RHLR_PSEAE
ID RHLR_PSEAE Reviewed; 241 AA.
AC P54292; Q9HYD2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=HTH-type quorum-sensing regulator RhlR {ECO:0000305};
DE AltName: Full=Elastase modulator {ECO:0000303|PubMed:8522523};
DE AltName: Full=Regulatory protein RhlR;
GN Name=rhlR {ECO:0000303|PubMed:8144472};
GN Synonyms=lasM {ECO:0000303|PubMed:8522523},
GN vsmR {ECO:0000303|PubMed:7494482}; OrderedLocusNames=PA3477;
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=8522523; DOI=10.1128/jb.177.24.7155-7163.1995;
RA Brint J.M., Ohman D.E.;
RT "Synthesis of multiple exoproducts in Pseudomonas aeruginosa is under the
RT control of RhlR-RhlI, another set of regulators in strain PAO1 with
RT homology to the autoinducer-responsive LuxR-LuxI family.";
RL J. Bacteriol. 177:7155-7163(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 2659 / PG201;
RX PubMed=8144472; DOI=10.1128/jb.176.7.2044-2054.1994;
RA Ochsner U.A., Koch A.K., Fiechter A., Reiser J.;
RT "Isolation and characterization of a regulatory gene affecting rhamnolipid
RT biosurfactant synthesis in Pseudomonas aeruginosa.";
RL J. Bacteriol. 176:2044-2054(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN QUORUM SENSING.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=7494482; DOI=10.1111/j.1365-2958.1995.mmi_17020333.x;
RA Latifi A., Winson M.K., Foglino M., Bycroft B.W., Stewart G.S.A.B.,
RA Lazdunski A., Williams P.;
RT "Multiple homologues of LuxR and LuxI control expression of virulence
RT determinants and secondary metabolites through quorum sensing in
RT Pseudomonas aeruginosa PAO1.";
RL Mol. Microbiol. 17:333-343(1995).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RC STRAIN=DSM 2659 / PG201;
RX PubMed=8051059; DOI=10.1016/s0021-9258(17)32089-6;
RA Ochsner U.A., Fiechter A., Reiser J.;
RT "Isolation, characterization, and expression in Escherichia coli of the
RT Pseudomonas aeruginosa rhlAB genes encoding a rhamnosyltransferase involved
RT in rhamnolipid biosurfactant synthesis.";
RL J. Biol. Chem. 269:19787-19795(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 232-241, FUNCTION, ACTIVITY
RP REGULATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 2659 / PG201;
RX PubMed=7604006; DOI=10.1073/pnas.92.14.6424;
RA Ochsner U.A., Reiser J.;
RT "Autoinducer-mediated regulation of rhamnolipid biosurfactant synthesis in
RT Pseudomonas aeruginosa.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:6424-6428(1995).
RN [7]
RP FUNCTION, DNA-BINDING, AND ACTIVITY REGULATION.
RX PubMed=14526008; DOI=10.1128/jb.185.20.5976-5983.2003;
RA Medina G., Juarez K., Valderrama B., Soberon-Chavez G.;
RT "Mechanism of Pseudomonas aeruginosa RhlR transcriptional regulation of the
RT rhlAB promoter.";
RL J. Bacteriol. 185:5976-5983(2003).
RN [8]
RP TRANSCRIPTIONAL REGULATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=14600219; DOI=10.1099/mic.0.26282-0;
RA Medina G., Juarez K., Diaz R., Soberon-Chavez G.;
RT "Transcriptional regulation of Pseudomonas aeruginosa rhlR, encoding a
RT quorum-sensing regulatory protein.";
RL Microbiology 149:3073-3081(2003).
RN [9]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=12657054; DOI=10.1046/j.1365-2958.2003.03422.x;
RA Ventre I., Ledgham F., Prima V., Lazdunski A., Foglino M., Sturgis J.N.;
RT "Dimerization of the quorum sensing regulator RhlR: development of a method
RT using EGFP fluorescence anisotropy.";
RL Mol. Microbiol. 48:187-198(2003).
RN [10]
RP FUNCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=15576196; DOI=10.1016/j.vaccine.2004.08.011;
RA Wagner V.E., Gillis R.J., Iglewski B.H.;
RT "Transcriptome analysis of quorum-sensing regulation and virulence factor
RT expression in Pseudomonas aeruginosa.";
RL Vaccine 22:S15-S20(2004).
