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Database: UniProt
Entry: A0A1Q8IWT9_9BURK
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ID   A0A1Q8IWT9_9BURK        Unreviewed;       990 AA.
AC   A0A1Q8IWT9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BTH42_13220 {ECO:0000313|EMBL:OLL31165.1};
OS   Burkholderia sp. SRS-W-2-2016.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1926878 {ECO:0000313|EMBL:OLL31165.1, ECO:0000313|Proteomes:UP000186182};
RN   [1] {ECO:0000313|Proteomes:UP000186182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRS-W-2-2016 {ECO:0000313|Proteomes:UP000186182};
RA   Chauhan A.;
RL   Submitted (DEC-2016) 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:OLL31165.1}.
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DR   EMBL; MSDV01000026; OLL31165.1; -; Genomic_DNA.
DR   RefSeq; WP_075299930.1; NZ_MSDV01000026.1.
DR   AlphaFoldDB; A0A1Q8IWT9; -.
DR   STRING; 1926878.BTH42_13220; -.
DR   Proteomes; UP000186182; 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   CDD; cd00156; REC; 1.
DR   CDD; cd18161; REC_hyHK_blue-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
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:SF49; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08448; PAS_4; 2.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 2.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000186182}.
FT   DOMAIN          31..88
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          90..142
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          229..287
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          394..449
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          487..710
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          730..846
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          876..987
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         780
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         925
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   990 AA;  108469 MW;  024BEF2FA17C69E7 CRC64;
     MQVNDQSVAG ATLSGNGHFE LMIERVRDYA IYLLTPAGLV KSWNEGAERI KGYSAAEIIG
     QHFSLFYTAE DRATDLPARA LDISVREGKF ESEGWRVRKD GSRFRAHVVL DALFDDAGHH
     IGYAKITRDI TAEYEARRSA EQQNQLALDA RNREYQELLR LFEQAPGFVC FFRGPEHVYQ
     LQNSAHHRLA GFRDILGKPV RQALPELVGQ GFFELLDEVY RSGKAFVGRA LPLRVDPLAA
     EKNEEGEVRF IDFVYQPIVD DHGAVVGIFS QGNDVTEQVL AQQALEHKQE ELERLVLERT
     AALEKTSQTL QLARELHLDK AHLLQLFEQA PGFICVLKTG QHIFELANSA YRSLVGERDL
     VGRRVQDALP EVTEQGFIEL LDRVFRTGQP FVGTSVPVKI QPRDSAKLET RFLDFVYQPI
     SGPDGEVIGI FVQGHDVTAQ KLAQDELQRY QTSLEALVQE RTRELEHTQT ALQRSQKLEA
     IGKLTGGIAH DFNNILQVIG GNLQLLQSHL IDDCPALNRV NTATSAVERG AKLSSQLLAF
     ARRQPLQPVA TNLAPVITGM DDMLRRALGE SVIIETVLAG GLWNVLVDPN QLENVVLNLA
     INARDAMPDG GKLSIELGNS MLDDDYVASD DDLLPGQYVL LAISDTGVGM TREVMERACD
     PFFTTKPEGT GTGLGLSMAY GFVKQSGGHF KIYSEPGHGS TIKIYLPRSH EAVVQTAPPV
     TLAVVGGSET ILVVEDDLAV QATVVEMLRE LGYHVLKADN AESALGILRS GLSIDLLFTD
     VVMPGTMRSP DLARRAKALL PDIEVLFTSG YTQNAIVHGG RLDAGVHLLT KPYRREQLAR
     KIRHLLSNGQ AAALARAEPP AAETEAAVPS PCRALHVLVV EDQPDLREMA VELIRMMGHH
     AQAAASGEEA IEVFARSGFD VLLTDVGLPG IDGVELSRQL VTVKPGLHVI FASGYGHAIG
     DGADRLGTVL PKPYTFAGLE TLLASFSGED
//
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