PTXR_PSEAE
ID PTXR_PSEAE Reviewed; 312 AA.
AC P72131; Q9R7G8;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=HTH-type transcriptional regulator PtxR {ECO:0000305};
DE AltName: Full=Pseudomonas exotoxin A regulator {ECO:0000303|PubMed:8843437};
GN Name=ptxR {ECO:0000303|PubMed:8843437}; OrderedLocusNames=PA2258;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8843437; DOI=10.1046/j.1365-2958.1996.6251337.x;
RA Hamood A.N., Colmer J.A., Ochsner U.A., Vasil M.L.;
RT "Isolation and characterization of a Pseudomonas aeruginosa gene, ptxR,
RT which positively regulates exotoxin A production.";
RL Mol. Microbiol. 21:97-110(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9852033; DOI=10.1128/jb.180.24.6784-6788.1998;
RA Vasil M.L., Ochsner U.A., Johnson Z., Colmer J.A., Hamood A.N.;
RT "The fur-regulated gene encoding the alternative sigma factor PvdS is
RT required for iron-dependent expression of the LysR-type regulator ptxR in
RT Pseudomonas aeruginosa.";
RL J. Bacteriol. 180:6784-6788(1998).
RN [4]
RP ACTIVITY REGULATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1, and PA103;
RX PubMed=9645431; DOI=10.1007/s004380050729;
RA Colmer J.A., Hamood A.N.;
RT "Characterization of ptxS, a Pseudomonas aeruginosa gene which interferes
RT with the effect of the exotoxin A positive regulatory gene, ptxR.";
RL Mol. Gen. Genet. 258:250-259(1998).
RN [5]
RP FUNCTION.
RX PubMed=10696480; DOI=10.1139/w99-103;
RA Colmer J.A., Hamood A.N.;
RT "Expression of ptxR and its effect on toxA and regA expression during the
RT growth cycle of Pseudomonas aeruginosa strain PAO1.";
RL Can. J. Microbiol. 45:1008-1016(1999).
RN [6]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=16000716; DOI=10.1099/mic.0.27754-0;
RA Gaines J.M., Carty N.L., Colmer-Hamood J.A., Hamood A.N.;
RT "Effect of static growth and different levels of environmental oxygen on
RT toxA and ptxR expression in the Pseudomonas aeruginosa strain PAO1.";
RL Microbiology 151:2263-2275(2005).
RN [7]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=16699585; DOI=10.1139/w05-138;
RA Colmer-Hamood J.A., Aramaki H., Gaines J.M., Hamood A.N.;
RT "Transcriptional analysis of the Pseudomonas aeruginosa toxA regulatory
RT gene ptxR.";
RL Can. J. Microbiol. 52:343-356(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16803594; DOI=10.1111/j.1365-2958.2006.05269.x;
RA Carty N.L., Layland N., Colmer-Hamood J.A., Calfee M.W., Pesci E.C.,
RA Hamood A.N.;
RT "PtxR modulates the expression of QS-controlled virulence factors in the
RT Pseudomonas aeruginosa strain PAO1.";
RL Mol. Microbiol. 61:782-794(2006).
RN [9]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=18048935; DOI=10.1099/mic.0.2007/011338-0;
RA Gaines J.M., Carty N.L., Tiburzi F., Davinic M., Visca P.,
RA Colmer-Hamood J.A., Hamood A.N.;
RT "Regulation of the Pseudomonas aeruginosa toxA, regA and ptxR genes by the
RT iron-starvation sigma factor PvdS under reduced levels of oxygen.";
RL Microbiology 153:4219-4233(2007).
RN [10]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=18227247; DOI=10.1099/mic.0.2007/011577-0;
RA Ferrell E., Carty N.L., Colmer-Hamood J.A., Hamood A.N., West S.E.H.;
RT "Regulation of Pseudomonas aeruginosa ptxR by Vfr.";
RL Microbiology 154:431-439(2008).
RN [11]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH PTXS, AND MUTAGENESIS OF
RP LYS-39; SER-40; GLU-44; ARG-47 AND ASP-52.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=22844393; DOI=10.1371/journal.pone.0039390;
RA Daddaoua A., Fillet S., Fernandez M., Udaondo Z., Krell T., Ramos J.L.;
RT "Genes for carbon metabolism and the ToxA virulence factor in Pseudomonas
RT aeruginosa are regulated through molecular interactions of PtxR and PtxS.";
RL PLoS ONE 7:e39390-e39390(2012).
