ID   LOVHK_RHIL3             Reviewed;         345 AA.
AC   Q1M667;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Blue-light-activated histidine kinase;
DE            EC=2.7.13.3;
DE   AltName: Full=R-LOV-histidine kinase;
DE            Short=R-LOV-HK;
GN   Name=lov; OrderedLocusNames=pRL110320;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OG   Plasmid pRL11.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
RN   [2]
RP   FUNCTION, FLAVIN CHROMOPHORE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   CYS-75 AND HIS-163.
RC   STRAIN=3841;
RX   PubMed=22773814; DOI=10.1073/pnas.1121292109;
RA   Bonomi H.R., Posadas D.M., Paris G., Carrica Mdel C., Frederickson M.,
RA   Pietrasanta L.I., Bogomolni R.A., Zorreguieta A., Goldbaum F.A.;
RT   "Light regulates attachment, exopolysaccharide production, and nodulation
RT   in Rhizobium leguminosarum through a LOV-histidine kinase photoreceptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12135-12140(2012).
CC   -!- FUNCTION: Photoreceptor that regulates flagella synthesis,
CC       exopolysaccharide production and biofilm formation in response to
CC       light. Also required for competitive nodulation.
CC       {ECO:0000269|PubMed:22773814}.
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
CC       (Probable). {ECO:0000269|PubMed:22773814}.
CC   -!- DISRUPTION PHENOTYPE: Mutant produces similar amounts of
CC       exopolysaccharides and shows no significant differences in the biofilm
CC       biomass between light and dark conditions. Mutant also forms a higher
CC       number of white nodules compared with the wild-type, independently of
CC       the illumination conditions. {ECO:0000269|PubMed:22773814}.
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DR   EMBL; AM236085; CAK03271.1; -; Genomic_DNA.
DR   RefSeq; WP_011655064.1; NC_008384.1.
DR   AlphaFoldDB; Q1M667; -.
DR   SMR; Q1M667; -.
DR   EnsemblBacteria; CAK03271; CAK03271; pRL110320.
DR   KEGG; rle:pRL110320; -.
DR   HOGENOM; CLU_000445_114_57_5; -.
DR   OMA; EHRLEFM; -.
DR   OrthoDB; 1755994at2; -.
DR   Proteomes; UP000006575; Plasmid pRL11.
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   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55785; SSF55785; 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; Plasmid; Receptor;
KW   Sensory transduction; Transferase.
FT   CHAIN           1..345
FT                   /note="Blue-light-activated histidine kinase"
FT                   /id="PRO_0000424955"
FT   DOMAIN          25..98
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          99..153
FT                   /note="PAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..236
FT                   /note="HWE histidine kinase domain"
FT   MOD_RES         75
FT                   /note="S-4a-FMN cysteine"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         163
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         75
FT                   /note="C->A: Lack of activity."
FT                   /evidence="ECO:0000269|PubMed:22773814"
FT   MUTAGEN         163
FT                   /note="H->A: Lack of activity."
FT                   /evidence="ECO:0000269|PubMed:22773814"
SQ   SEQUENCE   345 AA;  37723 MW;  A0EFA9E891E969A5 CRC64;
     MTPHTKEKLH GDLPSASSKA ASADRKELAA IAFERTRMPM VVTDGRKPDL PIVLANKAFL
     ELTGYPAQEV LGRNCRFLQG PATSPIAVAE IRAAIAGERE VSVEILNYKK SGEQFWNRLH
     LSPVHGDDGK ILYFFGSQID MTEYRRIEAL EASEHRLLME VDHRSKNVLA IVDSIVRLSN
     ADDPALYAAA IQHRVQALAR AHTLLAARGW TNISLEELIR QQVTPFAATR AIFNGPDINM
     PAPVVQPLAL VLHELAVNAA HHGALAVAQG RLSISWKPRP SGAGFYIRWQ EVGAPTPPKL
     AKRGFGTVIV GAMVEKQLKG RLQKIWSDEG LLIDIEIPSA GPTCA