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Database: UniProt
Entry: A0A158FJF3_9BURK
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ID   A0A158FJF3_9BURK        Unreviewed;       832 AA.
AC   A0A158FJF3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AWB64_01390 {ECO:0000313|EMBL:SAL20008.1};
OS   Caballeronia sordidicola.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=196367 {ECO:0000313|EMBL:SAL20008.1, ECO:0000313|Proteomes:UP000054893};
RN   [1] {ECO:0000313|EMBL:SAL20008.1, ECO:0000313|Proteomes:UP000054893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 22029 {ECO:0000313|EMBL:SAL20008.1};
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; FCOC02000003; SAL20008.1; -; Genomic_DNA.
DR   RefSeq; WP_060817886.1; NZ_FCOC02000003.1.
DR   AlphaFoldDB; A0A158FJF3; -.
DR   OrthoDB; 5389366at2; -.
DR   Proteomes; UP000054893; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   CDD; cd18161; REC_hyHK_blue-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 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; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
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; SSF55781; GAF domain-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; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SAL20008.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          256..308
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          327..397
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          465..690
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          713..828
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         763
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   832 AA;  92082 MW;  472C962EA6D03CCB CRC64;
     MQKPPLFSTL SQLEFERAVL GRVVAGMPLH EVLEHVIHRV ENRSEQPMRA SVLLVDATGK
     RLIHGAAPSL PEEYNRIVDG LETGPLMGSC GAAAFRGEPV IVEDIETDPV WAAFRDIARK
     FELRACWSMP ICAADGRVLG TFANYYSVPK KPSAEELDDI AQVASVTALA IERHASDRAL
     RESEERLRIA QRAGGIGTFE LFPDTGRMAV SEELCRQWGL TPRHETHLDV LLELVHPDDR
     ARVLAAHRTM PTGALDYLEY RIHRADSGEE RWMARREEAV AHNNAGLRFI GVTYDITDHK
     RFEERLRVSE TQLRRLNDSL AAEVDARTRE RNSIWRNSRD LFIVASSAGV LRAVNPAWTD
     ILGFREDELI GRSFAEIVHP DDVQATDAAL QSVAHTGRVR FENRNRHKDG SYRWVSWVAA
     FEGDTLYGNG RDVTSEKETR RALQQTEEAL RQAQKMEALG QLTGGIAHDF NNLLQGITGP
     LELIRRYTQL GRTDDIDRFI TMATGAANRA ASLTHRLLAF SRRQPLDPKP VNADELLHSI
     DDLLKRTMGE AIDTRVIHNP HLWLTRCDAN QLENALLNFA INARDAMPEG GRLTLETDNV
     ELGREFAASH PDVTPGQYVV VSASDTGVGM PDDVKARAFD PFYTTKPLGQ GTGLGLSMAY
     GFAKQSGGIA TIESAPDAGT TIRLYLPRFT GGAGKQESAT ALTEAHRAAD GHVILVVEDD
     TSVRELVCEI LRDLDYEVLE AIDGPSGLAI LNSRARIDLL VTDVGLPGLN GRQLADAARA
     TRPALRVLFM TGYAESATRA NGFLDTGMEM ITKPFTLESM ASRIRRMVTM AR
//
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