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LOVHK_PSESM
ID   LOVHK_PSESM             Reviewed;         534 AA.
AC   Q881J7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Blue-light-activated protein;
DE   Includes:
DE     RecName: Full=Blue-light-activated histidine kinase;
DE              EC=2.7.13.3;
DE     AltName: Full=PS-LOV-histidine kinase;
DE              Short=PS-LOV-HK;
DE   Includes:
DE     RecName: Full=Response regulator;
GN   OrderedLocusNames=PSPTO_2896;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
RN   [2]
RP   FUNCTION IN LIGHT SENSING, FLAVIN CHROMOPHORE, KINASE ACTIVITY, INDUCTION,
RP   AND ROLE IN VIRULENCE.
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=17717187; DOI=10.1126/science.1144306;
RA   Swartz T.E., Tseng T.-S., Frederickson M.A., Paris G., Comerci D.J.,
RA   Rajashekara G., Kim J.-G., Mudgett M.B., Splitter G.A., Ugalde R.A.,
RA   Goldbaum F.A., Briggs W.R., Bogomolni R.A.;
RT   "Blue-light-activated histidine kinases: two-component sensors in
RT   bacteria.";
RL   Science 317:1090-1093(2007).
CC   -!- FUNCTION: Photosensitive kinase and response regulator that is involved
CC       in increased bacterial virulence upon exposure to light.
CC       {ECO:0000269|PubMed:17717187}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- INDUCTION: Constitutively expressed when grown in minimal media.
CC       {ECO:0000269|PubMed:17717187}.
CC   -!- PTM: FMN binds covalently to cysteine after exposure to blue light and
CC       this bond is spontaneously broken in the dark.
CC   -!- MISCELLANEOUS: Treatment of phosphorylated protein with alkaline buffer
CC       to hydrolyze phospho-aspartates does not significantly reduce
CC       phosphorylation in assays performed in vitro. Therefore, it is not
CC       clear whether Asp-461 is really phosphorylated by His-164.
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DR   EMBL; AE016853; AAO56389.1; -; Genomic_DNA.
DR   RefSeq; NP_792694.1; NC_004578.1.
DR   RefSeq; WP_007243883.1; NC_004578.1.
DR   AlphaFoldDB; Q881J7; -.
DR   SMR; Q881J7; -.
DR   STRING; 223283.PSPTO_2896; -.
DR   EnsemblBacteria; AAO56389; AAO56389; PSPTO_2896.
DR   GeneID; 1184550; -.
DR   KEGG; pst:PSPTO_2896; -.
DR   PATRIC; fig|223283.9.peg.2955; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_114_51_6; -.
DR   OMA; HIRIETV; -.
DR   OrthoDB; 1755994at2; -.
DR   PhylomeDB; Q881J7; -.
DR   PHI-base; PHI:3796; -.
DR   Proteomes; UP000002515; 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   1: Evidence at protein level;
KW   ATP-binding; Chromophore; Flavoprotein; FMN; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Photoreceptor protein; Receptor; Reference proteome;
KW   Sensory transduction; Transferase; Virulence.
FT   CHAIN           1..534
FT                   /note="Blue-light-activated protein"
FT                   /id="PRO_0000361293"
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   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;  58935 MW;  F3D647AA3380F84B CRC64;
     MSENKTRVDN AATGDIQHQG KDIFFAAVET TRMPMIVTDP NRPDNPIIFS NRAFLEMTGY
     TAEEILGTNC RFLQGPDTDP AVVQSIRDAI AQRNDISAEI INYRKDGSSF WNALFISPVY
     NDAGDLIYFF ASQLDISRRK DAEEALRQAQ KMEALGQLTG GIAHDFNNLL QVMGGYIDLI
     GSAAEKPVID VQRVQRSVYH AKSAVERAST LTKQLLAFAR KQKLQGRVLN LNGLVSIVEP
     LIERTFGPEV AIETDLEPAL KNCRIDPTQA EVALLNIFIN ARDALIGREN PKVFIETRNL
     LVDELANMSY DGLLPGRYVS IAVTDNGIGM PASIRDRVMD PFFTTKEEGK GSGLGLSMVY
     GFAKQSGGAA RIYTEEGVGT TLRLYFPVDE AGLTNTESPQ ASDRRLGSSE RILIVEDRPD
     VAELAKMVLD DYGYVSEIVL NAREALKKFE SGNMYDLLFT DLIMPGGMNG VMLAREVRRR
     YPKVKVLLTT GYAESSIERT DIGGSEFDVV SKPCMPHDLA RKVRQVLDGP NGIA
 
 
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