ID A0A1H7N3I6_9BURK Unreviewed; 838 AA.
AC A0A1H7N3I6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05192542_105293 {ECO:0000313|EMBL:SEL17515.1};
OS Paraburkholderia caballeronis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=416943 {ECO:0000313|EMBL:SEL17515.1, ECO:0000313|Proteomes:UP000199120};
RN [1] {ECO:0000313|Proteomes:UP000199120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26416 {ECO:0000313|Proteomes:UP000199120};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOAJ01000005; SEL17515.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7N3I6; -.
DR STRING; 416943.SAMN05445871_1519; -.
DR OrthoDB; 1931120at2; -.
DR Proteomes; UP000199120; 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; 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:SEL17515.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000199120};
KW Transferase {ECO:0000313|EMBL:SEL17515.1};
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..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 93939 MW; 7577CDB8F79F7FB0 CRC64;
MLTERLFARS ARTPASPGAS SPSRWHHGPW WSNSYLLTPL LSILVFLIVM SLILWSLNRR
EQQQQEDTLY RNVAWAQQQI RLSMTGAQEQ LQALARDLAT GHGDPQSFQV SAGDIMQAHP
EILYLNWYTS VHQPRWPATA LPTLGQRLAK PTDAQMDEAV KAAFNEARTT RRQVYSPLIH
DDFGNGYITL QTPVYRDREF LGSIAAVFSV EGMLKHDIPP ELSAKYKISI LDVNNRELAT
TSTRPRLPRD VYYDLPLDPP GQGLSVRVYS YPQMTNFTNN TLVWLVAGLS CFVLWSLWSL
WKHTRQRFEA QQALYAEAFF RRAMENSVLI GMRVLDMHGR ITHVNPAFCR MTGWDESDLV
NKTAPFPYWP RDAYPEMQRQ LDMTLRGKAP SSGFELRVRR KDGSTFHARL YVSPLIDSSG
RQTGWMSSMT DITEPKRARE ELAAAHERFT TVLESLDAAV SVLAADEAEL LFANRYYRHL
FGIRPDGHLE LAGGGGFDSA QASSDSIDMV DAFAGLPAAA LTESAADAQE IYVESIQKWF
EVRRQYIQWV DGHLAQMQIA TDITTRKQAQ ELARQQDEKL QFTSRLMTMG EMASSLAHEL
NQPLAAINNY ASGTVALVKS GRASADNLLP VLEKTAQQAV RAGMIIKRIR EFVKRSEPKR
QATRVADIVA DAVGLAEIEA RKRRIRIVTD MRARMPVIYV DPVLIEQVLV NLLKNAAEAM
ADARPNAVDP VIRVVVQRDG GYVCISVVDQ GPGVDEATAE RLFEPFYSTK SDGMGMGLNI
CRSIIESHRG RLWVVNNVEA DGHISGATFH CNLPIGEADG QRPDRSDEPT PQTVTGEP
//
