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Database: UniProt
Entry: A0A1H9KN46_9BURK
LinkDB: A0A1H9KN46_9BURK
Original site: A0A1H9KN46_9BURK 
ID   A0A1H9KN46_9BURK        Unreviewed;       892 AA.
AC   A0A1H9KN46;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN02982919_01605 {ECO:0000313|EMBL:SER00512.1};
OS   Giesbergeria anulus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Giesbergeria.
OX   NCBI_TaxID=180197 {ECO:0000313|EMBL:SER00512.1, ECO:0000313|Proteomes:UP000199766};
RN   [1] {ECO:0000313|EMBL:SER00512.1, ECO:0000313|Proteomes:UP000199766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35958 {ECO:0000313|EMBL:SER00512.1,
RC   ECO:0000313|Proteomes:UP000199766};
RA   de Groot N.N.;
RL   Submitted (OCT-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};
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DR   EMBL; FOGD01000003; SER00512.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9KN46; -.
DR   STRING; 180197.SAMN02982919_01605; -.
DR   OrthoDB; 8552871at2; -.
DR   Proteomes; UP000199766; Unassembled WGS sequence.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 4.
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; 4.
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; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 4.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF13188; PAS_8; 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; 4.
DR   SMART; SM00091; PAS; 4.
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); 4.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 4.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199766}.
FT   DOMAIN          3..58
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          73..127
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          128..186
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          208..262
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          256..328
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          332..385
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          382..453
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          526..742
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          767..884
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         817
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   892 AA;  98635 MW;  A3F0AF2DEA5E2494 CRC64;
     MTSTEILRHA LDQHAIVSLT DAAGNILEVN DKFCTISGYR REELLGQNHR ALKSGRHPAQ
     FYEEMWNTIS AGHTWQGDLC NRARDGKEYW VRSTITPIPG ADGLPEKYIS IRTDITYIKA
     VDLVLRENEL RYRSLVNSVS VGIVLHNRHG AITECNPAAE QILGLPREQI LERLHADAVW
     RCIHPDGRAF ADTDYPAIQT LRTGVSLRDV LMGVYRADGS LVWLSASSEP IRAPDNPQQI
     SAAVVSFVNV TESRYIETRF AFAVEGAGDG VWDWNIATGV ISFSGNYEGM LGYAKGELSN
     DITHLIAMVY PQDLPGVQKN LTDYLEGRVP HYTVEVRLRC KDSSYKWVLC RGTVVQHNAD
     GKPARMIGIH SDISAQKQAE NELLVFRRLV ESTDQAIRVA DRDGRIQYVN PAYQALLGYQ
     AEEVIGQDFA LIGTAPDQNQ QVQGIMDCLS RSEGWRGLFK LRRKDGSEFI SQSNIRSITS
     PESGELLHSF NMFIDYSEEM ARQEALITAR EAADRANQAK SDFLSSMSHE LRTPMNAIIG
     FAQMLEYDSE LTADQQDNVH EILKAGRHLL DLINEVLDLA KIESGRVDLS MEGIDLAVLG
     EDCRQLLQPI ADQAGIHLGI ELPSKSVVFA DRVRLKQVLL NLLSNAIKYN RPHGTVRLSV
     TASKPGYLRL AVADTGLGIA SKRITELFQP FNRLGAEASE IEGTGIGLTI TRRLVEMMGG
     EISVESTLGV GSTFWVNLAV GLTAQIGTDE MLNDANTPVE VGMATSTVLA IDDNPANLKL
     IAKVMGTRDN IHLLSAHTPE LGIELALAHR PDLILLDINM PGMDGYQVLE VLKSHMVLRA
     IPVIAVTANA MPHDIERGKR AGFANYMTKP IQISALMETI EYCLKDTKKP LP
//
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