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Database: UniProt
Entry: A0A103E6K4_9BURK
LinkDB: A0A103E6K4_9BURK
Original site: A0A103E6K4_9BURK 
ID   A0A103E6K4_9BURK        Unreviewed;       436 AA.
AC   A0A103E6K4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=WS67_05530 {ECO:0000313|EMBL:KVE29315.1};
OS   Burkholderia singularis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=1503053 {ECO:0000313|EMBL:KVE29315.1, ECO:0000313|Proteomes:UP000062788};
RN   [1] {ECO:0000313|EMBL:KVE29315.1, ECO:0000313|Proteomes:UP000062788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSV85 {ECO:0000313|EMBL:KVE29315.1,
RC   ECO:0000313|Proteomes:UP000062788};
RA   Sahl J., Keim P., Wagner D.;
RT   "Expanding the genomic diversity of Burkholderia species for the
RT   development of highly accurate diagnostics.";
RL   Submitted (NOV-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   -!- 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:KVE29315.1}.
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DR   EMBL; LOWA01000014; KVE29315.1; -; Genomic_DNA.
DR   RefSeq; WP_059513819.1; NZ_LOWA01000014.1.
DR   AlphaFoldDB; A0A103E6K4; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000062788; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
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; 1.
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; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR021766; PhoR.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR014310; Sig_transdc_His_kinase_PhoR.
DR   NCBIfam; TIGR02966; phoR_proteo; 1.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF11808; PhoR; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KVE29315.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062788};
KW   Transferase {ECO:0000313|EMBL:KVE29315.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          213..428
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   436 AA;  49231 MW;  6A19FC42CFCD7C63 CRC64;
     MNIIWARFLV SLVLLALVGV LIAVFAGVAA ALAFMLVMLV VQGFFSTFHT QRLWRLLDAP
     VYGEVPSAPG IWGEIYYRLH KLAKQWHAQV RQVEQQHSRF IQAIQASPNG VVMLDDHDQI
     EWCNAIAEVH FGLDTKRDLR QHITHLVRHP DFVRYLNDQR YDETLVMRAM GGSRQNVLAV
     QVFPYGENRK LLLTQDITEL ERTDAMRRDF VANVSHELKT PLTVLSGFLE TLRELPLADD
     ERARYLELME QQASRMRSIV TDLLVLAKLE GETNPPADRA VDMQAVLDHL KDDAQTLSNG
     HHDIMFDIDE TLTVTGSQTE IFSALGNLVT NAVRYTPEGG KIRVEWRRDG AQAVFSVTDS
     GLGIPAADLP RLTERFYRVD RSRSRDTGGT GLGLAICKHV LQRHDAQLLI QSEEGRGSTF
     SARFPAHRTI GRRHAA
//
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