RN [11]
RP FUNCTION, AND DNA-BINDING.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=22262098; DOI=10.1099/mic.0.054726-0;
RA Aguirre-Ramirez M., Medina G., Gonzalez-Valdez A., Grosso-Becerra V.,
RA Soberon-Chavez G.;
RT "The Pseudomonas aeruginosa rmlBDAC operon, encoding dTDP-L-rhamnose
RT biosynthetic enzymes, is regulated by the quorum-sensing transcriptional
RT regulator RhlR and the alternative sigma factor sigmaS.";
RL Microbiology 158:908-916(2012).
RN [12]
RP ACTIVITY REGULATION, AND INTERACTION WITH ROSMARINIC ACID.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=26732761; DOI=10.1126/scisignal.aaa8271;
RA Corral-Lugo A., Daddaoua A., Ortega A., Espinosa-Urgel M., Krell T.;
RT "Rosmarinic acid is a homoserine lactone mimic produced by plants that
RT activates a bacterial quorum-sensing regulator.";
RL Sci. Signal. 9:ra1-ra1(2016).
RN [13]
RP ACTIVITY REGULATION, AND INTERACTION WITH ROSMARINIC ACID.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=30051572; DOI=10.1111/1462-2920.14301;
RA Fernandez M., Corral-Lugo A., Krell T.;
RT "The plant compound rosmarinic acid induces a broad quorum sensing response
RT in Pseudomonas aeruginosa PAO1.";
RL Environ. Microbiol. 20:4230-4244(2018).
CC -!- FUNCTION: Quorum-sensing regulator that controls the expression of
CC multiple virulence factors in response to extracellular signaling
CC molecules called autoinducers (PubMed:7494482, PubMed:8522523,
CC PubMed:15576196). Involved, among others, in the transcriptional
CC regulation of genes that are responsible for rhamnolipid surfactant
CC biosynthesis (PubMed:8144472, PubMed:7604006, PubMed:14526008). Acts by
CC binding to a specific sequence in the rhlAB regulatory region, both in
CC the presence and in the absence of its autoinducer (PubMed:14526008).
CC In the former case it activates transcription of the promoter, whereas
CC in the latter it acts as a transcriptional repressor (PubMed:14526008).
CC Also regulates the expression of the rmlBDAC operon, encoding dTDP-L-
CC rhamnose biosynthetic enzymes, by binding to the rml box in the
CC promoter region (PubMed:22262098). In addition, is involved in the
CC regulation of the production of elastase (lasB) and pyocyanine
CC (PubMed:8144472, PubMed:7604006, PubMed:8522523).
CC {ECO:0000269|PubMed:14526008, ECO:0000269|PubMed:15576196,
CC ECO:0000269|PubMed:22262098, ECO:0000269|PubMed:7494482,
CC ECO:0000269|PubMed:7604006, ECO:0000269|PubMed:8144472,
CC ECO:0000269|PubMed:8522523}.
CC -!- ACTIVITY REGULATION: Activated by interaction with the autoinducer
CC signal molecule N-butanoyl-L-homoserine lactone (C4-HSL or BHL), the
CC product of the RhlI synthase (PubMed:7604006, PubMed:14526008,
CC PubMed:26732761). Is also activated by binding to rosmarinic acid (RA),
CC a homoserine lactone mimic produced by plants, which induces a broad
CC quorum sensing response, including the induction of all major quorum
CC sensing controlled virulence factors. Rosmarinic acid secretion may be
CC a plant defense mechanism to stimulate a premature quorum sensing
CC response (PubMed:26732761, PubMed:30051572).
CC {ECO:0000269|PubMed:14526008, ECO:0000269|PubMed:26732761,
CC ECO:0000269|PubMed:30051572, ECO:0000269|PubMed:7604006}.
CC -!- SUBUNIT: Homodimer in the absence of any acyl-L-homoserine lactone
CC (PubMed:12657054). The presence of the autoinducer C4-HSL has no
CC significant effect on dimerization whereas N-(3-oxododecanoyl)-L-
CC homoserine lactone (3O-C12-HSL), the LasR inducer, is able to
CC dissociate the RhlR homodimers into monomers (PubMed:12657054).
CC {ECO:0000269|PubMed:12657054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12657054}.
CC -!- INDUCTION: The rhlR promoter region contains four different
CC transcription start sites, two of which are included in the upstream
CC gene (rhlB) coding region. The rhlR gene is subject to a complex
CC transcriptional regulation. Expression is dependent on LasR and on
CC different regulatory proteins such as Vfr and RhlR itself, and also on
CC the alternative sigma factor sigma(54). Expression is partially LasR-
CC independent under certain culture conditions and is strongly influenced
CC by environmental factors. {ECO:0000269|PubMed:14600219}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant shows defects in the production
CC of rhamnolipids, elastase and pyocyanine (PubMed:8144472,
CC PubMed:7604006, PubMed:8522523). It also exhibits reduced LasA protease
CC activity and casein-degrading activity (PubMed:8522523).
