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Database: UniProt
Entry: A0A158IJ70_9BURK
LinkDB: A0A158IJ70_9BURK
Original site: A0A158IJ70_9BURK 
ID   A0A158IJ70_9BURK        Unreviewed;       600 AA.
AC   A0A158IJ70;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AWB69_06133 {ECO:0000313|EMBL:SAL56672.1};
OS   Caballeronia udeis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=1232866 {ECO:0000313|EMBL:SAL56672.1, ECO:0000313|Proteomes:UP000054683};
RN   [1] {ECO:0000313|EMBL:SAL56672.1, ECO:0000313|Proteomes:UP000054683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 27134 {ECO:0000313|EMBL:SAL56672.1};
RA   Oliw E.H.;
RL   Submitted (JAN-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; FCOK02000053; SAL56672.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158IJ70; -.
DR   Proteomes; UP000054683; 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; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
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   PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SAL56672.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        48..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          304..356
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          364..597
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..218
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   600 AA;  64650 MW;  56930DBE5D2156A7 CRC64;
     MHSETHGEPL GAQAVSPTAQ TPLGSSRNIW KALGTRSRAR AGKIRFGITW KMFLAVLIAC
     LTISLTMGYA LRLSFENGFL HYVRARDAGR LNAVMAKVTA EYAAHGSWNF LRQHPEEWVT
     LLDAAHDQAL RQEMVEAQTN KLPSWRTFPG SASVQQMLGP LSGKEEGPHW GMRLPAPAFA
     DSGVAASRDR GVGRDVTFDE SPYDRPPAPR PPPGRGGRGA PQPATLFDAN HDLVATTDSE
     PPPDVALKPV IYNGKIVGWV AANAPNTLSD AADIAFQAQQ ARATWEIAGV AVIVAALVAM
     LLARIVLAPV KRLMIATHRL AGGDYTTRVA AGRRDELDRL AGDFNVLADS LQRAERSRRD
     FIADISHELR TPLAVLRSEL EAIEDGVHAF DRHSLASLQN EVAMLNKLIE DLYELSLSDV
     GALSYRKVPA DIGQLVRASV DAMRESFRAK QIALSLTLPE ASGDGSANEL ANELAIESTG
     MVFQVDPARF VQLLKNLLLN SLRYTDPGGS VCVSVSVGPR GWQLDIQDSL PGVPAEALPH
     LFERLYRVDE SRSRQSGGAG LGLALCRAIV TAHGGTTVAR PSPLGGVWIT AHFEPEGVAA
//
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