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 27-MAR-2024, entry version 101. 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; Pseudomonadota; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 Gene3D; 2.10.70.100; -; 1. DR Gene3D; 3.30.450.20; PAS domain; 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 NCBIfam; TIGR00229; sensory_box; 2. DR PANTHER; PTHR41523:SF7; ETHYLENE RESPONSE SENSOR PROTEIN; 1. DR PANTHER; PTHR41523; TWO-COMPONENT SYSTEM SENSOR PROTEIN; 1. 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; PYP-like sensor domain (PAS domain); 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 //