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Database: UniProt
Entry: A0A108CSD6_9BURK
LinkDB: A0A108CSD6_9BURK
Original site: A0A108CSD6_9BURK 
ID   A0A108CSD6_9BURK        Unreviewed;       767 AA.
AC   A0A108CSD6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=WM16_08635 {ECO:0000313|EMBL:KWK79684.1};
OS   Burkholderia ubonensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=101571 {ECO:0000313|EMBL:KWK79684.1, ECO:0000313|Proteomes:UP000065504};
RN   [1] {ECO:0000313|EMBL:KWK79684.1, ECO:0000313|Proteomes:UP000065504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSMB782WGS {ECO:0000313|EMBL:KWK79684.1,
RC   ECO:0000313|Proteomes:UP000065504};
RA   Sahl J., Keim P., Wagner D.;
RT   "Expanding the genomic diversity of Burkholderia species for the
RT   development of highly accurate diagnostics.";
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   -!- 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:KWK79684.1}.
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DR   EMBL; LPLU01000048; KWK79684.1; -; Genomic_DNA.
DR   RefSeq; WP_060234096.1; NZ_LPLU01000048.1.
DR   AlphaFoldDB; A0A108CSD6; -.
DR   Proteomes; UP000065504; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 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; 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; IPR038318; KdpD_sf.
DR   InterPro; IPR025201; KdpD_TM.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
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; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF13493; DUF4118; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 2.
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); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000313|EMBL:KWK79684.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:KWK79684.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        42..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        87..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          122..195
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          247..292
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          401..618
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          644..762
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          365..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         693
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   767 AA;  82333 MW;  B1C0750616B87B25 CRC64;
     MIRIERGRIK HCATAVVMVA IATVLQALAI RYGGVNLPLL LYYPMLACAA WMTSFGAGLL
     ATAISAALAW MLFLSDPAAY TGSLAERLVR LGTFMLVGAL ACAIASALRR MGDAQRHRES
     AERRHDETVL ASLPQGVIAT DPGGRLTFIN ATAAELAGCR PDDALGRRAQ DVLRVCDAQG
     RRVQATPLER VLDGAAGAMC DRHWLAGSVD LVPIVEIAAP MHDADGNVDG AVMLLRDARM
     ERIRADASRT LRAVVDASPD ALVGVDAARR IVSWNPAAQR MFGYDTHEAL GRDVAILVAA
     RWWRRHPLAD GSRRRRDDLV PTDCLCVRRD GSRFRATVRA SPVRGGGRDD SRERVALSLT
     LRASDEQRRR DRRTQRSLRG ARDARQQADT SNRLKDELLA TVSHELRTPL NVIYGWVEVL
     RHSGDQALQQ QAIDAIDRSA RSLTRMVGDI LDASSLATGK LRIDAMPVDL VRIAAEVAGA
     FRSAAAAQGV ALDTDCALDT CVVSGDGERL RQMLSNLLSN ALKFTPRGGR VTIRLARKDA
     HAELSVADTG QGIAPEFVPH VFDAFRRADD SPASSRRGLG LGLSIVRHIA ELHGGTVTVD
     SAGRHRGATF TVTLPTGWQP VGPMAWGAVE PAGNGEATML DAQRVLLVDD DATTRVSLAA
     ALRTLGAAVD VASSGREAFA KAAGMRPTVV LSDLAMPDGD GYWLLDALRR DVARGLAGVR
     VLAVTAHVGQ ADERRVLAAG FDGYLRKPVD VRQLARAIAR ATGGRRA
//
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