QSEF_ECO57
ID QSEF_ECO57 Reviewed; 444 AA.
AC P0AFU5; P21712; P77512;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Transcriptional regulatory protein QseF;
DE AltName: Full=Quorum-sensing regulator protein F;
GN Name=qseF; Synonyms=yfhA; OrderedLocusNames=Z3830, ECs3420;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP FUNCTION IN VIRULENCE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=O157:H7 / 86-24 / EHEC;
RX PubMed=17220220; DOI=10.1128/jb.01848-06;
RA Reading N.C., Torres A.G., Kendall M.M., Hughes D.T., Yamamoto K.,
RA Sperandio V.;
RT "A novel two-component signaling system that activates transcription of an
RT enterohemorrhagic Escherichia coli effector involved in remodeling of host
RT actin.";
RL J. Bacteriol. 189:2468-2476(2007).
RN [4]
RP FUNCTION.
RC STRAIN=O157:H7 / 86-24 / EHEC;
RX PubMed=19289831; DOI=10.1073/pnas.0811409106;
RA Reading N.C., Rasko D.A., Torres A.G., Sperandio V.;
RT "The two-component system QseEF and the membrane protein QseG link
RT adrenergic and stress sensing to bacterial pathogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5889-5894(2009).
RN [5]
RP FUNCTION.
RC STRAIN=O157:H7 / 86-24 / EHEC;
RX PubMed=20056703; DOI=10.1099/mic.0.033027-0;
RA Reading N.C., Rasko D., Torres A.G., Sperandio V.;
RT "A transcriptome study of the QseEF two-component system and the QseG
RT membrane protein in enterohaemorrhagic Escherichia coli O157:H7.";
RL Microbiology 156:1167-1175(2010).
CC -!- FUNCTION: Member of the two-component regulatory system QseF/QseE
CC involved in the regulation of virulence and metabolism in EHEC.
CC Required for pedestal formation in host epithelial cells during
CC infection. Regulates various metabolic and virulence genes, many iron-
CC utilization genes and some two-component systems such as RcsB/RcsC and
CC PhoP/PhoQ. Activates, indirectly, transcription of EspF(U) to induce
CC pedestal formation. {ECO:0000269|PubMed:17220220,
CC ECO:0000269|PubMed:19289831, ECO:0000269|PubMed:20056703}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by epinephrine during late exponential growth,
CC probably via the QseC sensor. {ECO:0000269|PubMed:17220220}.
CC -!- PTM: Phosphorylated by QseE. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mutants are unable to form pedestals.
CC {ECO:0000269|PubMed:17220220}.
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DR EMBL; AE005174; AAG57668.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36843.1; -; Genomic_DNA.
DR PIR; D91056; D91056.
DR PIR; H85900; H85900.
DR RefSeq; NP_311447.1; NC_002695.1.
DR RefSeq; WP_001295369.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AFU5; -.
DR SMR; P0AFU5; -.
DR STRING; 155864.EDL933_3719; -.
DR EnsemblBacteria; AAG57668; AAG57668; Z3830.
DR EnsemblBacteria; BAB36843; BAB36843; ECs_3420.
DR GeneID; 914905; -.
DR KEGG; ece:Z3830; -.
DR KEGG; ecs:ECs_3420; -.
DR PATRIC; fig|386585.9.peg.3574; -.
DR eggNOG; COG2204; Bacteria.
DR HOGENOM; CLU_000445_0_6_6; -.
DR OMA; YRAVVMS; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; DNA-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..444
FT /note="Transcriptional regulatory protein QseF"
FT /id="PRO_0000081378"
FT DOMAIN 7..121
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 136..366
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 414..433
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT BINDING 164..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 227..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 444 AA; 49148 MW; 6553C027DE5513EF CRC64;
MSHKPAHLLL VDDDPGLLKL LGLRLTSEGY SVVTAESGAE GLRVLNREKV DLVISDLRMD
EMDGMQLFAE IQKVQPGMPV IILTAHGSIP DAVAATQQGV FSFLTKPVDK DALYQAIDDA
LEQSAPATDE RWREAIVTRS PLMLRLLEQA RLVAQSDVSV LINGQSGTGK EIFAQAIHNA
SPRNSKPFIA INCGALPEQL LESELFGHAR GAFTGAVSNR EGLFQAAEGG TLFLDEIGDM
PAPLQVKLLR VLQERKVRPL GSNRDIDINV RIISATHRDL PKAMARGEFR EDLYYRLNVV
SLKIPALAER TEDIPLLANH LLRQAAERHK PFVRAFSTDA MKRLMTASWP GNVRQLVNVI
EQCVALTSSP VISDALVEQA LEGENTALPT FVEARNQFEL NYLRKLLQIT KGNVTHAARM
AGRNRTEFYK LLSRHELDAN DFKE
