PTXS_PSEAE
ID PTXS_PSEAE Reviewed; 340 AA.
AC G3XD97;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=HTH-type transcriptional regulator PtxS {ECO:0000305};
GN Name=ptxS {ECO:0000303|PubMed:9645431};
GN OrderedLocusNames=PA2259 {ECO:0000312|EMBL:AAG05647.1};
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, 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 [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 FUNCTION, AND TRANSCRIPTIONAL REGULATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10438759; DOI=10.1128/jb.181.16.4890-4895.1999;
RA Swanson B.L., Colmer J.A., Hamood A.N.;
RT "The Pseudomonas aeruginosa exotoxin A regulatory gene, ptxS: evidence for
RT negative autoregulation.";
RL J. Bacteriol. 181:4890-4895(1999).
RN [4]
RP FUNCTION, AND TRANSCRIPTIONAL REGULATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10894751; DOI=10.1128/jb.182.15.4366-4371.2000;
RA Swanson B.L., Hamood A.N.;
RT "Autoregulation of the Pseudomonas aeruginosa protein PtxS occurs through a
RT specific operator site within the ptxS upstream region.";
RL J. Bacteriol. 182:4366-4371(2000).
RN [5]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10931350; DOI=10.1046/j.1365-2958.2000.02012.x;
RA Swanson B.L., Hager P., Phibbs P. Jr., Ochsner U., Vasil M.L., Hamood A.N.;
RT "Characterization of the 2-ketogluconate utilization operon in Pseudomonas
RT aeruginosa PAO1.";
RL Mol. Microbiol. 37:561-573(2000).
RN [6]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=15528665; DOI=10.1099/mic.0.27270-0;
RA Westfall L.W., Luna A.M., Francisco M.S., Diggle S.P., Worrall K.E.,
RA Williams P., Camara M., Hamood A.N.;
RT "The Pseudomonas aeruginosa global regulator MvaT specifically binds to the
RT ptxS upstream region and enhances ptxS expression.";
RL Microbiology 150:3797-3806(2004).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH PTXR, AND TRANSCRIPTIONAL
RP REGULATION.
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 [8]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH PTXR.
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: Negatively regulates glucose metabolism by binding directly
CC to the promoter region of the kgu and gad operons (PubMed:22844393,
CC PubMed:24019239). It also negatively regulates its own synthesis
CC (PubMed:10438759, PubMed:10894751, PubMed:22844393).
CC {ECO:0000269|PubMed:10438759, ECO:0000269|PubMed:10894751,
CC ECO:0000269|PubMed:22844393, ECO:0000269|PubMed:24019239}.
CC -!- FUNCTION: In addition, in pathogenic strains, PtxS modulates PtxR
CC activity in response to 2-ketogluconate (PubMed:9645431,
CC PubMed:22844393, PubMed:24019239). In the presence of PtxR, which also
CC binds to the kgu and gad promoter regions, PtxS and PtxR form a tight
CC complex, creating a DNA-loop that prevents RNA polymerase promoter
CC access and expression of the glucose metabolism genes (PubMed:10931350,
CC PubMed:22844393, PubMed:24019239). Binding of the 2-ketogluconate
CC effector to PtxS causes PtxS/PtxR complex dissociation and leads to the
CC dissolution of the repression DNA-loop, facilitating the entry of the
CC RNA polymerase and enabling the transcription of the genes
CC (PubMed:22844393, PubMed:24019239). Also plays an important role in the
CC regulation of the expression of the virulence factor exotoxin A (toxA)
CC (PubMed:9645431, PubMed:22844393). PtxS does not bind directly to the
CC toxA promoter but negatively regulates the production of exotoxin A by
CC binding to PtxR and interfering with its positive regulator activity
CC (PubMed:9645431, PubMed:22844393). In the presence of 2-ketogluconate,
CC PtxS is released and PtxR can recruit RNA polymerase (PubMed:22844393).
CC {ECO:0000269|PubMed:10931350, ECO:0000269|PubMed:22844393,
CC ECO:0000269|PubMed:24019239, ECO:0000269|PubMed:9645431}.
