACI
LinkDB: A0A433HB87_9BACI
Original site: A0A433HB87_9BACI 
ID   A0A433HB87_9BACI        Unreviewed;       334 AA.
AC   A0A433HB87;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ELQ35_19955 {ECO:0000313|EMBL:RUQ25528.1};
OS   Peribacillus cavernae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX   NCBI_TaxID=1674310 {ECO:0000313|EMBL:RUQ25528.1, ECO:0000313|Proteomes:UP000267430};
RN   [1] {ECO:0000313|EMBL:RUQ25528.1, ECO:0000313|Proteomes:UP000267430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L5 {ECO:0000313|EMBL:RUQ25528.1,
RC   ECO:0000313|Proteomes:UP000267430};
RA   Seuylemezian A., Vaishampayan P.;
RT   "Bacillus chawlae sp. nov., Bacillus glennii sp. nov., and Bacillus saganii
RT   sp. nov. Isolated from the Vehicle Assembly Building at Kennedy Space
RT   Center where the Viking Spacecraft were Assembled.";
RL   Submitted (DEC-2018) 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:RUQ25528.1}.
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DR   EMBL; RYZZ01000040; RUQ25528.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433HB87; -.
DR   OrthoDB; 9780487at2; -.
DR   Proteomes; UP000267430; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF2; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000313|EMBL:RUQ25528.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267430};
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        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          121..326
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   334 AA;  39383 MW;  933271E9840682A5 CRC64;
     MIRRFIAERR SWILFFLFQL LILLFIAYLD PSISLSAMSY IVFLSLVLFI FFLFLRYQRE
     TAFFKQLEER VNDLDLSSLT TSRSPFETIV EKSIIEQTEH LKQTASRNRV QMEQEKDEML
     SWIHEVKTPL TALHLMIQRM EDDQLKARLT YEWLRIHLLL DQQLHQKRIP FIENDLYMED
     TDIETLLFTE LKTLQSWCIQ KGIGFDFDLQ VTHVLSDSKW LAFIIRQILT NAVKYSESSD
     IIIRSYLKAD RTFLDITDHG RGIDSRDLSR IFDKGFTSTT VHHDQASTGM GLYLAKKAAD
     SLHIKMSVNS KVNYRTTFTL AFPRKNEFVH IIGM
//
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