ID A0A1G6I2T3_9BURK Unreviewed; 837 AA.
AC A0A1G6I2T3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05421548_103236 {ECO:0000313|EMBL:SDC00784.1};
OS Paraburkholderia lycopersici.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=416944 {ECO:0000313|EMBL:SDC00784.1, ECO:0000313|Proteomes:UP000198908};
RN [1] {ECO:0000313|Proteomes:UP000198908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TNe-862 {ECO:0000313|Proteomes:UP000198908};
RA Varghese N., Submissions S.;
RL Submitted (SEP-2016) 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; FMYQ01000003; SDC00784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6I2T3; -.
DR STRING; 416944.SAMN05421548_103236; -.
DR OrthoDB; 1931120at2; -.
DR Proteomes; UP000198908; 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; PF00512; HisKA; 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; 2.
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 Kinase {ECO:0000313|EMBL:SDC00784.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:SDC00784.1};
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 595..817
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 93975 MW; C9E25149CAE72B9B CRC64;
MLTERLFARS ARPPGTPGES SPSRWHHGPW WSNSYLLTPL LSILVFLIVM SLILWSLNRR
EQQQQEDTLY RNVAWAQQQI RLSMTGAQEQ LQALARDVAA GHGDPQYFQT STTDIMQGHP
EMLYLNWYTS QQQPRWPNTA MPVFGQRLAK PNDAQMDEAV KAAFAEARST RRQVYSPLIY
DDLGNGYITL QTPVYRDREF LGSIAAVFSV EGILKHDIPP ELSAKYKISI LDANNRELAT
TSTRPRLPRD VYYDLPLDPP GQGVSVRVYS YPQMTNFTNN TLVWLVAGLS CFVLWSLWSL
WKHTRQRFEA QQALYAEAFF RRAMENSVLI GMRVLDMHGR ITHVNPAFCR MTGWDESDLV
GKNAPFPYWP RDAYPEMQRQ LDMTLRGKAP SSGFELRVRR KDGSQFHARL YVSPLIDSSG
RQTGWMSSMT DITEPKRARE ELAAAHERFT TVLESLDAAV SVLAADEAEL LFANRYYRHL
FGIRPDGHLE LAGGGGFDSA NASSDSIDMV DAFAGLPATA LTESTADAQE VYVESIQKWF
EVRRQYIQWV DGHLAQMQIA TDITTRKQAQ ELARQQDEKL QFTSRLMTMG EMASSLAHEL
NQPLAAINNY ASGTVALVKS GRAAPDNLLP VLEKTAQQAV RAGMIIKRIR EFVKRSEPKR
QATRVADIVA DAVGLAEIEA RKRRIRIVTD MRSRMPVIYV DPVLIEQVLV NLLKNAAEAM
AEARPNALDP VIRVIVKREG GNVCVSVVDQ GPGVDEATAE RLFEPFYSTK SDGMGMGLNI
CRSIIESHRG RLWVVNNVEA DGHISGATFH CSLPIGESDT PSRNSDEPTP QTVTGEP
//