CC {ECO:0000269|PubMed:7604006, ECO:0000269|PubMed:8144472,
CC ECO:0000269|PubMed:8522523}.
CC -!- SIMILARITY: Belongs to the autoinducer-regulated transcriptional
CC regulatory protein family. {ECO:0000305}.
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DR EMBL; U40458; AAC44036.1; -; Genomic_DNA.
DR EMBL; L08962; AAA25983.1; -; Genomic_DNA.
DR EMBL; U15644; AAA89073.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06865.1; -; Genomic_DNA.
DR EMBL; L28170; AAA62130.1; -; Genomic_DNA.
DR PIR; B83212; B83212.
DR PIR; C53652; C53652.
DR PIR; S70174; S70174.
DR RefSeq; NP_252167.1; NC_002516.2.
DR RefSeq; WP_003119559.1; NZ_QZGE01000039.1.
DR AlphaFoldDB; P54292; -.
DR SMR; P54292; -.
DR STRING; 287.DR97_4444; -.
DR BindingDB; P54292; -.
DR ChEMBL; CHEMBL3112386; -.
DR PaxDb; P54292; -.
DR PRIDE; P54292; -.
DR EnsemblBacteria; AAG06865; AAG06865; PA3477.
DR GeneID; 878968; -.
DR KEGG; pae:PA3477; -.
DR PATRIC; fig|208964.12.peg.3640; -.
DR PseudoCAP; PA3477; -.
DR HOGENOM; CLU_072786_7_1_6; -.
DR InParanoid; P54292; -.
DR OMA; NHTVDWY; -.
DR PhylomeDB; P54292; -.
DR BioCyc; PAER208964:G1FZ6-3545-MON; -.
DR PHI-base; PHI:6748; -.
DR PHI-base; PHI:6996; -.
DR PHI-base; PHI:7656; -.
DR PHI-base; PHI:8547; -.
DR PHI-base; PHI:8822; -.
DR Proteomes; UP000002438; Chromosome.
DR CollecTF; EXPREG_00000b10; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IMP:CollecTF.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:PHI-base.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IMP:CollecTF.
DR GO; GO:0038023; F:signaling receptor activity; TAS:PHI-base.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:0010467; P:gene expression; IMP:CACAO.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IMP:PseudoCAP.
DR GO; GO:0045862; P:positive regulation of proteolysis; IMP:PseudoCAP.
DR GO; GO:0062162; P:positive regulation of pyocyanine biosynthetic process; IMP:PHI-base.
DR GO; GO:1900378; P:positive regulation of secondary metabolite biosynthetic process; IMP:PseudoCAP.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEP:CollecTF.
DR GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW.
DR CDD; cd06170; LuxR_C_like; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.450.80; -; 1.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR005143; TF_LuxR_autoind-bd_dom.
DR InterPro; IPR036693; TF_LuxR_autoind-bd_dom_sf.
DR InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF03472; Autoind_bind; 1.
DR Pfam; PF00196; GerE; 1.
DR PRINTS; PR00038; HTHLUXR.
DR SMART; SM00421; HTH_LUXR; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF75516; SSF75516; 1.
DR PROSITE; PS00622; HTH_LUXR_1; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Quorum sensing; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..241
FT /note="HTH-type quorum-sensing regulator RhlR"
FT /id="PRO_0000184186"
FT DOMAIN 174..239
FT /note="HTH luxR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT DNA_BIND 198..217
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT CONFLICT 12
FT /note="D -> H (in Ref. 3; AAA89073)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="S -> C (in Ref. 3; AAA89073)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="S -> R (in Ref. 3; AAA89073)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 241 AA; 27578 MW; 70C0AEA8C1DE0D4B CRC64;
MRNDGGFLLW WDGLRSEMQP IHDSQGVFAV LEKEVRRLGF DYYAYGVRHT IPFTRPKTEV
HGTYPKAWLE RYQMQNYGAV DPAILNGLRS SEMVVWSDSL FDQSRMLWNE ARDWGLCVGA
TLPIRAPNNL LSVLSVARDQ QNISSFEREE IRLRLRCMIE LLTQKLTDLE HPMLMSNPVC
LSHREREILQ WTADGKSSGE IAIILSISES TVNFHHKNIQ KKFDAPNKTL AAAYAAALGL
I
