ID A0A2N7WGF5_9BURK Unreviewed; 812 AA.
AC A0A2N7WGF5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C0Z19_01655 {ECO:0000313|EMBL:PMS28441.1};
OS Trinickia soli.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=380675 {ECO:0000313|EMBL:PMS28441.1, ECO:0000313|Proteomes:UP000235347};
RN [1] {ECO:0000313|EMBL:PMS28441.1, ECO:0000313|Proteomes:UP000235347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP25-8 {ECO:0000313|EMBL:PMS28441.1,
RC ECO:0000313|Proteomes:UP000235347};
RA Estrada-de los Santos P., Palmer M., Chavez-Ramirez B., Beukes C.,
RA Steenkamp E.T., Hirsch A.M., Manyaka P., Maluk M., Lafos M., Crook M.,
RA Gross E., Simon M.F., Bueno dos Reis Junior F., Poole P.S., Venter S.N.,
RA James E.K.;
RT "Whole genome analyses suggest that Burkholderia sensu lato contains two
RT further novel genera in the rhizoxinica-symbiotica group Mycetohabitans
RT gen. nov., and Trinickia gen. nov.: implications for the evolution of
RT diazotrophy and nodulation in the Burkholderiaceae.";
RL Submitted (JAN-2018) 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 -!- 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:PMS28441.1}.
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DR EMBL; PNYB01000001; PMS28441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N7WGF5; -.
DR Proteomes; UP000235347; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007890; CHASE2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR017181; Sig_transdc_His_kin_CHASE2.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF05226; CHASE2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PIRSF; PIRSF037347; STHK_CHASE2_PAS_prd; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01080; CHASE2; 1.
DR SMART; SM00387; HATPase_c; 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 PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:PMS28441.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000235347};
KW Transferase {ECO:0000313|EMBL:PMS28441.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 594..809
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 812 AA; 88977 MW; 428549E03826EE7F CRC64;
MTTEPTPGLP SPARGTWRPT LTVWQRFMWE WLVIGSLGVA IICACVFGQV AANFDRLVYD
RLLTLQSQPL SSDIEIVGID DDSVSELGRW PWPRTLQARL IDAVARAGAA AIVYDVLLTE
SSPADRDLAQ ALRAVPTYLP LFVDARAGDQ PILPVPPLAA AAAGTGHIDV VPDPDGIVRG
VSLRESAGGA SWPYIVMPLL ADIRSGKIAV ANGRYRGDPK QPASTADPAS DDVVEGARSR
VLVPFSGHLA SGQRISARRL LDGQAPTDAL RGKIVFVGLT ASGLLTHLAT PISGRWGPTS
DTLLHASALS ALLTGRAIRP AGPHWQFAAP LVSLALLLTG FLFLSPWRTL LLTCALGLLS
FALSAVLLDY ACVWMTPVPT LIALLVVYPL WGWRRLEMTM WRLQRELQRL ADDADLLPSI
PARPRDVRGD ALERHIALVE QAADRVQDMK RFVWDCLNSL PEPILIADRQ GLICVANKAA
HDYFARVGSV APEGRALTDA LGEMTFIKTI GPETGFDAEV QAHWPDVLDP TDLARVRAVK
RGIEVRDRTG RDYLLRYARC RNARGEASGF WVAGMVEVTA LHAAEQARED ALRLLSHDMR
SPHASVLALI EEEVATTRSE RVRTLLRHIE RYTRRALTLA DDFVQLTRAE SQAYVFEPVN
LVDIVLDASD EIWPQARAKR IRVETRFDGD GHWIRADRSL MTRAVTNLLN NAVKYSPEDT
VVHVSLTAAA TGRTDCRIAD QGYGMAEEAR AHLFERFRRF RVPGQPHTQG AGLGMALVKT
VVTRHDGEVK VESEPGRGTV VTVSVPRWDG AM
//
