LVHK2_ERYLH
ID LVHK2_ERYLH Reviewed; 346 AA.
AC Q2NB77;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Blue-light-activated histidine kinase 2;
DE EC=2.7.13.3;
DE AltName: Full=EL346-LOV-histidine kinase;
DE Short=EL346-LOV-HK;
GN OrderedLocusNames=ELI_04860;
OS Erythrobacter litoralis (strain HTCC2594).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=314225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2594;
RX PubMed=19168610; DOI=10.1128/jb.00026-09;
RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL J. Bacteriol. 191:2419-2420(2009).
RN [2]
RP FUNCTION IN LIGHT SENSING, FLAVIN CHROMOPHORE, KINASE ACTIVITY, AND ROLE IN
RP VIRULENCE.
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. {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 -!- PTM: FMN binds covalently to cysteine after exposure to blue light and
CC this bond is spontaneously broken in the dark.
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DR EMBL; CP000157; ABC63064.1; -; Genomic_DNA.
DR RefSeq; WP_011413900.1; NC_007722.1.
DR PDB; 4R38; X-ray; 1.60 A; A/B/C/D=1-134.
DR PDB; 4R39; X-ray; 2.60 A; A/B/C/D=121-346.
DR PDB; 4R3A; X-ray; 2.92 A; A/B=1-346.
DR PDBsum; 4R38; -.
DR PDBsum; 4R39; -.
DR PDBsum; 4R3A; -.
DR AlphaFoldDB; Q2NB77; -.
DR SMR; Q2NB77; -.
DR STRING; 314225.ELI_04860; -.
DR EnsemblBacteria; ABC63064; ABC63064; ELI_04860.
DR KEGG; eli:ELI_04860; -.
DR eggNOG; COG3920; Bacteria.
DR HOGENOM; CLU_000445_114_57_5; -.
DR OMA; DWQLTER; -.
DR OrthoDB; 1755994at2; -.
DR Proteomes; UP000008808; Chromosome.
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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR Pfam; PF13581; HATPase_c_2; 1.
DR Pfam; PF07568; HisKA_2; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
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; Sensory transduction; Transferase; Virulence.
FT CHAIN 1..346
FT /note="Blue-light-activated histidine kinase 2"
FT /id="PRO_0000361290"
FT DOMAIN 8..82
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 79..133
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 139..334
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 55
FT /note="S-4a-FMN cysteine"
FT MOD_RES 142
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT HELIX 10..14
FT /evidence="ECO:0007829|PDB:4R3A"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:4R38"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:4R38"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:4R38"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:4R38"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:4R38"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:4R38"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:4R38"
FT STRAND 94..104
FT /evidence="ECO:0007829|PDB:4R38"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:4R38"
FT HELIX 130..141
FT /evidence="ECO:0007829|PDB:4R39"
FT HELIX 146..162
FT /evidence="ECO:0007829|PDB:4R39"
FT HELIX 172..189
FT /evidence="ECO:0007829|PDB:4R39"
FT HELIX 201..216
FT /evidence="ECO:0007829|PDB:4R39"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:4R39"
FT HELIX 234..254
FT /evidence="ECO:0007829|PDB:4R39"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:4R39"
FT STRAND 262..270
FT /evidence="ECO:0007829|PDB:4R39"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:4R39"
FT STRAND 275..282
FT /evidence="ECO:0007829|PDB:4R39"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:4R39"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:4R39"
FT HELIX 299..310
FT /evidence="ECO:0007829|PDB:4R39"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:4R39"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:4R39"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:4R39"
FT HELIX 335..341
FT /evidence="ECO:0007829|PDB:4R39"
SQ SEQUENCE 346 AA; 37948 MW; 061BB3B0E412D440 CRC64;
MAVGLAEHDK EAWGRLPFSL TIADISQDDE PLIYVNRAFE QMTGYSRSSV VGRNCRFLQG
EKTDPGAVER LAKAIRNCEE VEETIYNYRA DGEGFWNHLL MGPLEDQDEK CRYFVGIQVD
MGQSESPDRA TELDRQLAEV QHRVKNHLAM IVSMIRIQSS QAGGVGSQFD SLSRRVEALQ
LLYQEMDIAG AAKATDKIIP LGAYLGRIAS AINHIDGRGA IKVNVQADTV DVPVETAGRI
GLLVSEVLTN ALQHAFSDRA SGVVQLRSSV MSGEQLRVTV EDDGRGIPED CDWPNEGNLG
SRIVRQLVQG LGAELNVTRG GTGTIVNIDI PLSQQKTLIA DERTKD