CC -!- ACTIVITY REGULATION: 2-ketogluconate acts as a molecular effector and
CC causes dissociation of the PtxS/PtxR complex.
CC {ECO:0000269|PubMed:10931350, ECO:0000269|PubMed:22844393,
CC ECO:0000269|PubMed:24019239}.
CC -!- SUBUNIT: Interacts with PtxR in the absence of 2-ketogluconate
CC (PubMed:22844393, PubMed:24019239). Binding of the 2-ketogluconate
CC effector to PtxS causes PtxS/PtxR complex dissociation
CC (PubMed:22844393, PubMed:24019239). {ECO:0000269|PubMed:22844393,
CC ECO:0000269|PubMed:24019239}.
CC -!- INDUCTION: Expression is enhanced by the global regulator MvaT, which
CC binds to the ptxR-ptxS intergenic region (PubMed:15528665). Negatively
CC autoregulates its own synthesis by binding to a specific operator site
CC within the ptxS upstream region (PubMed:10438759, PubMed:10894751,
CC PubMed:22844393). {ECO:0000269|PubMed:10438759,
CC ECO:0000269|PubMed:10894751, ECO:0000269|PubMed:15528665,
CC ECO:0000269|PubMed:22844393}.
CC -!- DOMAIN: Contains an N-terminal helix-turn-helix DNA-binding domain and
CC a C-terminal domain that binds the effector. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mutant exhibits a twofold increase in exotoxin A
CC production. {ECO:0000269|PubMed:9645431}.
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DR EMBL; AE004091; AAG05647.1; -; Genomic_DNA.
DR PIR; E83364; E83364.
DR RefSeq; NP_250949.1; NC_002516.2.
DR RefSeq; WP_003113738.1; NZ_QZGE01000014.1.
DR SMR; G3XD97; -.
DR STRING; 287.DR97_6174; -.
DR PaxDb; G3XD97; -.
DR PRIDE; G3XD97; -.
DR EnsemblBacteria; AAG05647; AAG05647; PA2259.
DR GeneID; 877811; -.
DR KEGG; pae:PA2259; -.
DR PATRIC; fig|208964.12.peg.2361; -.
DR PseudoCAP; PA2259; -.
DR HOGENOM; CLU_037628_6_0_6; -.
DR InParanoid; G3XD97; -.
DR OMA; MHGVETA; -.
DR PhylomeDB; G3XD97; -.
DR Proteomes; UP000002438; Chromosome.
DR CollecTF; EXPREG_00000500; -.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:CollecTF.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:PseudoCAP.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd01392; HTH_LacI; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR000843; HTH_LacI.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR001761; Peripla_BP/Lac1_sug-bd_dom.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00356; LacI; 1.
DR Pfam; PF00532; Peripla_BP_1; 1.
DR SMART; SM00354; HTH_LACI; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS50932; HTH_LACI_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..340
FT /note="HTH-type transcriptional regulator PtxS"
FT /id="PRO_0000456054"
FT DOMAIN 12..67
FT /note="HTH lacI-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT DNA_BIND 14..33
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
SQ SEQUENCE 340 AA; 37391 MW; F977BD13FCF35EF4 CRC64;
MNGSVLPSRG RVTINQVAEA AGVSKASVSR YIGGDRQLLA DATARRIERA IDQLDYRPNQ
MARGLKRGRT RLIGMLVADI LNPYSVAVMH GVETACREHG YSLVVCNTDR DDEQERHHLA
ALQSYNVEGL IVNTLGHHPG ELRALHRELP MVLVDRQLAE LDTDLVGLDN ADAVEQALDH
LQHRGFRDIL LVTEPLDGTS SRIERVQAFN ASIGRRPALK GQVLQTDDFF RDGLRAFLSA
SGPGPKALFT CNGVATLCAT RQLRDLGCRL FDEVGLLALD ELDWYPLVGS GITALAQPTD
EIGRTAFERL LARLEGDREP ARRVTFPAQL IVRGSTHPRG
