ID B9BN20_9BURK Unreviewed; 794 AA.
AC B9BN20;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BURMUCGD2_2247 {ECO:0000313|EMBL:EEE08030.1};
OS Burkholderia multivorans CGD2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=513052 {ECO:0000313|EMBL:EEE08030.1, ECO:0000313|Proteomes:UP000004535};
RN [1] {ECO:0000313|EMBL:EEE08030.1, ECO:0000313|Proteomes:UP000004535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGD2 {ECO:0000313|EMBL:EEE08030.1,
RC ECO:0000313|Proteomes:UP000004535};
RX PubMed=23105085; DOI=10.1128/JB.01306-12;
RA Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., Radune D.,
RA Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., Greenberg D.E.,
RA Holland S.M., Goldberg J.B.;
RT "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic
RT Granulomatous Disease Burkholderia multivorans Isolates.";
RL J. Bacteriol. 194:6356-6357(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:EEE08030.1}.
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DR EMBL; ACFC01000003; EEE08030.1; -; Genomic_DNA.
DR RefSeq; WP_006404982.1; NZ_ACFC01000003.1.
DR AlphaFoldDB; B9BN20; -.
DR Proteomes; UP000004535; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
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; 1.
DR InterPro; IPR007890; CHASE2.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR017181; Sig_transdc_His_kin_CHASE2.
DR PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF05226; CHASE2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PIRSF; PIRSF037347; STHK_CHASE2_PAS_prd; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01080; CHASE2; 1.
DR SMART; SM00387; HATPase_c; 1.
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); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 574..790
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 794 AA; 86757 MW; 4AA7FE35759C7369 CRC64;
MKADSVSPRR QLGRRFLLEW IAIGCLGIAV ICACALGRAS SSVDGLIYDR LLMLRSLPLS
PDVVVVDIDN RSVSALGRWP WSRNVHARLL DTLARAQPAA VVYDVLFTEP SPDDRAFADA
MARVPTFLPV LLSPEQDGKR ALDPPVAALA ARAMGLGHIN LEVDPDGIVR SVALFEDDGR
TRWPQLMVPV YRAIAAGKLH PAGGAPGPRA HDLSRDATGE GRYLIPFSRN TPAYPTLSFD
DVLEGRVKPD ALRGKIVVVG VTASGLYDRF ATPVSGDFGP LAGVYIHASV LDMLTTGSAI
SPVSRPALFA ASLLPLAALL GGFLMLSPWR ALLLTLSLAA LAVIASIALL FEARVWLSPA
PAVFGLIAVY PIWNWRRLEM TMSYLRRELQ RLADEPHLLP EAPRARRVGG DVLERQMALM
AQAAQRLQDM KRFVWDSLDS MPEPIFVTDR AGTVLIANHA AKRYGSRLAL PLPEGRPLRA
ALGELTFVKT VDGNAEHDVA IRDSWPAALD PTLAAEHDVM ARGIEVRDRD GLDHLLRYAA
CTNAQGHVTG WIAGLVDVTE LHAAERQREE ALHLLSHDMR SPQSSILALV EIERDRVESD
TMRALLARIE RYAHRALSLA DEFVQLARAE SQAYQLETTS LVDVLIDASD EVWPQAQAKR
IRIDTDVGTE MCWVRADRSL ITRAFVNVLN NAVKYSPSDT TITCTLTVEH ASKRMFCTIR
DQGYGIAPED QRHLFERFKR FHAGERPEIS GSGLGMAFVK TVVTRHGGSV SVDSEVGVGT
AVTVSLPAID EPSA
//
