LVHTH_ERYLH
ID LVHTH_ERYLH Reviewed; 225 AA.
AC Q2NB98;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Light-activated DNA-binding protein EL222 {ECO:0000303|PubMed:21606338};
DE Short=EL222 {ECO:0000303|PubMed:21606338};
DE AltName: Full=LOV-HTH DNA-binding protein;
GN OrderedLocusNames=ELI_04755;
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 X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 4-225 IN COMPLEX WITH FMN IN THE
RP DARK STATE, FUNCTION, SUBUNIT, DOMAIN, FLAVIN CHROMOPHORE, DNA-BINDING, AND
RP MUTAGENESIS OF LEU-123.
RX PubMed=21606338; DOI=10.1073/pnas.1100262108;
RA Nash A.I., McNulty R., Shillito M.E., Swartz T.E., Bogomolni R.A.,
RA Luecke H., Gardner K.H.;
RT "Structural basis of photosensitivity in a bacterial light-oxygen-
RT voltage/helix-turn-helix (LOV-HTH) DNA-binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9449-9454(2011).
CC -!- FUNCTION: Has reversible, light-dependent DNA-binding activity. Upon
CC illumination an internal FMN-protein adduct is formed which changes the
CC protein conformation so that the previously sequestered DNA-binding
CC domain is free to bind DNA. Binds to sequences within in its own
CC promoter when illuminated but not when it has been incubated in the
CC dark. {ECO:0000269|PubMed:21606338}.
CC -!- SUBUNIT: Monomer in solution, probably binds DNA as a homodimer.
CC {ECO:0000305|PubMed:21606338}.
CC -!- DOMAIN: Light induces structural changes; in the dark protein is
CC compact and resistant to exogenous protease, in the light protein is
CC less compact while protease treatment generates an N-terminal fragment
CC corresponding to approximately residues 14-156 (the LOV domain).
CC {ECO:0000269|PubMed:21606338}.
CC -!- PTM: FMN binds covalently to cysteine after exposure to blue light,
CC this bond is spontaneously broken in the dark; Cys-78 is 3.9 Angstroms
CC from C4a of FMN in the dark, suggesting this is the adduct that is
CC made. {ECO:0000305|PubMed:21606338}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
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DR EMBL; CP000157; ABC63043.1; -; Genomic_DNA.
DR PDB; 3P7N; X-ray; 2.10 A; A/B=4-225.
DR PDBsum; 3P7N; -.
DR AlphaFoldDB; Q2NB98; -.
DR SMR; Q2NB98; -.
DR STRING; 314225.ELI_04755; -.
DR EnsemblBacteria; ABC63043; ABC63043; ELI_04755.
DR KEGG; eli:ELI_04755; -.
DR eggNOG; COG4566; Bacteria.
DR HOGENOM; CLU_1239118_0_0_5; -.
DR OMA; VECNDAF; -.
DR EvolutionaryTrace; Q2NB98; -.
DR Proteomes; UP000008808; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd06170; LuxR_C_like; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00196; GerE; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00038; HTHLUXR.
DR SMART; SM00421; HTH_LUXR; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromophore; DNA-binding; Flavoprotein; FMN;
KW Nucleotide-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..225
FT /note="Light-activated DNA-binding protein EL222"
FT /id="PRO_0000435112"
FT DOMAIN 51..77
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 102..156
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 159..224
FT /note="HTH luxR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT DNA_BIND 183..202
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 77..79
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0007744|PDB:3P7N"
FT BINDING 95
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0007744|PDB:3P7N"
FT BINDING 110
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0007744|PDB:3P7N"
FT BINDING 141
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0007744|PDB:3P7N"
FT MOD_RES 78
FT /note="S-4a-FMN cysteine"
FT /evidence="ECO:0000305|PubMed:21606338"
FT MUTAGEN 123
FT /note="L->K: Alters conformation of protein; constitutively
FT binds DNA and is more sensitive to protease than wild-type
FT in the dark."
FT /evidence="ECO:0000269|PubMed:21606338"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:3P7N"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:3P7N"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:3P7N"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:3P7N"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3P7N"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:3P7N"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:3P7N"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:3P7N"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:3P7N"
FT STRAND 117..128
FT /evidence="ECO:0007829|PDB:3P7N"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:3P7N"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:3P7N"
FT HELIX 168..178
FT /evidence="ECO:0007829|PDB:3P7N"
FT HELIX 183..190
FT /evidence="ECO:0007829|PDB:3P7N"
FT HELIX 194..207
FT /evidence="ECO:0007829|PDB:3P7N"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:3P7N"
SQ SEQUENCE 225 AA; 24741 MW; B9B0267263993430 CRC64;
MLDMGQDRPI DGSGAPGADD TRVEVQPPAQ WVLDLIEASP IASVVSDPRL ADNPLIAINQ
AFTDLTGYSE EECVGRNCRF LAGSGTEPWL TDKIRQGVRE HKPVLVEILN YKKDGTPFRN
AVLVAPIYDD DDELLYFLGS QVEVDDDQPN MGMARRERAA EMLKTLSPRQ LEVTTLVASG
LRNKEVAARL GLSEKTVKMH RGLVMEKLNL KTSADLVRIA VEAGI
