ID A0A0D6ZF94_9BACI Unreviewed; 468 AA.
AC A0A0D6ZF94;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=UB32_00210 {ECO:0000313|EMBL:KIY23945.1};
OS Mesobacillus subterraneus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=285983 {ECO:0000313|EMBL:KIY23945.1, ECO:0000313|Proteomes:UP000032512};
RN [1] {ECO:0000313|EMBL:KIY23945.1, ECO:0000313|Proteomes:UP000032512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MITOT1 {ECO:0000313|EMBL:KIY23945.1,
RC ECO:0000313|Proteomes:UP000032512};
RA Peet K.C., Thompson J.R.;
RT "Draft genome sequences of the supercritical CO2 tolerant bacteria Bacillus
RT subterraneus MITOT1 and Bacillus cereus MIT0214.";
RL Submitted (JAN-2015) 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:KIY23945.1}.
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DR EMBL; JXIQ01000001; KIY23945.1; -; Genomic_DNA.
DR RefSeq; WP_044390203.1; NZ_JXIQ01000001.1.
DR AlphaFoldDB; A0A0D6ZF94; -.
DR PATRIC; fig|285983.3.peg.47; -.
DR OrthoDB; 3436at2; -.
DR Proteomes; UP000032512; 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 CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 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 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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KIY23945.1};
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:UP000032512};
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 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 186..238
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 253..468
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 226..253
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 468 AA; 54074 MW; 2C4DD7DE468BA381 CRC64;
MKVKYIYQQF LSHISIIIVA FLILSLVFTK YVETLVYKNK TEELVSYGEN ILRDLDRGVE
LPDQVINQYA RVLFGRDIQF SVFDENIQLL NPIKWRGPAI ELTEKEWSQL TNGKPIVKNY
DLERYNRAVT LVVLPYLDRG RFVGGILLTS PISGTRETIA EINKYLFYTM LIGLFVSFLL
SWILSRIHVN RIKKLQEATS TVSAGDYTVK VPSSDFDEIG ELAKDFNSMV DKLNESKSEI
VNLENRRRQF MSDVSHELRT PLTTISGIVE GLRNDMIPEA EKERGINLVS QETKRLIRLV
NENLDYDKIR SNQVQLHLED IELVEVFEII QEQLELQAGE RNNQIRIEVE DSAKVHADYD
RLVQILINIT KNSIQFTENG MITLRGRKRE QMTVMEIEDT GIGIDPAEIE KIWHRFYKAD
LSRTSNPFGE FGLGLSIVKQ LVQMHKGKIK VESEHGKGTK FVIELPFR
//
