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Database: UniProt
Entry: A0A1H7VN86_9BURK
LinkDB: A0A1H7VN86_9BURK
Original site: A0A1H7VN86_9BURK 
ID   A0A1H7VN86_9BURK        Unreviewed;       799 AA.
AC   A0A1H7VN86;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SAMN05192542_12623 {ECO:0000313|EMBL:SEM10349.1};
OS   Paraburkholderia caballeronis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=416943 {ECO:0000313|EMBL:SEM10349.1, ECO:0000313|Proteomes:UP000199120};
RN   [1] {ECO:0000313|Proteomes:UP000199120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 26416 {ECO:0000313|Proteomes:UP000199120};
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; FOAJ01000026; SEM10349.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7VN86; -.
DR   STRING; 416943.SAMN05445871_4335; -.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000199120; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR024478; HlyB_4HB_MCP.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   PANTHER; PTHR43395:SF10; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF12729; 4HB_MCP_1; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50113; PAC; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00110}; Reference proteome {ECO:0000313|Proteomes:UP000199120};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          207..260
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          351..403
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          414..521
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   MOD_RES         459
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   799 AA;  87134 MW;  F6DD54BECBE514DB CRC64;
     MTIRHRITLL VVLMFVALMS IGGYAVYQTR RSATEVRSVT QGVVPSALAS ADLVSQLKDV
     QLATMTLVYA PDVNMVSQAQ DELKAKQKTL SDALDVQGSA AASHAQVGLV AQARESLANY
     FSAIADTAKM KAEGKNEMAQ AFLFANVAQY RDELEGIVTT LRVEKNRQKD DAIKSLNDML
     STTTSAIAGV TGGAVLLLTV IGLLLYRQIT QPLTRMQSMM SEIASNQDFT RRVPVGRMDE
     IGHSIVAFNG MIEKIQQSSA QLKRKTADIQ AMLQNMQQGI LTIVDGAQIH AEYSAYLEAI
     FETNEIAGQP VMDLVFSHTD LDANALSQVD AAIYACLGED SINFAFNQHL LVNEITRTMP
     DGRKKILDLS WSAITDETDT VVRLMLCVRD VTELRELAAE AGEQKRQLEM IGEILSVSEE
     KFHHFVESST SFIQQNERII SQDACPDSAA IAELFRNMHT IKGNARTYRF QHLTGVAHEA
     EQRYDALRRG EPLDDGGWDP QALIDDLARV KEALTHYATI NEVSLGRKSA SQAGLDTSRF
     VPVEREAIDA SLRQIEHADV SDLKSMQAMR EAVRHTLRLF GTERVDDMLS GVLDSLPSLA
     KELGKAEPVV RIDDHGYRLR SEAGPTLTNV FVHLLRNSID HGIEKPDERA VVAKPSAGTI
     LLDVNVASGD GTLQITLGDD GRGLALARIR GIAVERGWID ADAEIADEEV AEFIFRSGFS
     TASAVTDVSG RGVGMDAVRD FLTREGGRIA LHFVDGKRGA AYRRFETIVT LPGRWAVGTA
     GLAPAPVRAA GASQAETLA
//
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