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Database: UniProt
Entry: J1EHG9_9BURK
LinkDB: J1EHG9_9BURK
Original site: J1EHG9_9BURK 
ID   J1EHG9_9BURK            Unreviewed;       619 AA.
AC   J1EHG9;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=PMI14_03623 {ECO:0000313|EMBL:EJE51684.1};
OS   Acidovorax sp. CF316.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1144317 {ECO:0000313|EMBL:EJE51684.1, ECO:0000313|Proteomes:UP000004811};
RN   [1] {ECO:0000313|EMBL:EJE51684.1, ECO:0000313|Proteomes:UP000004811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF316 {ECO:0000313|EMBL:EJE51684.1,
RC   ECO:0000313|Proteomes:UP000004811};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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:EJE51684.1}.
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DR   EMBL; AKJX01000134; EJE51684.1; -; Genomic_DNA.
DR   RefSeq; WP_007856333.1; NZ_AKJX01000134.1.
DR   AlphaFoldDB; J1EHG9; -.
DR   PATRIC; fig|1144317.3.peg.3300; -.
DR   Proteomes; UP000004811; 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; 3.
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; 3.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13426; PAS_9; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
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); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 3.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004811}.
FT   DOMAIN          11..73
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          127..180
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          204..254
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          248..300
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          325..375
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          393..613
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          600..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   619 AA;  67757 MW;  BA0CA9F96D49D265 CRC64;
     MASDFSGAHW EQNPDALLVI APDGTVLHWN PAAEATFGYT EAEARGRRLV QLIVPPDQVQ
     DEESICAKAL QSGLAVHESV RQRKDGSLVH VNVSTRAVFG ADGRLDYFLS SKKDVTQLKV
     LRDAKLVEAR FRDLLESTPD AIVMVNATGR IVLVNSQAER VFGYPRGQLL GQAIEVLLPQ
     RYRNAHLGHR SGFFAQPRTR TMGAGLELYG VRSDGSEFPV EISLSPLETE EGTMVMSAIR
     NITARKKADQ KFRDLLESAP DAMVIVDRDG HIVLVNSQAV KLFGWAREEL LGRQIELLVP
     VRHRSQHPHH RGGFFAEPRT RSMGAGLDLY GLRKDGTEFP VEISLSPLET EEGLFVSSAI
     RDVTERKRFE QALRDKNLEL ENAARVKDRF LASMSHELRT PLNAIIGFTG TLLMRLPGPL
     NTEQEKQLRI VQTGARHLLS LINDLLDVAK LGDGSHSLQL EAMDCRAVVE EVAATLGPDA
     QRKGLAFLVS VPGQAVLART DRRALTQVAI NLVGNAIKFT GQGRVLVQLD APDPASQRLS
     LRVQDTGPGI PLADQARLFE PFSRVEGAAR RQEGSGLGLH LSRKLAQALG GDITLHSQPG
     EGSTFILDLP GAPPSEVES
//
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