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Database: UniProt
Entry: P54292
LinkDB: P54292
Original site: P54292 
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   26-FEB-2020, entry version 124.
DE   RecName: Full=Regulatory protein RhlR;
DE   AltName: Full=Elastase modulator;
GN   Name=rhlR; Synonyms=lasM, vsmR; 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].
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].
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].
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;
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.
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).
CC   -!- FUNCTION: Necessary for transcriptional activation of the rhlAB genes
CC       encoding the rhamnosyltransferase. It also functions as a
CC       transcriptional activator of elastase structural gene (lasB). Binds to
CC       autoinducer molecules BHL (N-butanoyl-L-homoserine lactone), and HHL
CC       (N-hexanoyl-L-homoserine lactone).
CC   -!- SIMILARITY: Belongs to the autoinducer-regulated transcriptional
CC       regulatory protein family. {ECO:0000305}.
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   SMR; 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   eggNOG; ENOG4105VJY; Bacteria.
DR   eggNOG; COG2771; LUCA.
DR   HOGENOM; CLU_072786_7_1_6; -.
DR   InParanoid; P54292; -.
DR   KO; K18099; -.
DR   OMA; NHTVDWY; -.
DR   PhylomeDB; P54292; -.
DR   BioCyc; PAER208964:G1FZ6-3545-MONOMER; -.
DR   Proteomes; UP000002438; Chromosome.
DR   CollecTF; EXPREG_00000b10; -.
DR   GO; GO:0032993; C:protein-DNA complex; IDA:CollecTF.
DR   GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:CollecTF.
DR   GO; GO:0001217; F:DNA-binding transcription repressor activity; IDA:CollecTF.
DR   GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA: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: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   3: Inferred from homology;
KW   Activator; DNA-binding; Quorum sensing; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..241
FT                   /note="Regulatory protein 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
//
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