ID   LVHK1_ERYLH             Reviewed;         360 AA.
AC   Q2NCA3;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Blue-light-activated histidine kinase 1;
DE            EC=2.7.13.3;
DE   AltName: Full=EL360-LOV-histidine kinase;
DE            Short=EL360-LOV-HK;
GN   OrderedLocusNames=ELI_02980;
OS   Erythrobacter litoralis (strain HTCC2594).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=314225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2594;
RX   PubMed=19168610; DOI=10.1128/jb.00026-09;
RA   Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL   J. Bacteriol. 191:2419-2420(2009).
RN   [2]
RP   FUNCTION IN LIGHT SENSING, FLAVIN CHROMOPHORE, KINASE ACTIVITY, AND ROLE IN
RP   VIRULENCE.
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 that is involved in increased bacterial
CC       virulence upon exposure to light. {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   -!- PTM: FMN binds covalently to cysteine after exposure to blue light and
CC       this bond is spontaneously broken in the dark.
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DR   EMBL; CP000157; ABC62688.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2NCA3; -.
DR   SMR; Q2NCA3; -.
DR   STRING; 314225.ELI_02980; -.
DR   EnsemblBacteria; ABC62688; ABC62688; ELI_02980.
DR   KEGG; eli:ELI_02980; -.
DR   eggNOG; COG3920; Bacteria.
DR   HOGENOM; CLU_000445_114_57_5; -.
DR   OMA; EMEEYSH; -.
DR   Proteomes; UP000008808; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR   Pfam; PF07536; HWE_HK; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   SMART; SM00911; HWE_HK; 1.
DR   SMART; SM00086; PAC; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 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..360
FT                   /note="Blue-light-activated histidine kinase 1"
FT                   /id="PRO_0000361289"
FT   DOMAIN          38..109
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          109..163
FT                   /note="PAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   REGION          260..303
FT                   /note="HWE histidine kinase domain"
FT   MOD_RES         85
FT                   /note="S-4a-FMN cysteine"
FT   MOD_RES         173
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   360 AA;  39975 MW;  51D26E97C1D62717 CRC64;
     MPLKGEISAQ AGREFDTSRL DLRAIIDPRD LRVDPTRLFL ETTQQTRLAI CISDPHQPDC
     PVVYVNQAFL DLTGYAREEI VGRNCRFLQG ADTDPEQVRK LREGIAAERY TVVDLLNYRK
     DGIPFWNAVH VGPIYGEDGT LQYFYGSQWD ITDIVAERRK AETQRRIAAE LRHRTGNIFA
     VLNAIIGLTS RRERDVSEFA DKLSERVSAL ASAHRMTIMD EPDQEAVAID DLVTGVMKPY
     RNRFAERVTT SGPKIELGPR SVTALGLALH ELATNAVKYG ALSVDAGRVE ISWSREDGDV
     TLVWQEQGGP TVSQEQSEPV KGNGTMLIDG MIASLTGSIE RDFAAAGLQA KITLPVHQPE