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Database: UniProt
Entry: C2NCT4_BACCE
LinkDB: C2NCT4_BACCE
Original site: C2NCT4_BACCE 
ID   C2NCT4_BACCE            Unreviewed;       534 AA.
AC   C2NCT4;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=bcere0004_4850 {ECO:0000313|EMBL:EEK58117.1};
OS   Bacillus cereus BGSC 6E1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=526970 {ECO:0000313|EMBL:EEK58117.1};
RN   [1] {ECO:0000313|EMBL:EEK58117.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGSC 6E1 {ECO:0000313|EMBL:EEK58117.1};
RX   PubMed=22645259; DOI=10.1101/gr.134437.111;
RA   Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA   Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA   Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT   "Genomic characterization of the Bacillus cereus sensu lato species:
RT   Backdrop to the evolution of Bacillus anthracis.";
RL   Genome Res. 22:1512-1524(2012).
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:EEK58117.1}.
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DR   EMBL; ACLU01000022; EEK58117.1; -; Genomic_DNA.
DR   RefSeq; WP_000746395.1; NZ_CM000716.1.
DR   AlphaFoldDB; C2NCT4; -.
DR   HOGENOM; CLU_020211_11_2_9; -.
DR   Proteomes; UP000000284; Chromosome.
DR   GO; GO:0005886; C:plasma 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   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
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; IPR039506; SPOB_a.
DR   PANTHER; PTHR43547:SF10; SENSOR HISTIDINE KINASE DCUS; 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   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   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:0000313|EMBL:EEK58117.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          317..529
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   534 AA;  59671 MW;  D8E3DCBDC2EB32D4 CRC64;
     MKKRKRLWNL WKTITLLVCI VVIFSLLVTD ILISHNVERT TEDSQAEKAK TIAHIVANDS
     IVIDGLIGKA DTSAIQTYTN RILKNTGVQF IVVMDMNGIR KSHPNPQKIG HHFIGGDEGP
     ALKGKEHVSL AEGTLGISMR VFVPVFSETG EQLGAVAVGI LADNVKERVK ESRHIIYIGV
     GVGVLVGMIG AILLARHIKK SLFGLEPHRI AKILEERNTM LQSVKEGIIA VDKEANVTLI
     NNEAKRLFKK SGLEEDFIGK DVELYMPNSR IKEVLQTGEV QLNEEQNIYG ITIVTNRVPL
     YVKGEIVGAI ATFRDKTEIR KLAEELTGIR LYAEALRAQS HEFMNKMHVV LGLTHMKQYE
     ELQKYISGMV SEHQYEIGGV MKRIKSPVFA GFLLGKLSYA REKNIKLIIS EDSYMPEIDD
     ESITHELITI VGNLIDNALE AVTNCEKKQV EVEIQYGNTL IITVQDTGKG IQEKEIEALF
     TKGYSTKGDN RGYGLYLVKE SIQRINGEIH MHSLVGKGTK ITIEIPKGRD ERQI
//
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