RN [12]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, INTERACTION WITH PTXS, AND
RP MUTAGENESIS OF VAL-173 AND TRP-269.
RX PubMed=24019239; DOI=10.1093/nar/gkt773;
RA Daddaoua A., Krell T., Ramos J.L.;
RT "Transcriptional control by two interacting regulatory proteins:
RT identification of the PtxS binding site at PtxR.";
RL Nucleic Acids Res. 41:10150-10156(2013).
CC -!- FUNCTION: Plays an important role in the regulation of the production
CC of the virulence factor exotoxin A (toxA), via positive regulation of
CC the transcription of the toxA gene (PubMed:8843437, PubMed:10696480,
CC PubMed:22844393). Acts by binding directly to the toxA promoter region
CC (PubMed:22844393). Besides toxA, PtxR modulates the expression of genes
CC that code for the QS-controlled virulence factors (PubMed:16803594). It
CC negatively regulates the expression of the rhamnolipid and pyocyanine
CC genes, through the autoinducer synthase RhlI, and the PQS synthesis
CC operon pqsABCDE, while it positively regulates the expression of lasB
CC through the autoinducer synthase LasI (PubMed:16803594). Also
CC positively regulates the expression of the exotoxin A regulatory
CC protein (toxR or regA) (PubMed:8843437, PubMed:10696480).
CC {ECO:0000269|PubMed:10696480, ECO:0000269|PubMed:16803594,
CC ECO:0000269|PubMed:22844393, ECO:0000269|PubMed:8843437}.
CC -!- FUNCTION: In addition, is involved in the positive regulation of
CC glucose metabolism via the regulation of the expression of the kgu and
CC gad operons (PubMed:22844393, PubMed:24019239). Acts by binding
CC directly to the promoter region of the kgu and gad operons
CC (PubMed:22844393, PubMed:24019239). {ECO:0000269|PubMed:22844393,
CC ECO:0000269|PubMed:24019239}.
CC -!- ACTIVITY REGULATION: Negatively regulated by PtxS, which interacts with
CC PtxR and prevents its activity. {ECO:0000269|PubMed:22844393,
CC ECO:0000269|PubMed:24019239, ECO:0000269|PubMed:9645431}.
CC -!- SUBUNIT: Monomer in solution (PubMed:24019239). May dimerize on binding
CC to DNA (PubMed:24019239). Interacts with PtxS in the absence of 2-
CC ketogluconate (PubMed:22844393, PubMed:24019239). Binding of the 2-
CC ketogluconate effector to PtxS causes PtxS/PtxR complex dissociation
CC (PubMed:22844393, PubMed:24019239). {ECO:0000269|PubMed:22844393,
CC ECO:0000269|PubMed:24019239}.
CC -!- INDUCTION: The level of expression at different time points of growth
CC is generally low (PubMed:16000716, PubMed:16699585). Expression
CC increases when P.aeruginosa is grown in static cultures and under
CC reduced levels of environmental oxygen, two conditions that resemble
CC the environment within the lung alveoli of cystic fibrosis patients
CC (PubMed:16000716). The ptxR upstream region contains two independent
CC transcription initiation sites (T1 and T2), and potential binding sites
CC for multiple regulators (PubMed:9852033, PubMed:16699585,
CC PubMed:18048935, PubMed:18227247). Under aerobic conditions in iron-
CC deficient medium, ptxR expression follows a biphasic curve that
CC involves the P1 promoter only (PubMed:16699585). Iron eliminates the
CC second peak of expression but does not affect expression from the P2
CC promoter (PubMed:16699585). Under microaerobic conditions, iron
CC represses expression from subclones that carry P1 alone or P2 alone at
CC both early and late stages of growth (PubMed:16699585). Under anaerobic
CC conditions, expression increases considerably (PubMed:16699585). P1 is
CC recognized by sigma-70 (PubMed:16699585). Regulated by the iron-
CC starvation sigma factor PvdS under reduced levels of oxygen
CC (PubMed:18048935). Vfr may be required for P2 expression throughout the
CC growth cycle in iron-deficient medium (PubMed:18227247).
