ID   A0A1H6RJI9_9PSED        Unreviewed;       650 AA.
AC   A0A1H6RJI9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN03159495_0615 {ECO:0000313|EMBL:SEI51372.1};
OS   Pseudomonas sp. NFR16.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1566248 {ECO:0000313|EMBL:SEI51372.1, ECO:0000313|Proteomes:UP000199219};
RN   [1] {ECO:0000313|EMBL:SEI51372.1, ECO:0000313|Proteomes:UP000199219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NFR16 {ECO:0000313|EMBL:SEI51372.1,
RC   ECO:0000313|Proteomes:UP000199219};
RA   de Groot N.N.;
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; FNYJ01000001; SEI51372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6RJI9; -.
DR   STRING; 1566248.SAMN03159495_0615; -.
DR   OrthoDB; 6973808at2; -.
DR   Proteomes; UP000199219; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
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; 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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
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; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}.
FT   DOMAIN          6..123
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          289..509
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          529..644
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         55
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         579
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   650 AA;  71332 MW;  C1949CA449783DF7 CRC64;
     MKAETRLLIV DDNAATRYAL RRRMERQGFT VLEAGTGTEG LALIAARIPD ALILDVNLPD
     MSGFDIVRQL RTEPRTALLP VVHVSAASIQ TGDIVTGLEA GADAYLVHPV DPDVLLATLR
     TLLRVRDTEF ALRESEERFR EIFVNVSAPI AVMDGDFAVH ECNHAFAQLI SQGPEEHSLM
     QCFSEDQEAV LAGLREALVA GERWKGTLSM RVKGDVRETE WQVSPYRATG LSLVFIEDVT
     EHRRREQSHL RQLDSVNSQL AHEVAERART EEQLLQAQKM DAIGKLTGGI AHDFNNLLTG
     IVTGLELIKK RTEDARPEKV LTYADAALAS ARSASALTQR LLAFARQQPL DTQPTDINQH
     VRSLEDLLSR TIGKRIGLTL ELTSRSAIAM VDSGQLESAV LNLVINARDA LPEGGNIWIS
     TFEAYSQGHS RMEDGAYIAL TVRDDGVGIE HHLIDKVFDP FFTTKPIGEG TGLGLSTIYG
     FARQSGGDVN IRSVVGHGTE VTLMLPAAVE QSVPPQLAPV PAELGAGEHI LIVEDTASVR
     MFVNEVLTDA GYRCTQAADV NTALSIMEQD RSIDLLLTDV GMPQMNGREM ARLVRGWRPE
     LPVLFMTGYA ENALNRQHFL GEGMDMIIKP FQLVEFLCKV RAMLDGGAAH
//