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Database: UniProt
Entry: V6MKU8_9BACL
LinkDB: V6MKU8_9BACL
Original site: V6MKU8_9BACL 
ID   V6MKU8_9BACL            Unreviewed;       599 AA.
AC   V6MKU8;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=T458_01945 {ECO:0000313|EMBL:EST56098.1};
OS   Brevibacillus panacihumi W25.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1408254 {ECO:0000313|EMBL:EST56098.1, ECO:0000313|Proteomes:UP000017973};
RN   [1] {ECO:0000313|EMBL:EST56098.1, ECO:0000313|Proteomes:UP000017973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W25 {ECO:0000313|EMBL:EST56098.1,
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:EST56098.1}.
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DR   EMBL; AYJU01000001; EST56098.1; -; Genomic_DNA.
DR   RefSeq; WP_023554476.1; NZ_KI629782.1.
DR   AlphaFoldDB; V6MKU8; -.
DR   STRING; 1408254.T458_01945; -.
DR   PATRIC; fig|1408254.3.peg.397; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_2_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; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 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   Gene3D; 3.30.450.20; PAS 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; IPR041328; HisK_sensor.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_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; PF18698; HisK_sensor; 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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 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:EST56098.1};
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        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          208..260
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          378..596
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   599 AA;  66972 MW;  B4240DAEC8D43B2B CRC64;
     MDVIFRSVVG KLWMTIIALF ALVLTVFSLL LVQSFDNFYH NRQTSNLQDL AIGLRDGLAQ
     SEDKQSALEL ASRFGLVHHT GLVVVDEQKN IIGKSEGKPL PRIPVDQLLA EKGLKLTEAI
     EGKHPLPERF SLSLSEPDRN NPAARNGTLP ILAVAVPLEI SSGHKGAVVL YQTIEDFDDT
     LTEVRLLIFV VGVIAFTATT FFAFFLSSRI TSPLRQMKET AHRIAEGDFH AEIPIRTTDE
     IGELAASLNT MATRLNQLVD ALSKEKEQLA SVLRSMVDGV VMIDGEGNVV VANPPAEHFL
     RDWRYEHPDE PFPLYGYYQQ VVRGGYEVAE DIPVQGRIWS LVMVPLMDKE QIRGAVAVIR
     DMTRERKLDK MRNDFVANVS HELRTPLSML QGYSEAIVDD MVATPEEHKE LAQIIYDESV
     RMTKLVNELL SLARMEAGHV ELFKERVELR PYLERIHRKF SNLAREQDIS LSLEVTTPHQ
     HADFDPDRME QVLTNLIDNA LRHTPSHGSV MIRARGEKVL WLEISDTGSG IPQEDLPFVF
     ERFYKADKAR TRGRAGGTGL GLAIAKNIID AHGGTISVQS KLGEGTTFTI SILVDTKTN
//
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