LOVHK_BRUME
ID LOVHK_BRUME Reviewed; 489 AA.
AC Q8YC53;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Blue-light-activated histidine kinase;
DE EC=2.7.13.3;
DE AltName: Full=BM-LOV-histidine kinase;
DE Short=BM-LOV-HK;
GN OrderedLocusNames=BMEII0679;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
RN [2]
RP FUNCTION IN LIGHT SENSING, FLAVIN CHROMOPHORE, ADDUCT STATE STABILITY,
RP KINASE ACTIVITY, INDUCTION, ROLE IN VIRULENCE, AND MUTAGENESIS OF CYS-69.
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
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. 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.
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: Induced after invasion of host macrophages.
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. However, this protein
CC presents an adduct state that is extremely and unusually stable and
CC does not decay measurably in 2h.
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DR EMBL; AE008918; AAL53921.1; -; Genomic_DNA.
DR PIR; AF3594; AF3594.
DR RefSeq; WP_002971240.1; NZ_GG703779.1.
DR PDB; 3T50; X-ray; 1.64 A; A/B=28-139.
DR PDB; 6PH2; X-ray; 2.34 A; A/B/C/D=15-155.
DR PDB; 6PH3; X-ray; 2.74 A; A/B/C/D=15-273.
DR PDB; 6PH4; X-ray; 3.25 A; A/B=15-489.
DR PDBsum; 3T50; -.
DR PDBsum; 6PH2; -.
DR PDBsum; 6PH3; -.
DR PDBsum; 6PH4; -.
DR AlphaFoldDB; Q8YC53; -.
DR SMR; Q8YC53; -.
DR STRING; 224914.BMEII0679; -.
DR EnsemblBacteria; AAL53921; AAL53921; BMEII0679.
DR GeneID; 45053625; -.
DR GeneID; 55592260; -.
DR KEGG; bme:BMEII0679; -.
DR PATRIC; fig|224914.52.peg.2686; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG3920; Bacteria.
DR OMA; EHRLEFM; -.
DR BRENDA; 2.7.13.3; 995.
DR PHI-base; PHI:3169; -.
DR Proteomes; UP000000419; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chromophore; Flavoprotein; FMN; Kinase;
KW Nucleotide-binding; Phosphoprotein; Photoreceptor protein; Receptor;
KW Repeat; Sensory transduction; Transferase; Virulence.
FT CHAIN 1..489
FT /note="Blue-light-activated histidine kinase"
FT /id="PRO_0000361285"
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 285..367
FT /note="HWE histidine kinase domain"
FT MOD_RES 69
FT /note="S-4a-FMN cysteine"
FT MOD_RES 288
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MUTAGEN 69
FT /note="C->A: No effect on FMN binding; loss of ability to
FT form S-4a-FMN cysteine; loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:17717187"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:6PH2"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:3T50"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:3T50"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:3T50"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:3T50"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:3T50"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:3T50"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:3T50"
FT STRAND 108..119
FT /evidence="ECO:0007829|PDB:3T50"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:3T50"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:3T50"
FT HELIX 141..169
FT /evidence="ECO:0007829|PDB:6PH3"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:6PH3"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:6PH3"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:6PH3"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:6PH3"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:6PH3"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:6PH3"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:6PH3"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:6PH3"
FT STRAND 245..255
FT /evidence="ECO:0007829|PDB:6PH3"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:6PH3"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:6PH3"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:6PH4"
FT HELIX 276..286
FT /evidence="ECO:0007829|PDB:6PH4"
FT TURN 287..290
FT /evidence="ECO:0007829|PDB:6PH4"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:6PH4"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:6PH4"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6PH4"
FT TURN 311..322
FT /evidence="ECO:0007829|PDB:6PH4"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:6PH4"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:6PH4"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:6PH4"
FT HELIX 342..348
FT /evidence="ECO:0007829|PDB:6PH4"
FT TURN 349..352
FT /evidence="ECO:0007829|PDB:6PH4"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:6PH4"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:6PH4"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:6PH4"
FT HELIX 372..391
FT /evidence="ECO:0007829|PDB:6PH4"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:6PH4"
FT STRAND 401..409
FT /evidence="ECO:0007829|PDB:6PH4"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:6PH4"
FT STRAND 416..425
FT /evidence="ECO:0007829|PDB:6PH4"
FT HELIX 438..441
FT /evidence="ECO:0007829|PDB:6PH4"
FT TURN 442..451
FT /evidence="ECO:0007829|PDB:6PH4"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:6PH4"
FT STRAND 460..469
FT /evidence="ECO:0007829|PDB:6PH4"
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
