BLUF_ECOLI
ID BLUF_ECOLI Reviewed; 403 AA.
AC P75990;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Blue light- and temperature-regulated antirepressor BluF;
DE Short=Blrp;
GN Name=bluF {ECO:0000303|PubMed:22783906};
GN Synonyms=blrp {ECO:0000303|PubMed:15453820}, ycgF;
GN OrderedLocusNames=b1163, JW1150;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP INDUCTION BY COLD SHOCK.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=14527658; DOI=10.1016/s0923-2508(03)00167-0;
RA Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V., Pesole G.,
RA Deho G.;
RT "Changes in Escherichia coli transcriptome during acclimatization at low
RT temperature.";
RL Res. Microbiol. 154:573-580(2003).
RN [5]
RP FAD-BINDING, REVERSIBLE PHOTOCYCLE, AND MONOMERIC SUBUNIT.
RX PubMed=15453820; DOI=10.1562/2004-06-16-ra-203;
RA Rajagopal S., Key J.M., Purcell E.B., Boerema D.J., Moffat K.;
RT "Purification and initial characterization of a putative blue light-
RT regulated phosphodiesterase from Escherichia coli.";
RL Photochem. Photobiol. 80:542-547(2004).
RN [6]
RP LIGHT-INDUCED FOURIER TRANSFORM INFRARED (FTIR) DIFFERENCE SPECTROSCOPY.
RX PubMed=16533062; DOI=10.1021/bi051820x;
RA Hasegawa K., Masuda S., Ono T.A.;
RT "Light induced structural changes of a full-length protein and its BLUF
RT domain in YcgF(Blrp), a blue-light sensing protein that uses FAD (BLUF).";
RL Biochemistry 45:3785-3793(2006).
RN [7]
RP TRANSIENT DIMERIZATION.
RX PubMed=17489591; DOI=10.1021/ja065682q;
RA Nakasone Y., Ono T.A., Ishii A., Masuda S., Terazima M.;
RT "Transient dimerization and conformational change of a BLUF protein:
RT YcgF.";
RL J. Am. Chem. Soc. 129:7028-7035(2007).
RN [8]
RP FLAVIN-BINDING TO THE BLUF DOMAIN, AND IMPORTANCE OF THE JOINING HELIX.
RX PubMed=18792053; DOI=10.1002/cbic.200800280;
RA Schroeder C., Werner K., Otten H., Kratzig S., Schwalbe H., Essen L.O.;
RT "Influence of a joining helix on the BLUF domain of the YcgF photoreceptor
RT from Escherichia coli.";
RL ChemBioChem 9:2463-2473(2008).
RN [9]
RP LACK OF C-DI-GMP PHOSPHODIESTERASE ACTIVITY, FUNCTION, INTERACTION WITH
RP BLUR, MUTAGENESIS OF 193-ILE--GLN-195, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100;
RX PubMed=19240136; DOI=10.1101/gad.499409;
RA Tschowri N., Busse S., Hengge R.;
RT "The BLUF-EAL protein YcgF acts as a direct anti-repressor in a blue-light
RT response of Escherichia coli.";
RL Genes Dev. 23:522-534(2009).
RN [10]
RP INDUCTION, AND RPOS-REPRESSION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=19332833; DOI=10.1099/mic.0.024257-0;
RA Sommerfeldt N., Possling A., Becker G., Pesavento C., Tschowri N.,
RA Hengge R.;
RT "Gene expression patterns and differential input into curli fimbriae
RT regulation of all GGDEF/EAL domain proteins in Escherichia coli.";
RL Microbiology 155:1318-1331(2009).
RN [11]
RP CONFORMATION CHANGE AFTER PHOTOINDUCED DIMERIZATION.
RX PubMed=20141167; DOI=10.1021/bi902121z;
RA Nakasone Y., Ono T.A., Ishii A., Masuda S., Terazima M.;
RT "Temperature-sensitive reaction of a photosensor protein YcgF: possibility
RT of a role of temperature sensor.";
RL Biochemistry 49:2288-2296(2010).
RN [12]
RP FUNCTION, AND INTERACTION WITH BLUR AND MLRA.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=22783906; DOI=10.1111/j.1365-2958.2012.08147.x;
RA Tschowri N., Lindenberg S., Hengge R.;
RT "Molecular function and potential evolution of the biofilm-modulating blue
RT light-signalling pathway of Escherichia coli.";
RL Mol. Microbiol. 85:893-906(2012).
CC -!- FUNCTION: Binds to and releases the BluR repressor from its bound DNA
CC target in a blue light-dependent (470 nm) fashion. A shift to low
CC temperature also triggers a BluF-mediated relief of repression by BluR,
CC suggesting BluF may serve as a thermometer. Blue light may act to
CC increase the affinity of BluF for BluR, allowing it to be released from
CC its operator. The protein has a reversible photocycle, and undergoes
CC structural changes, probably in the EAL domain, in response to light.
CC {ECO:0000269|PubMed:15453820, ECO:0000269|PubMed:19240136,
CC ECO:0000269|PubMed:20141167, ECO:0000269|PubMed:22783906}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:15453820};
CC Note=Binds 1 FAD per subunit, non-covalently bound to the BLUF domain.
