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Database: UniProt
Entry: A0A2A2DMC3_9PSED
LinkDB: A0A2A2DMC3_9PSED
Original site: A0A2A2DMC3_9PSED 
ID   A0A2A2DMC3_9PSED        Unreviewed;       407 AA.
AC   A0A2A2DMC3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BZL43_23070 {ECO:0000313|EMBL:PAU53362.1};
OS   Pseudomonas sp. PICF141.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1949067 {ECO:0000313|EMBL:PAU53362.1, ECO:0000313|Proteomes:UP000217819};
RN   [1] {ECO:0000313|EMBL:PAU53362.1, ECO:0000313|Proteomes:UP000217819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PICF141 {ECO:0000313|EMBL:PAU53362.1,
RC   ECO:0000313|Proteomes:UP000217819};
RA   Gomez-Lama C., Legarda-Cristobal G., Trivino J.C., Mercado-Blanco J.;
RT   "Genome sequences of Pseudomonas strains PIC25, PIC105 and PICF141
RT   indigenous of the olive (Olea europaea L.) cv. Picual rhizosphere and
RT   effective biological control agents against Verticillium dahliae.";
RL   Submitted (JAN-2017) 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:PAU53362.1}.
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DR   EMBL; MUNM01000078; PAU53362.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2DMC3; -.
DR   OrthoDB; 9776727at2; -.
DR   Proteomes; UP000217819; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
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; 1.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065:SF29; SENSOR PROTEIN KINASE FLES; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 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; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:PAU53362.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:PAU53362.1}.
FT   DOMAIN          77..114
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          192..397
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   407 AA;  44534 MW;  2BBD09F868A4366D CRC64;
     MPQAVQMSPA LDASGQPSSV EQASRLGLEQ AFALFSQMSS QLTDSYSMLE ARVTELKGEL
     AVVSAQRMQE LSEKERLANR LQNLLDLLPG GVIVIDAQGI VREANPAASE LLGLPLEGEL
     WRHVIARCFA PREDDGHEIS LKDGRRLSIA TRSLDAEPGQ LVLLNDLTET RHLQDQLARH
     ERLSSLGRMV ASLAHQIRTP LSAALLYASH LTEQALPVET QQRFAGRLKE RLHELEHQVR
     DMLVFARGEL PLTDRVSPRM LMQALQAAAL THVQDLPIRW QCDSHAGELL CNRDTLVGAI
     LNLIENAIQA SAGGVRLKVH LYTRGNNLRL CVSDRGSGID TKVLARLGEP FFTTKTTGTG
     LGLTVVKAVV RAHQGELQLR SRPGRGTCAQ VILPIFSGDQ PDAQGAK
//
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