LOVHK_BRUA2
ID LOVHK_BRUA2 Reviewed; 489 AA.
AC Q2YKK7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Blue-light-activated histidine kinase;
DE EC=2.7.13.3;
DE AltName: Full=BA-LOV-histidine kinase;
DE Short=BA-LOV-HK;
GN OrderedLocusNames=BAB2_0652;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
RN [2]
RP ROLE IN VIRULENCE, INDUCTION, AND MUTAGENESIS OF CYS-69.
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 host
CC (By similarity). This photoreceptor protein is directly related to the
CC bacterium's survival and replication within host macrophages, as it is
CC required for optimal replication of bacteria inside macrophages.
CC {ECO:0000250, 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. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAJ12818.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM040265; CAJ12818.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002971240.1; NZ_KN046823.1.
DR PDB; 5EPV; X-ray; 2.51 A; A/B/C/D=266-489.
DR PDB; 6PPS; X-ray; 2.80 A; A/B/C/D=1-273.
DR PDBsum; 5EPV; -.
DR PDBsum; 6PPS; -.
DR AlphaFoldDB; Q2YKK7; -.
DR SMR; Q2YKK7; -.
DR STRING; 359391.BAB2_0652; -.
DR EnsemblBacteria; CAJ12818; CAJ12818; BAB2_0652.
DR GeneID; 45053625; -.
DR GeneID; 55592260; -.
DR KEGG; bmf:BAB2_0652; -.
DR PATRIC; fig|359391.11.peg.2834; -.
DR HOGENOM; CLU_000445_114_57_5; -.
DR BRENDA; 2.7.13.3; 994.
DR PHI-base; PHI:3306; -.
DR Proteomes; UP000002719; 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 Reference proteome; Repeat; Sensory transduction; Transferase; Virulence.
FT CHAIN 1..489
FT /note="Blue-light-activated histidine kinase"
FT /id="PRO_0000361282"
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"
FT MUTAGEN 69
FT /note="C->A: Loss of ability to multiply efficiently inside
FT host macrophages."
FT /evidence="ECO:0000269|PubMed:17717187"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:6PPS"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:6PPS"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:6PPS"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:6PPS"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:6PPS"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:6PPS"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:6PPS"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:6PPS"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:6PPS"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6PPS"
FT STRAND 108..119
FT /evidence="ECO:0007829|PDB:6PPS"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:6PPS"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:6PPS"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:6PPS"
FT HELIX 141..169
FT /evidence="ECO:0007829|PDB:6PPS"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:6PPS"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:6PPS"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:6PPS"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:6PPS"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6PPS"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:6PPS"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:6PPS"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:6PPS"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:6PPS"
FT STRAND 245..255
FT /evidence="ECO:0007829|PDB:6PPS"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:6PPS"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:6PPS"
FT HELIX 270..304
FT /evidence="ECO:0007829|PDB:5EPV"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:5EPV"
FT HELIX 311..333
FT /evidence="ECO:0007829|PDB:5EPV"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:5EPV"
FT HELIX 342..356
FT /evidence="ECO:0007829|PDB:5EPV"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:5EPV"
FT HELIX 372..391
FT /evidence="ECO:0007829|PDB:5EPV"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:5EPV"
FT STRAND 401..427
FT /evidence="ECO:0007829|PDB:5EPV"
FT HELIX 437..444
FT /evidence="ECO:0007829|PDB:5EPV"
FT HELIX 446..450
FT /evidence="ECO:0007829|PDB:5EPV"
FT STRAND 453..459
FT /evidence="ECO:0007829|PDB:5EPV"
FT STRAND 462..470
FT /evidence="ECO:0007829|PDB:5EPV"
FT TURN 473..475
FT /evidence="ECO:0007829|PDB:5EPV"
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
