ID   LOVHK_BRUSU             Reviewed;         489 AA.
AC   Q8FW73; G0KCW6;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Blue-light-activated histidine kinase;
DE            EC=2.7.13.3;
GN   OrderedLocusNames=BRA0588, BS1330_II0583;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
CC   -!- FUNCTION: Photosensitive kinase that is involved in increased bacterial
CC       virulence upon exposure to light. Once ejected from an infected animal
CC       host, sunlight acts as an environmental signal that increases the
CC       virulence of the bacterium, preparing it for infection of the next
CC       host. This photoreceptor protein is directly related to the bacterium's
CC       survival and replication within host macrophages (By similarity).
CC       {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN33777.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AEM20054.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014292; AAN33777.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002998; AEM20054.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002971240.1; NZ_KN046805.1.
DR   AlphaFoldDB; Q8FW73; -.
DR   SMR; Q8FW73; -.
DR   EnsemblBacteria; AEM20054; AEM20054; BS1330_II0583.
DR   GeneID; 45053625; -.
DR   GeneID; 55592260; -.
DR   KEGG; bms:BRA0588; -.
DR   KEGG; bsi:BS1330_II0583; -.
DR   PATRIC; fig|204722.21.peg.552; -.
DR   HOGENOM; CLU_000445_114_57_5; -.
DR   Proteomes; UP000007104; Chromosome II.
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; 2.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR   Pfam; PF07536; HWE_HK; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   SMART; SM00911; HWE_HK; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55785; SSF55785; 2.
DR   TIGRFAMs; TIGR00229; sensory_box; 2.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chromophore; Flavoprotein; FMN; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Photoreceptor protein; Receptor; Repeat;
KW   Sensory transduction; Transferase; Virulence.
FT   CHAIN           1..489
FT                   /note="Blue-light-activated histidine kinase"
FT                   /id="PRO_0000361288"
FT   DOMAIN          19..93
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          93..147
FT                   /note="PAC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   DOMAIN          232..281
FT                   /note="PAC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   REGION          259..341
FT                   /note="HWE histidine kinase domain"
FT   MOD_RES         69
FT                   /note="S-4a-FMN cysteine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         288
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   489 AA;  54874 MW;  6F2A04467FB26C5B CRC64;
     MAIDLRPFIP FGRGALSQAT DPFRAAVEFT LMPMLITNPH LPDNPIVFAN PAFLKLTGYE
     ADEVMGRNCR FLQGHGTDPA HVRAIKSAIA AEKPIDIDII NYKKSGEAFW NRLHISPVHN
     ANGRLQHFVS SQLDVTLELS RLVELEKERK TLSIETARSK DQLDYIVEVA NIGFWTREFY
     SGKMTCSAEC RRIYGFTPDE PVHFDTILDL VVLEDRMTVV QKAHQAVTGE PYSIEYRIVT
     RLGETRWLET RAKALTGENP LVLGIVQDVT ERKKAEANKA LVSREIAHRF KNSMAMVQSI
     ANQTLRNTYD PEQANRLFSE RLRALSQAHD MLLKENWAGA TIQQICATAL APFNSTFANR
     IHMSGPHLLV SDRVTVALSL AFYELATNAV KYGALSNEKG VINITWAIME DKGEKKFHMR
     WAESRGPEVM QPARRGFGQR LLHSVLAEEL KAKCDVEFAA SGLLIDVLAP ITPEVFPGMG
     HNVPEQRIA