ID B7JPG5_BACC0 Unreviewed; 534 AA.
AC B7JPG5;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=BCAH820_0632 {ECO:0000313|EMBL:ACK90362.1};
OS Bacillus cereus (strain AH820).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405535 {ECO:0000313|EMBL:ACK90362.1, ECO:0000313|Proteomes:UP000001363};
RN [1] {ECO:0000313|EMBL:ACK90362.1, ECO:0000313|Proteomes:UP000001363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH820 {ECO:0000313|EMBL:ACK90362.1,
RC ECO:0000313|Proteomes:UP000001363};
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH820.";
RL Submitted (OCT-2008) 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}.
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DR EMBL; CP001283; ACK90362.1; -; Genomic_DNA.
DR RefSeq; WP_000746416.1; NC_011773.1.
DR AlphaFoldDB; B7JPG5; -.
DR KEGG; bcu:BCAH820_0632; -.
DR HOGENOM; CLU_020211_11_2_9; -.
DR Proteomes; UP000001363; 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:ACK90362.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACK90362.1};
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; 59659 MW; 069FC3E63871F3D2 CRC64;
MKKRKRLWNL WKTITLLVCT VVIFSLLVTD ILISHNVERT TEDSQAEKAK TIAHIVANDS
IVIDGLIGKA DTSAIQTYTN RILKNTGVQF IVVMDMNGIR KSHPNPQKIG YHFIGGDEGP
ALKGKEHVSL AEGTLGISMR VFVPVFSETG EQLGAVAVGI SADNVKERVK 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
//
