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Database: UniProt
Entry: A0A1H2X9R7_9PSED
LinkDB: A0A1H2X9R7_9PSED
Original site: A0A1H2X9R7_9PSED 
ID   A0A1H2X9R7_9PSED        Unreviewed;       760 AA.
AC   A0A1H2X9R7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05216287_1825 {ECO:0000313|EMBL:SDW89498.1};
OS   Pseudomonas kuykendallii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1007099 {ECO:0000313|EMBL:SDW89498.1, ECO:0000313|Proteomes:UP000243778};
RN   [1] {ECO:0000313|Proteomes:UP000243778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-59562 {ECO:0000313|Proteomes:UP000243778};
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; FNNU01000002; SDW89498.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2X9R7; -.
DR   STRING; 1007099.SAMN05216287_1825; -.
DR   OrthoDB; 9177042at2; -.
DR   Proteomes; UP000243778; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd18774; PDC2_HK_sensor; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43065:SF49; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
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   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDW89498.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000243778};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        288..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          312..363
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          398..617
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          638..755
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          344..389
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         694
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   760 AA;  81964 MW;  20F944279A16A75A CRC64;
     MLGAFGHVDL GAACCGHPIV SIRFKLTLLV MAVLAPTLIA SLLAIGYVYQ DQRVRVAQSM
     RETTRALALA VDRDIAQRNA IIRTLSSVPS LSLADLERFY TTARDVADSW ENSIILVDTQ
     GQQLLNTRMP FGAELPHTPF LATPLDDPAA EFDVTNLYMA PIGKQYSFSV RRPIYIDGTL
     RYFLSMGSFA NQINEVLVDQ NLPKGWLGTV VDGSGRIVAR NISPEAFIGK HVTGPIAEAL
     GGSEEGFRET VSLDGIPLLS FYARSPESGW SVIIGLPISE VRQSAVQAMT VVGVFALLLI
     GVATLLAFWV GRRITRPLRM LDATAQAMGR GEAVHPASTG MSEIDRTAAV LAQASERIQN
     ASAEMSARVA AAVEQVERSQ KAMQQTQKLE ALGRLTGGIA HDFNNLLQTL TIGLQLADMA
     SSDPRAKKAI EACNKSVVRG TKLTRQLMAF GRHKVEETRH VDLLQLIVEM GDLLDGALPG
     RIGLTLELPE RPWPVFIDPL QCELAVLNLV FNARDAMPRG GKVTLSLAQR AVAEGEIEGL
     AAGAYAELCI VDSGEGMSEE VMSKAFEPFF TTKNVGEGTG LGLAQVYGFA SQAHGTVLLQ
     SAPGEGTRVR VLLPMSQEEG SVPLEAGAGP RPDVHSARVL LVDDDPLVRD VVAPALRELG
     FRVEVVGNAD EALQRYRERR GGAGKPRFDI VFSDIVMPGT LDGIGLAQAL REQEPNLPIV
     LATGYTERAP SDYGFTVLSK PYDVQTLVEA LRAELVRTAR
//
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