ID A0A158B7J9_9BURK Unreviewed; 844 AA.
AC A0A158B7J9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AWB77_02521 {ECO:0000313|EMBL:SAK65880.1};
OS Caballeronia fortuita.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=1777138 {ECO:0000313|EMBL:SAK65880.1, ECO:0000313|Proteomes:UP000054903};
RN [1] {ECO:0000313|Proteomes:UP000054903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Oliw E.H.;
RL Submitted (JAN-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; FCNX02000005; SAK65880.1; -; Genomic_DNA.
DR RefSeq; WP_061134729.1; NZ_FCNX02000005.1.
DR AlphaFoldDB; A0A158B7J9; -.
DR STRING; 1777138.AWB77_02521; -.
DR OrthoDB; 1931120at2; -.
DR Proteomes; UP000054903; 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; 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 Kinase {ECO:0000313|EMBL:SAK65880.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:SAK65880.1};
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..818
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 821..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 94928 MW; 396649553FC816A1 CRC64;
MLTERLIKRS ARSARKPADA SPSRWHHGPW WSNSYLLTPL ISILVFLVVM SLILWSLNRR
EQQQQEDTLY RNVAWAQQQI RLSMTGAQEQ IQALARDIAT GHGDPQTFQT SSTDIMQGHP
EILYMNWYTS EHKPRWPNTP LPVLGSRLAK PNDTQMDEAV QAAFDEARTT RRQVYSPLLY
DDLGNGYITL QTPVFRDREF LGSIAAVFSI EGILKHDIPS ELSAKYKISI TDLNNRELAT
TSSRPRLPRD MFYDLPLDPP GQGLSVRVYS YPQLTNFTNN TLVWLVAGLS CFVLWSLWSL
WKHTRQRFEA QQALYAEAFF RRAMENSVLI GMRVLDMHGR ITHVNPAFCR MTGWDESDLV
GKNAPFPYWP RDAYPEMQRQ LDMTLRGKAP SSGFELRVRR KDGSFFHARL YVSPLIDSSG
RQTGWMSSMT DITEPKRARE ELAAAHERFT TVLESLDAAV SVLAADEAEL LFANRYYRHL
FGIRPDGHLE LAGAGFDGSQ SSSSDTIDMV DTYAGLPATA LTESSADAQE VYVEGIQKWF
EVRRQYIQWV DGHLAQMQIA TDITQRKQAQ ELAHQQEEKL QFTSRLMTMG EMASSLAHEL
NQPLAAINNY CSGCVALVKS GRMTQETLLP VLEKTAQQAV RAGMIIKRIR EFVKRSEPKR
QATRVADIVA DAVGLAEIEA RKRKIRIITE IRSRMPVIYV DPVLIEQVLV NLLKNAAEAM
HDAKPNAVDP VIRVVVQRMD GGFVCISVVD QGPGVDEATA ERLFEPFYST KSDGMGMGLN
ICRSIIESHR GRLWVVNNVE ADGHVTGATF HCSLPIGAVD GSGGPGGTDA QDEHTRQQTV
TGEL
//
