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Database: UniProt
Entry: A0A5C8NV72_9BACI
LinkDB: A0A5C8NV72_9BACI
Original site: A0A5C8NV72_9BACI 
ID   A0A5C8NV72_9BACI        Unreviewed;       523 AA.
AC   A0A5C8NV72;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   18-JUN-2025, entry version 26.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=FHP05_07850 {ECO:0000313|EMBL:TXL65042.1};
OS   Cerasibacillus terrae.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Cerasibacillus.
OX   NCBI_TaxID=2498845 {ECO:0000313|EMBL:TXL65042.1, ECO:0000313|Proteomes:UP000321574};
RN   [1] {ECO:0000313|EMBL:TXL65042.1, ECO:0000313|Proteomes:UP000321574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-CFT480 {ECO:0000313|EMBL:TXL65042.1,
RC   ECO:0000313|Proteomes:UP000321574};
RA   Lin S.-Y., Tsai C.-F., Young C.-C.;
RT   "Cerasibacillus sp. nov., isolated from maize field.";
RL   Submitted (JUN-2019) 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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:TXL65042.1}.
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DR   EMBL; VDUW01000004; TXL65042.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5C8NV72; -.
DR   OrthoDB; 9792686at2; -.
DR   Proteomes; UP000321574; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd00130; PAS; 1.
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; 2.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR033463; sCache_3.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR   InterPro; IPR039506; SPOB_a.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43547:SF3; SENSOR PROTEIN CITS; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF17203; sCache_3_2; 1.
DR   Pfam; PF14689; SPOB_a; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:TXL65042.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000321574};
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        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        166..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          217..250
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          332..523
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   523 AA;  58361 MW;  E60B2FF107478F5F CRC64;
     MKKISLRTKI LVLIIGLILF VTILLTVFYS LIESSNTEDE IGDKALQFAT MISFMPTIKE
     AFATESPEEI IQPIAEEIRM MTGAEFVVIG NTKSIRYSHP TPTKVGKKMI GGDNDKALLK
     GQYYISKATG SLGPSLRGKA PIFNEKGEII GIVSVGFMID DVKTIIFSRL LTIGKVSFFV
     LLIGVMGGIL LARDIRKDIL GLEPYEIVSL YRDRDAILAS VHEGIIAIDE KGMITMMNQS
     AKSILGITED FYSKGFDEVF PELEVTLKHD NYGRVNNQEF IVNQRHVIIN VTPIIENDSI
     EGAVISFRDK TEIKEMIHTL AEVRKYSEDL RAQTHEYTNK LYVLSGLLQL EKYDEAIDLL
     QIEASYTSSQ NKILFEQIKD PTVQALLLGK LAKSSELKIE LIINPNSYLN RIPNTIKRTK
     VITIIGNLLD NALEAVIHFS KKEVTFFAID IGDDIIFEIA DSGPGITNSE ISQIFNRGYS
     TKRDKNRGHG LALVKETLSE LNGQIEINHG SEGGMIFSVF IPK
//
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