ID A0A3S2TRB6_9BURK Unreviewed; 1055 AA.
AC A0A3S2TRB6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ENE75_06395 {ECO:0000313|EMBL:RVT52093.1};
OS Rubrivivax albus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Rubrivivax.
OX NCBI_TaxID=2499835 {ECO:0000313|EMBL:RVT52093.1, ECO:0000313|Proteomes:UP000288178};
RN [1] {ECO:0000313|EMBL:RVT52093.1, ECO:0000313|Proteomes:UP000288178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICH-3 {ECO:0000313|EMBL:RVT52093.1,
RC ECO:0000313|Proteomes:UP000288178};
RA Chen W.-M.;
RL Submitted (JAN-2019) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RVT52093.1}.
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DR EMBL; SACT01000002; RVT52093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S2TRB6; -.
DR Proteomes; UP000288178; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; 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; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 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; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR007895; MASE1.
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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF05231; MASE1; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-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; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000288178};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 125..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 330..424
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 541..611
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 615..667
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 684..907
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 929..1046
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 906..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 979
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1055 AA; 112688 MW; 106DEE607D0AF26B CRC64;
MVRRPAAPLT VVLLTALVYG IVGAAAVQLA VHPGHAVAVY PSAGIALAVA LVYGWPALLG
AALGAAAVNV GLMVWHGQPG ATELAAGAAI GAGAAAQAAF GRALVRRWVS QPLVLAEFAD
VVRFYLLGGP AACLVSASVA HAALVAAGQM PLQGVSVSWW TWWLGDVLGV LLAAPVVLAL
VGQPREEWAP RRLTLVVPML LTTAMLAGAI GWAAHAHGER VRTAFERDAW SLADALDAQL
RRPLDVLQAM HGLFDTQQHI DPVEMQRATA PWLRDQPFIA AIGYSARVDP ADVADFEARA
RAEGPVADYR VFAREDAQTL PPSRHGVVAI RLIEPLATNR PALGVDAMTI RAARAAIQRA
AATGQPAATA GFRLTQATGD ETGIVIYRAL YQGDPRTDAE RRAAFTGVVF VTLRLETLVA
DMQRQVPMHL AWCLVDLDPG AERPRLAGAP GCEARPRATL RYLRNLTLGP RALQWQVAAE
PSQLPGVSEA GTTLFATTGL ITAGLLGALL LTVSGRQRRI ELAVTERTAD LRAASLALQE
SQDRLRNIVD HVPIGIIYAD ASGRLREANP DLLAMLGRVV LPAPPPALPD WVHVDDRAEV
EAFLQQVRTG EQPPARMQVR LVAADGSERT VRLGLSPLRG PDGQLQRLVG VVEDIGEHLQ
LEASERARRA AEASSQAKSE FVGRMSHELR TPLNAMLGFS QLLSRDNSAP LAAHQRRWID
QVQDAGWHLL NMINDTLDLS MIESGALRLT PVALDPRALL EATLSMIAAA ADRRALQVVP
ADIAPGVPPV LGDETRVKQI LTNLLSNAVK YNVDGGRIAV QVDVDPDTVP EQVVFRVSDT
GIGLSAEQID RLFHPFDRLG RESSGVEGTG IGLVISRRLV ECMGGSLTAS GQVGRGSMFE
LRLPRAATGP DVTPGKASPA SDGRYRQRRV HYVEDNETNV ALMRGMLAQR PQIALSVSTM
GLDALAAVRI ERPDLLLLDM HLPDIDGLDL LTHLKADDGT AGIPVIVLSA DATPERVARA
LHAGAEAYLS KPLNLTELLQ HVDALLEQGN TEWGE
//