QSEE_ECO57
ID QSEE_ECO57 Reviewed; 475 AA.
AC Q8XA47; Q7ABK5;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Sensor histidine kinase QseE;
DE EC=2.7.13.3;
DE AltName: Full=Quorum-sensing regulator protein E;
GN Name=qseE; Synonyms=yfhK; OrderedLocusNames=Z3833, ECs3422;
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, AUTOPHOSPHORYLATION, AND SUBCELLULAR LOCATION.
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. Autophosphorylates in response to epinephrine, sulfate or
CC phosphate and then probably transfers its phosphate group to QseF.
CC {ECO:0000269|PubMed:17220220, ECO:0000269|PubMed:19289831,
CC ECO:0000269|PubMed:20056703}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:19289831}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:19289831}.
CC -!- INDUCTION: Induced by epinephrine during late exponential growth,
CC probably via the QseC sensor. {ECO:0000269|PubMed:17220220}.
CC -!- PTM: Autophosphorylated.
CC -!- DISRUPTION PHENOTYPE: Mutants can still form pedestals.
CC {ECO:0000269|PubMed:17220220}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG57670.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB36845.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AE005174; AAG57670.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB36845.1; ALT_INIT; Genomic_DNA.
DR PIR; B85901; B85901.
DR PIR; F91056; F91056.
DR RefSeq; NP_311449.1; NC_002695.1.
DR RefSeq; WP_001301750.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XA47; -.
DR SMR; Q8XA47; -.
DR STRING; 155864.EDL933_3721; -.
DR EnsemblBacteria; AAG57670; AAG57670; Z3833.
DR EnsemblBacteria; BAB36845; BAB36845; ECs_3422.
DR GeneID; 914903; -.
DR KEGG; ece:Z3833; -.
DR KEGG; ecs:ECs_3422; -.
DR PATRIC; fig|386585.9.peg.3576; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_23_6; -.
DR OMA; IAQDCIK; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..475
FT /note="Sensor histidine kinase QseE"
FT /id="PRO_0000413889"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..173
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 256..472
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 259
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 475 AA; 53293 MW; 1AB32C5772BBF180 CRC64;
MKRWPVFPRS LRQLVMLAFL LILLPLLVLA WQAWQSLNAL SDQAALVNRT TLIDARRSEA
MTNAALEMER SYRQYCVLDD PTLAKVYQSQ RKRYSEMLDA HAGVLPDDKL YQALRQDLNN
LAQLQCNNSG PDAAAAARLE AFASANTEMV QATRTVVFSR GQQLQREIAE RGQYFGWQSL
VLFLVSLVMV LLFTRMIIGP VKNIERMINR LGEGRSLGNS VSFSGPSELR SVGQRILWLS
ERLSWLESQR HQFLRHLSHE LKTPLASMRE GTELLADQVV GPLTPEQKEV VSILDSSSRN
LQKLIEQLLD YNRKQADSAV ELDNVELAPL VETVVSAHSL PARAKMMHTD VDLKATACLA
EPMLLMSVLD NLYSNAVHYG AESGNICLRS SLHGARVYID VINTGTPIPQ EERAMIFEPF
FQGSHQRKGA VKGSGLGLSI ARDCIRRMQG ELYLVDESGQ DVCFRIELPS SKNTK
