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Database: UniProt
Entry: A0A1G8EBE2_9BURK
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ID   A0A1G8EBE2_9BURK        Unreviewed;       646 AA.
AC   A0A1G8EBE2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05444748_10240 {ECO:0000313|EMBL:SDH67206.1};
OS   Variovorax sp. OV700.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1882826 {ECO:0000313|EMBL:SDH67206.1, ECO:0000313|Proteomes:UP000199505};
RN   [1] {ECO:0000313|Proteomes:UP000199505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV700 {ECO:0000313|Proteomes:UP000199505};
RA   Varghese N., Submissions S.;
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};
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DR   EMBL; FNDR01000002; SDH67206.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8EBE2; -.
DR   STRING; 1882826.SAMN05444748_10240; -.
DR   Proteomes; UP000199505; 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; 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   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; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR017055; Sig_transdc_His_kinase_DctB.
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   PIRSF; PIRSF036431; STHK_DctB; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 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; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000313|EMBL:SDH67206.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:SDH67206.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        59..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        342..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          417..632
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   646 AA;  69488 MW;  E72A5659E572FC0C CRC64;
     MPEQTLGLAE TARDTRHRAA TDAAFAALCN NGFMISREPT RHFDLPSHTH RRWRSLPRWF
     GALSLVALAA FAGHHFALQN GLARLREAAD HRLDMLATGL DADLARFEYL PALLEMTPIV
     PALLRAPSDG ALRDAVNRYL DGVNAAAGAE MLYVLDAAGT SLAASDWDRA GTTVGQDLSF
     RPYVIDALGQ GKGRFYGVGI TSRKPGYYLS YALRRDQPVR GVVAVKVNLE ETERAWRMLP
     GNVALIDQRG VVILATREDL KFRPMLPLDA SQRAEVLRSR PYGEAGLQPL QWTLKEALAR
     DVQVVALDGV DQLASKRSLR GAPWQLMALD DLAPVRVGAR NAAITASLAM AVLLLLAVTL
     WQRRRAVRQK LANQAALQAA HDTLESTVTA RTAQLRAAQG EVVHAGKMAT LGQMSAGVVH
     ELNQPLTAMR TLSESAAILL DKSRFDDVRG NLQRIRGMVD RLARLTSQLK TFAHKGELPL
     APVPMAQALA DAQAIVAEAS KKNGVAIEVD VQPATVSVMA EEAALGSVLV NLMRNAIDAM
     QASPASRRTL RLEARPQDGR VILRVSDTGP GIPPDILPRL FEPFVTSKPA GTGLGLGLVI
     SAQLVRAMDG TLRAANLAEG GACFVADLPA AVQAILIPTP TGVINK
//
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