ID A0A1G6H170_9BURK Unreviewed; 810 AA.
AC A0A1G6H170;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05421548_101563 {ECO:0000313|EMBL:SDB88057.1};
OS Paraburkholderia lycopersici.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=416944 {ECO:0000313|EMBL:SDB88057.1, 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; FMYQ01000001; SDB88057.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6H170; -.
DR STRING; 416944.SAMN05421548_101563; -.
DR OrthoDB; 9815750at2; -.
DR Proteomes; UP000198908; 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; 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:SDB88057.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 49..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 335..387
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 545..773
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 780..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 810 AA; 87671 MW; 05354691895B45FD CRC64;
MLDKVRRATS FSSVVVKLLV STVAFTATLL LVLLAAASAN TEFFDRYYGW LYAANIVVAL
IFMSVVTALV IVIAVRLRRG KFGTRLLAKL AFFFALVGVV PGGIIYIVSY QFVSRSIESW
FDVNVETALT AGLNLGRGML DASLSDLQTK ARLMAEQIAS GDAAGTTLTL LRARDQFGVQ
DAMIVEPVRS MSGAAPDMHV VAQASSNFSS LMPGDMPTAL MLDQARGRGF AAIEGEVDGD
PHLHGPKGAL RLRVVTRIPD ANTTDLQPAE RFLQLEQPVP AALARNADAV QRAYREYQEK
ALGRTGLRKM YIGTLTLALF LATFVAMMLA LALGNQLARP LFLLAQGTKE VTEGDYTPKR
EIKSRDELGF LTQSFNAMTR QLSEARQAVE KNRIALEHSK AYLESILANL TAGVFVFDRQ
FRLTTANPGA ERIFRQPFQT QLGVSLDHIG ALTEFGAMVR KAFADQEASR GDGDHDRGHW
QQQFSVPMPG ETEPLTLLVR GARLVSDTGR DAGDMQTSGY VVVFDDISDV ISAQRSVAWG
EVARRLAHEI KNPLTPIQLS AERLQMKLTD KLAPSDAEVL KRGATTIVNQ VAAMKQMVDD
FRDYARTPPA VLASLQLNDL VSEVLTLYGA EEGKSAIKVE LSDLPVIRGD ATQLRQVIHN
LLQNAQDAVA DTENPRVTLE TRAVEYGDPD AQGRTRVAVR LTVSDNGPGF PARILTRAFE
PYVTTKAKGT GLGLAMVKKI VDEHGARIDI RNRLRAGDVI EGAQISILFL QLAGDATPDA
AAPGAGTSGD GHARAAAGRG SKATVQTRAA
//
