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Database: UniProt
Entry: A0A398BJS4_9BACI
LinkDB: A0A398BJS4_9BACI
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ID   A0A398BJS4_9BACI        Unreviewed;       594 AA.
AC   A0A398BJS4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=D1953_01515 {ECO:0000313|EMBL:RID89271.1};
OS   Peribacillus asahii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX   NCBI_TaxID=228899 {ECO:0000313|EMBL:RID89271.1, ECO:0000313|Proteomes:UP000266016};
RN   [1] {ECO:0000313|EMBL:RID89271.1, ECO:0000313|Proteomes:UP000266016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MA001 {ECO:0000313|EMBL:RID89271.1,
RC   ECO:0000313|Proteomes:UP000266016};
RA   Seuylemezian A., Vaishampayan P.;
RT   "Bacillus jemisoniae sp. nov., Bacillus chryseoplanitiae sp. nov., Bacillus
RT   resnikiae sp. nov., and Bacillus frankliniae sp. nov., isolated from Viking
RT   spacecraft and associated surfaces.";
RL   Submitted (AUG-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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:RID89271.1}.
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DR   EMBL; QWVS01000002; RID89271.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A398BJS4; -.
DR   Proteomes; UP000266016; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 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   Gene3D; 3.30.450.20; PAS 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; IPR041328; HisK_sensor.
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; 1.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF18698; HisK_sensor; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266016};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        173..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          194..246
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          372..591
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   594 AA;  66958 MW;  D1034041F185DEFA CRC64;
     MFWRSVVGKL WGTILLLVCF VLLVLTVLLV EFFENFQIET VENDLTKVAK QIVSVTNDHS
     NAIDVLQISS ELIGDETKML VLHDEEIVFS SLRDVNNQIT PQFLKEDRDL LKVFTDEKIV
     KKEMLLPASS KDEEKVSAIV VGIPLELNGE RDEVFLVQSL ESMEEAIQST TRFILLAAGV
     AIILTTIFAF FLSTRINAPL RKMREAALAV ARGKFDTKIP VLTQDEIGEL AIAFSQMAKQ
     LKYNMTALSE EKEHLASILS SMADGVITFS KNGTILEVNP PAERFLQGVY FEKGFSPEGS
     KNVPQVLMNL FDESERQGKE QIGEITLQGH HWGLIVSPLY SNDGTIRGAV AVIRDITDER
     RMDKLRTDFI ANVSHELRTP ISMLQGYSEA LVDDIAGNEE DKKEMSRIIY DESLRMGRLV
     NDLLDLARLE SGNMRLRYEQ VELMSYLTRI TSKFQVIAKE KDIKLSVDLE DTKIEWDFDP
     DRIEQVLTNL IDNAIRHTLK GGSVEVGQRK SDRGGLIIYV KDTGSGIPEE DLPFVFERFY
     KADKARTRGR SGTGLGLSIA KNIIDAHEGY MSVNSRLNEG TMFSFVLPMR QKSK
//
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