ID A0A0Q7CXK0_9BURK Unreviewed; 1052 AA.
AC A0A0Q7CXK0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASC67_04025 {ECO:0000313|EMBL:KQW69669.1};
OS Methylibium sp. Root1272.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=1736441 {ECO:0000313|EMBL:KQW69669.1, ECO:0000313|Proteomes:UP000053968};
RN [1] {ECO:0000313|EMBL:KQW69669.1, ECO:0000313|Proteomes:UP000053968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1272 {ECO:0000313|EMBL:KQW69669.1,
RC ECO:0000313|Proteomes:UP000053968};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW69669.1, ECO:0000313|Proteomes:UP000053968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1272 {ECO:0000313|EMBL:KQW69669.1,
RC ECO:0000313|Proteomes:UP000053968};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQW69669.1}.
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DR EMBL; LMDY01000012; KQW69669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q7CXK0; -.
DR STRING; 1736441.ASC67_04025; -.
DR Proteomes; UP000053968; 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 CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
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; IPR013655; PAS_fold_3.
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; PF08447; PAS_3; 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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..403
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 537..607
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 611..663
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 680..904
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 927..1044
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 977
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1052 AA; 114646 MW; A3D415B343339B4A CRC64;
MLVALTYVLT GAASLQLAIP PGYASPLFPP AGIALAAALV YGWRVLPAVT LGSLSVQMLV
YFNGDQQHVF RDALTGLAIA CGATMQTALG AWLVRRSLKE PLTLDGPASI LRLFGFGALA
ACTVGASLSV LALWLAGLLP TALLFDTWWT WWGGDALGVM IATPVVLTLI GRPRTAWRPR
RNTVALPLVI ATLLLALAIS QVARWDGQRD SARFERDAIS VSRTVELRLN AHLDALDAMH
SIYVASTNVD SREFERASAG WLRKLPSVQA IGWHERVARQ DLPAFEASLR SLGQPDYRVF
ERDAALSAND AELMVMRYIE PRAGNDTALG VNALSIRAAR EAIARARLSD GATVTPGFRL
TQETAQQTGV VVYRAVYRGD EPSRSLQGMV FLTLRMEDAL ARLVAGAPRY LQVCLLDADA
PPESRLLAGP PDCARAAANP LWSHNATVPF AGRAWELRVQ APNGVPNGPA AGPLSGESAT
AWLFSLTGLL GTGMMGALLL LVTGRTRQTE TAVAERTEQL EHEITERLAT EQALRESEQR
FRSIFNSVPI GVVYTDLQGR IKQPNAAYCT MTGYSEEELL SLSLASLTHP EDRAADLAIQ
QDLVDGRLPL YRRRKRYITK NGPVLWVSAT VSLLRDEHGQ PHRLVGLVED ISEHLRLEEA
EHARESAETA NRAKNEFLSR MSHELRTPLN AMLGFAQLLD LDRGEPLHER HRMWVTQIQQ
AGWHLLEMIN DVLDLSRIES GTLSLQVESL SLEPLIAASM ALVEPQARGR GLTLVRTMAE
HAPLQVLGDA TRVKQILTNL LSNAVKYNRE AGEVRVSTRR TEESDGTPML ELDVCDTGLG
IEPQLLTQLF QPFNRLGRER GATEGTGIGL VIAKLLAERQ GGSLKVRSEP GIGSTFTLRL
PLDSEARPMT ANQDADEEAN AAYNRRHVLY IEDNDTNVEV MRGIFGLRPQ VRLAVATTGL
DGLASVRTSA PDLILLDMHL PDIDGMVLLQ HLKSDEQTAE IPVIAVSADA LPAQISAALQ
AGAIRYLTKP VAIDEVLGVL DELLSQLTTR FG
//
