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Database: UniProt
Entry: A0A147HC86_9BURK
LinkDB: A0A147HC86_9BURK
Original site: A0A147HC86_9BURK 
ID   A0A147HC86_9BURK        Unreviewed;       548 AA.
AC   A0A147HC86;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=NS331_01465 {ECO:0000313|EMBL:KTT27554.1};
OS   Pseudacidovorax intermedius.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Pseudacidovorax.
OX   NCBI_TaxID=433924 {ECO:0000313|EMBL:KTT27554.1, ECO:0000313|Proteomes:UP000072741};
RN   [1] {ECO:0000313|EMBL:KTT27554.1, ECO:0000313|Proteomes:UP000072741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NS331 {ECO:0000313|EMBL:KTT27554.1,
RC   ECO:0000313|Proteomes:UP000072741};
RX   PubMed=26793183;
RA   Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA   Patil P.B.;
RT   "Genomic Resource of Rice Seed Associated Bacteria.";
RL   Front. Microbiol. 6:1551-1551(2016).
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:KTT27554.1}.
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DR   EMBL; LDSL01000011; KTT27554.1; -; Genomic_DNA.
DR   RefSeq; WP_058640251.1; NZ_LDSL01000011.1.
DR   AlphaFoldDB; A0A147HC86; -.
DR   PATRIC; fig|433924.3.peg.294; -.
DR   OrthoDB; 9792270at2; -.
DR   Proteomes; UP000072741; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-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; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KTT27554.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000072741};
KW   Transferase {ECO:0000313|EMBL:KTT27554.1}.
FT   DOMAIN          30..103
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          104..158
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          171..398
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          418..537
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         471
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   548 AA;  59987 MW;  114DF1B82C9CBE7A CRC64;
     MTRSPEKPSL QPSRLPIRAE GTPGEVRDHK DDIFFAAIEM TRMPMLVTDP RQPDNPIVFA
     NRAFLSMTGY TPEELIGTNC RFLQGPATDR ASVAVIREAI ESRTEVQIEL LNYRKDGSTF
     WNALFISPVY NPAGELVYFF ASQLDVSRRR DAEEGLAQAQ KMEALGQLTG GISHDFNNLL
     QVMSGHLDLL EVRGRMNKLD PEHVGRGVEN IREAVSKASK LTSQLLAFSR KQSLRGRVIN
     LNAVTKDMTD LAQRTLGEQI QVVFKFEQDI GNCQLDPTQL EVALLNVLVN ARDAMPEGGT
     LTIQTGSVEV SDDDTPAFSG LAPGRYSTLS VTDTGTGIDK ALLARVMDPF FTTKEEGKGT
     GLGLSMVYGF VKQSGGTVTM YSEVGIGTTV RMYFPTVDAR PAVATRSAHP AYRGGTERIL
     LVEDREEVGL LAQEMLEGLG YTVLMANSAQ QALRVFRGLA PEAQPDLLFS DVVMPGGMNG
     YTLAREIQKL RPSTRVLLTT GFDRDLGSLD HVAPAEFEIL KKPYRLGDLA RKVRDVLDGP
     TGSHSTAG
//
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