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Database: UniProt
Entry: A0A1H3CD87_9PSED
LinkDB: A0A1H3CD87_9PSED
Original site: A0A1H3CD87_9PSED 
ID   A0A1H3CD87_9PSED        Unreviewed;       911 AA.
AC   A0A1H3CD87;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05216287_3208 {ECO:0000313|EMBL:SDX52083.1};
OS   Pseudomonas kuykendallii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1007099 {ECO:0000313|EMBL:SDX52083.1, 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; FNNU01000004; SDX52083.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3CD87; -.
DR   STRING; 1007099.SAMN05216287_3208; -.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.60.40.2380; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR   InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR   Pfam; PF07696; 7TMR-DISMED2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 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; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SDX52083.1}; 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:0000313|EMBL:SDX52083.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        166..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        191..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        225..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        258..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        283..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        311..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          395..616
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          768..889
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         819
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   911 AA;  101324 MW;  B471BD3F917378FF CRC64;
     MPVAPLDQDE LRLSLGPYVG ILEDPEGLLD IEQVRRIEDR LFRPAPGVYP NMGKSRSTWW
     LKVDLRNSRP HTLDGFIEVN YPLLDDIQLY LIAPDGTLTR QAGGDTHPFG ERPVPVRNFW
     FPTRVPPGDS VLLVRVQTTS TAFVPLFFAT HAASASAQEV AMGFNGAFYG VLFAMFCYNL
     FLYLSLREPA YFWYLMYNVN IGLFAASFDG LMFQMLPDWL ELEALGIYAL MYSHCLFALQ
     FSRHFLHTRQ HFPSMDRALQ LLMLGTVVCL CSEPLIGMMA WTILASLTVL TVSFFSLLAG
     IYVWNAGLRY GSYYMLAWGV LLLTFIQATT GSLGLEVFGI YGATAVKIGV TVELITLSIG
     LADRINLLKE EGFLSRQTAE QAVIENKAKS RFLATMSHEI RTPLNGVLGM LQLLKETSLD
     RSQRFYVETI ASSGTALMAV INDILDYARI ESGKLTLENI SFDLEELVSD TLSLFTAQAM
     EKRLRLHVSL EGGVPQRIKG DPTRLKQVLM NLLGNAIKFT AEGHVALGVT RRTDARGQEQ
     LVFSVSDSGI GMRREVLNTL FQSFAQGDSS TTRRYGGSGL GLAISKELVE MMGGRIEAQS
     KLGQGTRFTF DIPLQAEPDT DELRHLLEGQ HALLASLDAT ALETVGHLLR RWGIHTEHCQ
     SPEHLLERLE SAPSPQLLVL MAPWPGSAEY WLDSLRSSLA PGQRVLLLCP PEQCQRVPAS
     QVLKLFALAQ PISVKPLREA LLKVYDRTEE LPPEAAPAPR QALGDAPCVL VAEDNAVNQL
     VVQGFLRKRG YRIRLVSNGV AAVEEYRHFP RGVQAILMDC EMPEMDGFEA TRRIRQLERE
     QDLPPVPIIA LTAHILEEHR QQGAAVGMDD FLGKPLDSLL LYATLERYLP RPSPAAAPVV
     EGTDDHSRPA R
//
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