CC {ECO:0000269|PubMed:15453820};
CC -!- SUBUNIT: Monomer, it undergoes transient dimerization following
CC photoexcitation or upon temperature reduction, with a relaxation time
CC of about 2 minutes. The dimer may be the inactive state. Interacts with
CC the N- and C-terminal domains of BluR. Can also interact with the C-
CC terminal domain of MlrA. {ECO:0000269|PubMed:15453820,
CC ECO:0000269|PubMed:17489591, ECO:0000269|PubMed:19240136,
CC ECO:0000269|PubMed:20141167, ECO:0000269|PubMed:22783906}.
CC -!- INDUCTION: Expression is strongly activated by cold shock (over 30-fold
CC at 16 degrees Celsius compared to 37 degrees) at low temperature in a
CC PNPase-dependent fashion. Repressed by RpoS.
CC {ECO:0000269|PubMed:14527658, ECO:0000269|PubMed:19332833}.
CC -!- DOMAIN: The joining helix is required for stability of the light-
CC adapted state. {ECO:0000269|PubMed:18792053}.
CC -!- DOMAIN: Contains a defective C-terminal cyclic-di-GMP phosphodiesterase
CC EAL domain, which lacks key amino acids required for phosphodiesterase
CC activity. Restoration of consensus amino acids in the degenerate EAL
CC domain does not restore phosphodiesterase activity and reduces ability
CC to antagonize BluR. {ECO:0000269|PubMed:22783906}.
CC -!- DISRUPTION PHENOTYPE: Reduces expression of ycgZ in the presence but
CC not the absence of BluR. At 16 degrees Celsius, reduces expression of
CC genes (including ycgZ) for several small proteins. While the BluR/F
CC system is induced at low temperatures under blue light irradiation, it
CC is not essential for growth under these conditions.
CC {ECO:0000269|PubMed:19240136}.
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DR EMBL; U00096; AAC74247.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35998.1; -; Genomic_DNA.
DR PIR; H64861; H64861.
DR RefSeq; NP_415681.1; NC_000913.3.
DR RefSeq; WP_001299269.1; NZ_STEB01000023.1.
DR AlphaFoldDB; P75990; -.
DR SMR; P75990; -.
DR BioGRID; 4262864; 21.
DR DIP; DIP-11553N; -.
DR IntAct; P75990; 13.
DR STRING; 511145.b1163; -.
DR PaxDb; P75990; -.
DR PRIDE; P75990; -.
DR EnsemblBacteria; AAC74247; AAC74247; b1163.
DR EnsemblBacteria; BAA35998; BAA35998; BAA35998.
DR GeneID; 66675021; -.
DR GeneID; 947592; -.
DR KEGG; ecj:JW1150; -.
DR KEGG; eco:b1163; -.
DR PATRIC; fig|1411691.4.peg.1127; -.
DR EchoBASE; EB3646; -.
DR eggNOG; COG2200; Bacteria.
DR HOGENOM; CLU_000445_70_33_6; -.
DR InParanoid; P75990; -.
DR OMA; GISQFQG; -.
DR PhylomeDB; P75990; -.
DR BioCyc; EcoCyc:G6603-MON; -.
DR PRO; PR:P75990; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009882; F:blue light photoreceptor activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:0009637; P:response to blue light; IDA:EcoCyc.
DR CDD; cd01948; EAL; 1.
DR Gene3D; 3.20.20.450; -; 1.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR007024; BLUF_domain.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR Pfam; PF04940; BLUF; 1.
DR Pfam; PF00563; EAL; 1.
DR SMART; SM01034; BLUF; 1.
DR SMART; SM00052; EAL; 1.
DR SUPFAM; SSF141868; SSF141868; 1.
DR SUPFAM; SSF54975; SSF54975; 1.
DR PROSITE; PS50925; BLUF; 1.
DR PROSITE; PS50883; EAL; 1.
PE 1: Evidence at protein level;
KW Chromophore; FAD; Flavoprotein; Photoreceptor protein; Receptor;
KW Reference proteome; Sensory transduction.
FT CHAIN 1..403
FT /note="Blue light- and temperature-regulated antirepressor
FT BluF"
FT /id="PRO_0000168852"
FT DOMAIN 2..93
FT /note="BLUF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00030"
FT DOMAIN 155..403
FT /note="EAL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00074"
FT REGION 98..144
FT /note="Joining helix"
FT MUTAGEN 193..195
FT /note="IVQ->LVR: Does not confer c-di-GMP phosphodiesterase
FT activity."
FT /evidence="ECO:0000269|PubMed:19240136"
SQ SEQUENCE 403 AA; 45295 MW; 57B662BEC10957DA CRC64;
MLTTLIYRSH IRDDEPVKKI EEMVSIANRR NMQSDVTGIL LFNGSHFFQL LEGPEEQVKM
IYRAICQDPR HYNIVELLCD YAPARRFGKA GMELFDLRLH ERDDVLQAVF DKGTSKFQLT
YDDRALQFFR TFVLATEQST YFEIPAEDSW LFIADGSDKE LDSCALSPTI NDHFAFHPIV
DPLSRRIIAF EAIVQKNEDS PSAIAVGQRK DGEIYTADLK SKALAFTMAH ALELGDKMIS
INLLPMTLVN EPDAVSFLLN EIKANALVPE QIIVEFTESE VISRFDEFAE AIKSLKAAGI
SVAIDHFGAG FAGLLLLSRF QPDRIKISQE LITNVHKSGP RQAIIQAIIK CCTSLEIQVS
AMGVATPEEW MWLESAGIEM FQGDLFAKAK LNGIPSIAWP EKK
