ID A0A1H7E966_9BURK Unreviewed; 729 AA.
AC A0A1H7E966;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-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=SAMN05518853_108159 {ECO:0000313|EMBL:SEK08632.1};
OS Variovorax sp. OK202.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1884311 {ECO:0000313|EMBL:SEK08632.1, ECO:0000313|Proteomes:UP000199192};
RN [1] {ECO:0000313|EMBL:SEK08632.1, ECO:0000313|Proteomes:UP000199192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK202 {ECO:0000313|EMBL:SEK08632.1,
RC ECO:0000313|Proteomes:UP000199192};
RA de Groot N.N.;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FNZJ01000008; SEK08632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7E966; -.
DR Proteomes; UP000199192; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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 CDD; cd12914; PDC1_DGC_like; 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; 3.
DR InterPro; IPR033479; dCache_1.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR017055; Sig_transdc_His_kinase_DctB.
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; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PIRSF; PIRSF036431; STHK_DctB; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 367..439
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 443..495
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 515..728
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 80530 MW; 496DD24805C817BE CRC64;
MPPLSPEPPV PSIATPPPPP RRRTRRAAAW LAALALALLL IGLAAQWAAT REANFQADSI
RRAMEVHVLG LRDSAGKYSY LPYTAGVHPA VLAALAHPED AAVKQRANLY IEEVNRQAGS
DALYLSDLQG LTLAASNWHT PQSFVGESYA NRPYFIDARA GRGGMFYGVG QTTGEPGLFI
SAPVRADGGA VLGVVTVKVS LRQLQEAWTF VRDPILLSDA RGVVFLSSVP SWLYQTRRAL
APGELERVRH DQQYGARTSF PALPWKVQRS DEQPGYLVAT DIGGKPRRFL AVDEPLPDLG
WTLTVMADHA EVTRARERTW MLGLLGAGVL LLGGLYWRLR ERRFAEQRDA RRDLELRVRE
RTHALDEAHA FRKAMEDSLL VGMRARDRQG RITYVNPAFC DMTGYGAGEL LGKLPPYPYW
HPDDVSQHWH HYDAMMSGQP ARSGFESRLR HRDGHEVITM VYTAPLIDAD GLHSGWMSSV
VDITEQKRAE LRQRQNDEQL QHAQRLASLG EMASTLAHEL NQPLMALSNF ASAAKAFAEQ
GNQQLLVDSL DETMAQAQRS AEIVRRIRGF VRQRTVGTED CAVSALVTNA LALLKGEMRQ
RQARAEVRVQ PGLPPVRGDR VLLEQVLLNL LSNSLQAMQA TPPEQRVVEV EAERLGARVH
IRVADRGAGI DDALAEQVFA PFFTTKPGGL GLGLNICRTI VEAHRGRLSF ADRPGGGTVF
TLELEIPSP
//