CC {ECO:0000269|PubMed:16000716, ECO:0000269|PubMed:16699585,
CC ECO:0000269|PubMed:18048935, ECO:0000269|PubMed:18227247,
CC ECO:0000269|PubMed:9852033}.
CC -!- DISRUPTION PHENOTYPE: Mutant produces lower levels of exotoxin A
CC (PubMed:8843437). Mutant also produces significantly more pyocyanine
CC than its parent strain (PubMed:16803594). {ECO:0000269|PubMed:16803594,
CC ECO:0000269|PubMed:8843437}.
CC -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; AF012100; AAC26481.3; -; Genomic_DNA.
DR EMBL; AE004091; AAG05646.1; -; Genomic_DNA.
DR PIR; S77670; S77670.
DR RefSeq; NP_250948.1; NC_002516.2.
DR RefSeq; WP_003089264.1; NZ_QZGE01000014.1.
DR AlphaFoldDB; P72131; -.
DR SMR; P72131; -.
DR STRING; 287.DR97_6175; -.
DR PaxDb; P72131; -.
DR PRIDE; P72131; -.
DR EnsemblBacteria; AAG05646; AAG05646; PA2258.
DR GeneID; 878030; -.
DR KEGG; pae:PA2258; -.
DR PATRIC; fig|208964.12.peg.2360; -.
DR PseudoCAP; PA2258; -.
DR HOGENOM; CLU_039613_16_2_6; -.
DR InParanoid; P72131; -.
DR OMA; FIAVVEH; -.
DR PhylomeDB; P72131; -.
DR BioCyc; PAER208964:G1FZ6-2297-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR CollecTF; EXPREG_00000bd0; -.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IPI:CollecTF.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IMP:PseudoCAP.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR GO; GO:1900377; P:negative regulation of secondary metabolite biosynthetic process; IMP:PseudoCAP.
DR GO; GO:0045862; P:positive regulation of proteolysis; IMP:PseudoCAP.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:PseudoCAP.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005119; LysR_subst-bd.
DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00126; HTH_1; 1.
DR Pfam; PF03466; LysR_substrate; 1.
DR PRINTS; PR00039; HTHLYSR.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50931; HTH_LYSR; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..312
FT /note="HTH-type transcriptional regulator PtxR"
FT /id="PRO_0000105746"
FT DOMAIN 11..68
FT /note="HTH lysR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT DNA_BIND 28..47
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT MUTAGEN 39
FT /note="K->A: Does not bind DNA."
FT /evidence="ECO:0000269|PubMed:22844393"
FT MUTAGEN 40
FT /note="S->A: Does not bind DNA."
FT /evidence="ECO:0000269|PubMed:22844393"
FT MUTAGEN 44
FT /note="E->A: Does not bind DNA."
FT /evidence="ECO:0000269|PubMed:22844393"
FT MUTAGEN 47
FT /note="R->A: Binds DNA with an affinity reduced by a factor
FT of 2."
FT /evidence="ECO:0000269|PubMed:22844393"
FT MUTAGEN 52
FT /note="D->A: Does not bind DNA."
FT /evidence="ECO:0000269|PubMed:22844393"
FT MUTAGEN 173
FT /note="V->A: Abolishes interaction with PtxS but does not
FT alter DNA binding."
FT /evidence="ECO:0000269|PubMed:24019239"
FT MUTAGEN 269
FT /note="W->A: Abolishes interaction with PtxS but does not
FT alter DNA binding."
FT /evidence="ECO:0000269|PubMed:24019239"
SQ SEQUENCE 312 AA; 34992 MW; EF6511EDCC2F6BBA CRC64;
MSAALERLNH LNLNHLYAFV AVAEHNSFTA AAEALGLSKS LLSEQLRRLE ADLGIQLLTR
TTRRMTLTDR GELLFGVAQR MLGELDGALS DVRDLQGEPS GRLRITAPQD FVKWHISSVS
AAFIRQFPKV QVEMLADDQF SDLVGQRIDL AVRIGWPRDS GLHASKLCDF QQVAVATPGY
LAGLPPVLQP HDLARCEWIG HTRLSTPWTW TFERQRERAT VQTRGRLLAN NTLAVYRLVL
DGAGVSVLPS FLVAREIARG RLVRLLPGWR LPQGGIYALY PSARYMPVRV RAFIESLREH
LGREPFRLAQ SE
