ID LASR_PSEAE Reviewed; 239 AA. AC P25084; Q51475; Q51476; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 08-MAY-2019, entry version 148. DE RecName: Full=Transcriptional activator protein LasR; GN Name=lasR; OrderedLocusNames=PA1430; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / OS JCM 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 / RC 1C / PRS 101 / PAO1; RX PubMed=1902216; DOI=10.1128/jb.173.9.3000-3009.1991; RA Gambello M.J., Iglewski B.H.; RT "Cloning and characterization of the Pseudomonas aeruginosa lasR gene, RT a transcriptional activator of elastase expression."; RL J. Bacteriol. 173:3000-3009(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29260 / PA103, and NBRC 13130 / JCM 20134; RX PubMed=7937080; DOI=10.1093/nar/22.18.3706; RA Fukushima J., Ishiwata T., Kurata M., You Z., Okuda K.; RT "Intracellular receptor-type transcription factor, LasR, contains a RT highly conserved amphipathic region which precedes the putative helix- RT turn-helix DNA binding motif."; RL Nucleic Acids Res. 22:3706-3707(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / 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., RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). CC -!- FUNCTION: Transcriptional activator of elastase structural gene CC (LasB). Binds to the PAI autoinducer. CC -!- MISCELLANEOUS: LasR in strain PA103 is not active, this is CC probably due to the change in position 180 of the sequence. CC -!- SIMILARITY: Belongs to the autoinducer-regulated transcriptional CC regulatory protein family. {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; M59425; AAA25874.1; -; Genomic_DNA. DR EMBL; D30813; BAA06490.1; -; Genomic_DNA. DR EMBL; D30812; BAA06489.1; -; Genomic_DNA. DR EMBL; AE004091; AAG04819.1; -; Genomic_DNA. DR PIR; A43660; A43660. DR PIR; S53692; S53692. DR PIR; S53693; S53693. DR RefSeq; NP_250121.1; NC_002516.2. DR RefSeq; WP_003082999.1; NZ_QZGE01000005.1. DR PDB; 2UV0; X-ray; 1.80 A; E/F/G/H=1-173. DR PDB; 3IX3; X-ray; 1.40 A; A/B=1-173. DR PDB; 3IX4; X-ray; 1.80 A; A/B/C/D/E/F/G/H=1-173. DR PDB; 3IX8; X-ray; 1.80 A; A/B/C/D=1-173. DR PDB; 3JPU; X-ray; 2.30 A; A/B/C/D/E=1-173. DR PDB; 4NG2; X-ray; 2.41 A; A/B/C/D=1-170. DR PDB; 6D6A; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-170. DR PDB; 6D6B; X-ray; 1.70 A; A/B/C/D/E/F/G/H=1-170. DR PDB; 6D6C; X-ray; 1.88 A; A/B/C/D/E/F/G/H/I/J/K/L=1-170. DR PDB; 6D6D; X-ray; 1.70 A; A/B=1-169. DR PDB; 6D6L; X-ray; 1.63 A; A/B/C/D=1-170. DR PDB; 6D6M; X-ray; 1.90 A; A/B/C/D=1-170. DR PDB; 6D6N; X-ray; 1.81 A; A/B/C/D=1-170. DR PDB; 6D6O; X-ray; 1.65 A; A/B/C/D=1-170. DR PDB; 6D6P; X-ray; 1.65 A; A/B/C/D=1-170. DR PDBsum; 2UV0; -. DR PDBsum; 3IX3; -. DR PDBsum; 3IX4; -. DR PDBsum; 3IX8; -. DR PDBsum; 3JPU; -. DR PDBsum; 4NG2; -. DR PDBsum; 6D6A; -. DR PDBsum; 6D6B; -. DR PDBsum; 6D6C; -. DR PDBsum; 6D6D; -. DR PDBsum; 6D6L; -. DR PDBsum; 