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Database: UniProt
Entry: B2JJU9_PARP8
LinkDB: B2JJU9_PARP8
Original site: B2JJU9_PARP8 
ID   B2JJU9_PARP8            Unreviewed;       803 AA.
AC   B2JJU9;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE   Flags: Precursor;
GN   OrderedLocusNames=Bphy_0041 {ECO:0000313|EMBL:ACC69236.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC69236.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA   James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA   Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA   Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT   range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
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; CP001043; ACC69236.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2JJU9; -.
DR   STRING; 391038.Bphy_0041; -.
DR   KEGG; bph:Bphy_0041; -.
DR   eggNOG; COG5000; Bacteria.
DR   HOGENOM; CLU_019564_0_0_4; -.
DR   Proteomes; UP000001192; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 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; IPR003660; HAMP_dom.
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; IPR017232; NtrY.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   PIRSF; PIRSF037532; STHK_NtrY; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-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; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACC69236.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        45..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        82..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        306..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          331..383
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          541..769
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          773..803
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        782..803
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   803 AA;  86799 MW;  C6AEBC529E433BAF CRC64;
     MRRATSAGSL VVRLLVSTVA VTAVLLLVLL AAASANTEFF DRYYGWLYAA NVAVALIFML
     IVAVLVVIIV TRLRKGKFGT RLLAKLAFFF ALVGVVPGGI IYIVSYQFVS RSIESWFDVN
     VETALTSGLN LGRGMLDASL SDLQTKGRLM AEQLASADSA GTTLTLLRLR DQFGVQDATI
     VEPSRSISGA TPDMHVVAQA TSNYASLVPG DLPTSIMIEQ ARGRGFASIE GEVDGDPKAR
     GAKGALRLRI VQRIPDANAS QLQPTERFLQ LTQPVSQSLA RNADAVQRAY REYQEKAIGR
     TGLRKMYIGT LTLALFLATF IAMMLALALG NQLARPLFLL AQGTKEVTEG DYTPKREIKS
     RDELGFLTQS FNAMTRQLSE ARLAVEANRI ALEHSKSYLE SILANLTAGV FVFDRQFRLT
     TANRGAERIF RQPFVSLLGS PLDRIGVLSE FGPMVRKAFA DLEAAGGNDQ GDTGHWQQQM
     ALQVPGEADP LTLLARGARL VSAAGNDSDD EETSGYVVVF DDISDVISAQ RSIAWGEVAR
     RLAHEIKNPL TPIQLSAERL QMKLADKLMP SDAEVLKRGA TTIVNQVAAM KQMVDDFRDY
     ARTPPAVLAN LQLNELVSEV LTLYGIEEGK SAIVVEMADL PVIRGDATQL RQVIHNLLQN
     AQDAVADVQH PRVLLETRTV EYGDPDADGK VSVAVRLTVS DNGPGFPARI LTRAFEPYVT
     TKAKGTGLGL AMVKKIVDEH GARIDIRNRL KAGDVIEGAQ ISILFLQLAD DKAAAPGSGP
     QAAHDSSGTS QGKTKATVQT RAA
//
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