ID B1Z0X0_BURA4 Unreviewed; 769 AA.
AC B1Z0X0;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-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};
GN OrderedLocusNames=BamMC406_3683 {ECO:0000313|EMBL:ACB66150.1};
OS Burkholderia ambifaria (strain MC40-6).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=398577 {ECO:0000313|EMBL:ACB66150.1, ECO:0000313|Proteomes:UP000001680};
RN [1] {ECO:0000313|Proteomes:UP000001680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC40-6 {ECO:0000313|Proteomes:UP000001680};
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia ambifaria MC40-6.";
RL Submitted (APR-2008) 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; CP001026; ACB66150.1; -; Genomic_DNA.
DR RefSeq; WP_012365553.1; NC_010552.1.
DR AlphaFoldDB; B1Z0X0; -.
DR KEGG; bac:BamMC406_3683; -.
DR HOGENOM; CLU_000650_2_1_4; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000001680; Chromosome 2.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR CDD; cd00088; HPT; 1.
DR CDD; cd19924; REC_CheV-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ACB66150.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:ACB66150.1}.
FT DOMAIN 5..109
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 255..487
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 489..623
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 647..763
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 52
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 696
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 769 AA; 83265 MW; 91E73B95F3FA87BB CRC64;
MSGDDDLSHL SLLELYREET RTQTQALSER LLALESGEPD SVALEACMRA AHSLKGAARI
VGVPLGVEIA GRMEECFVAA QAGTIALTAT HVDVLLAGVD LLVRVADPQA PPVSSTEIDA
FALALTGADG THAMPSPAFA PPPAPPSSVP FRDHDGAANE PVGAGAAVPP LALSAAVPDP
VPAGRAAGAG AMRRVRADTL NRLLSLSGES LVESRWLKPF AESMLRVKRA QRDAARSLDL
LYERFADELD AGVLASVNEV RHMLNDVQRS LAERMEEFDR FERRSTHIAE QLYDEALQCR
MRPFGDATRA YPRIVRDLAR SLGKQVRFSI VGEGTQVDRD ILDLLDAPLG HLLRNAIDHG
VDSPDARRAR GKPAEASVTL EARHSAGSLL VSVIDDGPGV DMDALRAAVV RQRLTDDETA
ARLSDPELLE FLLLPGFSMR DAVTDVSGRG VGLDAVQEMV RGVRGAVRIF NEPGAGMRFV
LQLPLTLSVI RSLLVEVGGE PYAFPLAHVR RTLELSHDDI DVLEGQPHFP FDGRRAGLVG
AHQLLDAGEP AVTRTSTAVV VVGGEPELYG VAVDRFLGER MLVVQPLDSR LQKIQNIAAG
ALLENGDPVL IVDVEDLIRS VDKLVRGGQL AKLTRDPQHA RADRRRRVLV VDDSLTVREL
ERKLLEKRGY DVTVAVDGMD GWNAVRSDAF DLVVTDVDMP RMDGIELVTL IRSDPALKRV
PVMIVSYKDR DEDRRRGLDA GADYYLAKSS FHDEALLDAV HDLIGGARG
//
