ID   LOVHK_PSEU2             Reviewed;         534 AA.
AC   Q4ZSY3;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Blue-light-activated protein;
DE   Includes:
DE     RecName: Full=Blue-light-activated histidine kinase;
DE              EC=2.7.13.3;
DE   Includes:
DE     RecName: Full=Response regulator;
GN   OrderedLocusNames=Psyr_2700;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC   -!- FUNCTION: Photosensitive kinase and response regulator that is involved
CC       in increased bacterial virulence upon exposure to light. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- PTM: FMN binds covalently to cysteine after exposure to blue light and
CC       this bond is spontaneously broken in the dark. {ECO:0000250}.
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DR   EMBL; CP000075; AAY37739.1; -; Genomic_DNA.
DR   RefSeq; WP_011267901.1; NC_007005.1.
DR   RefSeq; YP_235777.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZSY3; -.
DR   SMR; Q4ZSY3; -.
DR   STRING; 205918.Psyr_2700; -.
DR   EnsemblBacteria; AAY37739; AAY37739; Psyr_2700.
DR   KEGG; psb:Psyr_2700; -.
DR   PATRIC; fig|205918.7.peg.2760; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_114_51_6; -.
DR   OMA; HIRIETV; -.
DR   PHI-base; PHI:7700; -.
DR   Proteomes; UP000000426; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.565.10; -; 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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chromophore; Flavoprotein; FMN; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Photoreceptor protein; Receptor; Sensory transduction;
KW   Transferase; Virulence.
FT   CHAIN           1..534
FT                   /note="Blue-light-activated protein"
FT                   /id="PRO_0000361294"
FT   DOMAIN          20..93
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          94..148
FT                   /note="PAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   DOMAIN          161..390
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   DOMAIN          411..527
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MOD_RES         70
FT                   /note="S-4a-FMN cysteine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         164
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         461
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   534 AA;  59022 MW;  902CEBFB71110593 CRC64;
     MSENKTRVDN AATGDIKHQG KDIFFAAVET TRMPMIVTDP NRPDNPIIFA NRAFLEMTGY
     ASEEIIGSNC RFLQGPDTDR TAVQSIRDAI DQRVDISTEI LNYRKDGSSF WNALFISPVY
     NDAGELIYFF ASQLDISRRR DAEEALRQAQ KMEALGQLTG GIAHDFNNLL QVMGGYIDLI
     GSAAEKPVID VQRVQRSVHH AKSAVERAST LTKQLLAFAR KQKLQGRVLN LNGLVSTTEP
     LIERTFGPEV IIETDLDPAL KNCRIDPTQA EVALLNIFIN ARDALIGRLN PKIFIETRNL
     VVDELANMSY DGLLPGRYVS IAVTDNGIGM PASIRDRVMD PFFTTKEEGK GSGLGLSMVY
     GFAKQSGGAA RIYTEEGVGT TLRLYFPVDE AVLSKNDPPK ASERRIGSSE RILIVEDRPD
     VAELAKMVLD DYGYVSEIVL NAREALKRFE AGATYDLLFT DLIMPGGMNG VMLAREVRRR
     FPKVKVLLTT GYAESSIERT DIGGSEFEVV SKPCMPQDLA RKVRQVLDGP NGIA