ID G4MGA2_9BURK Unreviewed; 843 AA.
AC G4MGA2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BKIR_c64_0433 {ECO:0000313|EMBL:CCD40181.1};
OS Candidatus Paraburkholderia kirkii UZHbot1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1055526 {ECO:0000313|EMBL:CCD40181.1, ECO:0000313|Proteomes:UP000003511};
RN [1] {ECO:0000313|EMBL:CCD40181.1, ECO:0000313|Proteomes:UP000003511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UZHbot1 {ECO:0000313|EMBL:CCD40181.1,
RC ECO:0000313|Proteomes:UP000003511};
RA Carlier A.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCD40181.1, ECO:0000313|Proteomes:UP000003511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UZHbot1 {ECO:0000313|EMBL:CCD40181.1,
RC ECO:0000313|Proteomes:UP000003511};
RA Carlier A.L., Eberl L.;
RT "Draft genome sequence of Candidatus Burkholderia kirkii.";
RL Submitted (OCT-2011) 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};
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:CCD40181.1}.
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DR EMBL; CAFE01000239; CCD40181.1; -; Genomic_DNA.
DR AlphaFoldDB; G4MGA2; -.
DR STRING; 1055526.BKIR_c64_0433; -.
DR HOGENOM; CLU_011685_0_0_4; -.
DR BioCyc; CBUR1055526:G10QW-1818-MONOMER; -.
DR Proteomes; UP000003511; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; 2.
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; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13188; PAS_8; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000003511};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 316..388
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 392..444
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 596..819
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 824..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 95212 MW; 90E4AB03FBEF75D1 CRC64;
MLTERLIKRS ARVVRKPTDS SPTRWHHGPW WSNSYLLTPL ISILVFLVVM SLILWSLDRR
EQQQQEDTLY RNVAWAQQQI RLSMTGAQEQ IQALARDIAT GHGDPQTFQT SSTDIMQGHP
EILYMNWYTS EHKPRWPNTP LPVLGARLAK PNETQMGEAV QAAFDEARTT RRQVYSPLFY
DDLGNGYITL QTPVFRDREF LGSIAAVFSI EGILKHDIPS ELSAKYKISI TDLNNRELAT
TSSRPRLPRD MFYDLPLDPP GQGLSVRVYS YPQLTNFTNK TLVWLVAGLS CFVLWSLWSL
WKHTRQRFEA QQALYAEAFF RRAMENSVLI GMRVLDMHGR ITHVNPAFCR MTRWDESDLV
GKNAPFPYWP RDAYPEMQRQ LDMTLRGKAP SSGFELRVRR KDGSFFHARL YVSPLIDSSG
RQTGWMSSMT DITEPKRARE ELAAAHERFT TVLESLDAAV SVLAADEAEL LFANRYYRHL
FGIRPDGHLE LAGAGFDSGP QSSSSDTIDM VDTYAGLPAT ALTESSADAQ EVYVEGIQKW
FEVRRQYIQW VDGHLAQMQI ATDITQRKQA QELAHQQEEK LQFTSRLMTM GEMASSLAHE
LNQPLAALNN YCSGYVALVK SGRMTQETLL PVLEKTAQQA MRAGMIIKRI REFVKRSEPK
RQATRVADIV ADAVGLAEIE ARKRKIRIVT EIRSRMPVIY VDPVLIEQVL VNLLKNGAEA
MHDAKPHAVD PVIRVVVQRM DGGFVCISVV DQGPGVDEAT AERLFEPFYS TKSDGMGMGL
NICRSIIESH RGRLWVVNNV EADGHVTGAT FHCSLPIGAV DGSGTNGDAH DEHTRQQTVT
GEL
//
