ID V6M1N7_9BACL Unreviewed; 450 AA.
AC V6M1N7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=T458_14865 {ECO:0000313|EMBL:EST52267.1};
OS Brevibacillus panacihumi W25.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1408254 {ECO:0000313|EMBL:EST52267.1, ECO:0000313|Proteomes:UP000017973};
RN [1] {ECO:0000313|EMBL:EST52267.1, ECO:0000313|Proteomes:UP000017973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W25 {ECO:0000313|EMBL:EST52267.1,
RC ECO:0000313|Proteomes:UP000017973};
RX PubMed=24459276;
RA Wang X., Jin D., Zhou L., Wu L., An W., Chen Y., Zhao L.;
RT "Draft Genome Sequence of Brevibacillus panacihumi Strain W25, a
RT Halotolerant Hydrocarbon-Degrading Bacterium.";
RL Genome Announc. 2:e01215-13(2014).
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:EST52267.1}.
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DR EMBL; AYJU01000017; EST52267.1; -; Genomic_DNA.
DR RefSeq; WP_023556855.1; NZ_KI629785.1.
DR AlphaFoldDB; V6M1N7; -.
DR STRING; 1408254.T458_14865; -.
DR PATRIC; fig|1408254.3.peg.2903; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_6_9; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000017973; 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; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EST52267.1};
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:UP000017973};
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 7..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 171..223
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 231..450
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 450 AA; 49981 MW; 8DC378F5B9455AD4 CRC64;
MSVRRKLFFT IASFIVGMGI VYGLMTQFVI AGILKGVLDD DRSPQINALS QMFLDYYVQH
GESWSGVEQL DVKLPGVEQM EDVGYALLAK DTEGTLIKTG YVDVEQMLGL GIRKKLRWEG
NTIAILVYYD AEVAKSAKLH YGIRGSGIFV LLVGMILFVI LSLWVAFLLS KRLTAPLRAL
ITGIDRLGQG ELGVQVPVVT KDEYATVANA FNLMSTQLAQ AEKVRKNLTA DVAHELRTPL
TIIRGKLDQL QQEGRLIEPE RLLSLQDECI RLTKLVDDLH QLSLAEAKKL HLEKKWTSIP
DLLERCIERV KLDAEHKFIR VTLLSAPNIP LVEVDPNRMM QVFLNLLVNA VRYTPVGGKV
QVRVETGAGE TDTGKLLIQV SDTGEGIDAD QLPLLFNRFY RTDEARTRNK GGMGLGLAIS
QELVRLHEGS IEASSVRGKG TTFTVKLPIS
//