6D6M; -. DR PDBsum; 6D6N; -. DR PDBsum; 6D6O; -. DR PDBsum; 6D6P; -. DR SMR; P25084; -. DR BindingDB; P25084; -. DR ChEMBL; CHEMBL1075207; -. DR DrugBank; DB08324; N-3-OXO-DODECANOYL-L-HOMOSERINE LACTONE. DR PaxDb; P25084; -. DR PRIDE; P25084; -. DR DNASU; 881789; -. DR EnsemblBacteria; AAG04819; AAG04819; PA1430. DR GeneID; 881789; -. DR KEGG; pae:PA1430; -. DR PATRIC; fig|208964.12.peg.1480; -. DR PseudoCAP; PA1430; -. DR eggNOG; ENOG4105VJY; Bacteria. DR eggNOG; COG2771; LUCA. DR HOGENOM; HOG000111053; -. DR InParanoid; P25084; -. DR KO; K18304; -. DR OMA; AEGKTDW; -. DR PhylomeDB; P25084; -. DR BioCyc; PAER208964:G1FZ6-1456-MONOMER; -. DR EvolutionaryTrace; P25084; -. DR PRO; PR:P25084; -. DR Proteomes; UP000002438; Chromosome. DR CollecTF; EXPREG_000009b0; -. 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:0003700; F:DNA-binding transcription factor activity; IDA:PseudoCAP. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:CollecTF. DR GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:CollecTF. DR GO; GO:0009405; P:pathogenesis; IMP:PseudoCAP. DR GO; GO:0051544; P:positive regulation of elastin biosynthetic process; IMP:PseudoCAP. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:CACAO. DR GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW. DR GO; GO:0060310; P:regulation of elastin catabolic process; IMP:PseudoCAP. DR GO; GO:0010468; P:regulation of gene expression; IDA:CACAO. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:PseudoCAP. 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 3D-structure; Activator; Complete proteome; DNA-binding; KW Quorum sensing; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 239 Transcriptional activator protein LasR. FT /FTId=PRO_0000184160. FT DOMAIN 170 235 HTH luxR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00411}. FT DNA_BIND 194 213 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00411}. FT VARIANT 144 144 M -> I (in strain: IFO 3455 and PA103). FT VARIANT 180 180 R -> W (in strain: PA103). FT HELIX 8 12 {ECO:0000244|PDB:3IX3}. FT HELIX 15 29 {ECO:0000244|PDB:3IX3}. FT STRAND 33 40 {ECO:0000244|PDB:3IX3}. FT HELIX 47 49 {ECO:0000244|PDB:3IX3}. FT STRAND 50 54 {ECO:0000244|PDB:3IX3}. FT HELIX 58 66 {ECO:0000244|PDB:3IX3}. FT HELIX 69 71 {ECO:0000244|PDB:3IX3}. FT HELIX 74 81 {ECO:0000244|PDB:3IX3}. FT HELIX 90 92 {ECO:0000244|PDB:3IX3}. FT HELIX 96 107 {ECO:0000244|PDB:3IX3}. FT STRAND 112 119 {ECO:0000244|PDB:3IX3}. FT STRAND 125 131 {ECO:0000244|PDB:3IX3}. FT HELIX 137 145 {ECO:0000244|PDB:3IX3}. FT HELIX 148 167 {ECO:0000244|PDB:3IX3}. SQ SEQUENCE 239 AA; 26619 MW; 28B6E06E9187924A CRC64; MALVDGFLEL ERSSGKLEWS AILQKMASDL GFSKILFGLL PKDSQDYENA FIVGNYPAAW REHYDRAGYA RVDPTVSHCT QSVLPIFWEP SIYQTRKQHE FFEEASAAGL VYGLTMPLHG ARGELGALSL SVEAENRAEA NRFMESVLPT LWMLKDYALQ SGAGLAFEHP VSKPVVLTSR EKEVLQWCAI GKTSWEISVI CNCSEANVNF HMGNIRRKFG VTSRRVAAIM AVNLGLITL //