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Database: UniProt
Entry: Q9HWA4
LinkDB: Q9HWA4
Original site: Q9HWA4 
ID   PPRB_PSEAE              Reviewed;         275 AA.
AC   Q9HWA4;
DT   13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   13-NOV-2019, entry version 129.
DE   RecName: Full=Two-component response regulator PprB {ECO:0000303|PubMed:12499175};
GN   Name=pprB {ECO:0000303|PubMed:12499175}; OrderedLocusNames=PA4296;
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 [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).
RN   [2]
RP   FUNCTION, AND PHOSPHORYLATION.
RC   STRAIN=PAK;
RX   PubMed=12499175; DOI=10.1128/aac.47.1.95-101.2003;
RA   Wang Y., Ha U., Zeng L., Jin S.;
RT   "Regulation of membrane permeability by a two-component regulatory
RT   system in Pseudomonas aeruginosa.";
RL   Antimicrob. Agents Chemother. 47:95-101(2003).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15882421; DOI=10.1111/j.1365-2958.2005.04612.x;
RA   Dong Y.H., Zhang X.F., Soo H.M., Greenberg E.P., Zhang L.H.;
RT   "The two-component response regulator PprB modulates quorum-sensing
RT   signal production and global gene expression in Pseudomonas
RT   aeruginosa.";
RL   Mol. Microbiol. 56:1287-1301(2005).
RN   [4]
RP   FUNCTION.
RX   PubMed=19151143; DOI=10.1128/jb.01330-08;
RA   Bernard C.S., Bordi C., Termine E., Filloux A., de Bentzmann S.;
RT   "Organization and PprB-dependent control of the Pseudomonas aeruginosa
RT   tad Locus, involved in Flp pilus biology.";
RL   J. Bacteriol. 191:1961-1973(2009).
RN   [5]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=21091863; DOI=10.1111/j.1462-2920.2010.02372.x;
RA   Giraud C., Bernard C.S., Calderon V., Yang L., Filloux A., Molin S.,
RA   Fichant G., Bordi C., de Bentzmann S.;
RT   "The PprA-PprB two-component system activates CupE, the first non-
RT   archetypal Pseudomonas aeruginosa chaperone-usher pathway system
RT   assembling fimbriae.";
RL   Environ. Microbiol. 13:666-683(2011).
RN   [6]
RP   FUNCTION.
RX   PubMed=23209420; DOI=10.1371/journal.ppat.1003052;
RA   de Bentzmann S., Giraud C., Bernard C.S., Calderon V., Ewald F.,
RA   Plesiat P., Nguyen C., Grunwald D., Attree I., Jeannot K.,
RA   Fauvarque M.O., Bordi C.;
RT   "Unique biofilm signature, drug susceptibility and decreased virulence
RT   in Drosophila through the Pseudomonas aeruginosa two-component system
RT   PprAB.";
RL   PLoS Pathog. 8:E1003052-E1003052(2012).
RN   [7]
RP   FUNCTION, INDUCTION BY CARBON STARVATION, MUTAGENESIS OF ASP-60, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=31492668; DOI=10.1128/aem.01705-19;
RA   Wang C., Chen W., Xia A., Zhang R., Huang Y., Yang S., Ni L., Jin F.;
RT   "Carbon starvation induces the expression of PprB-regulated genes in
RT   Pseudomonas aeruginosa.";
RL   Appl. Environ. Microbiol. 0:0-0(2019).
CC   -!- FUNCTION: Member of the two-component regulatory system PprA/PprB
CC       involved in biofilm formation by controlling the expression of
CC       many related genes including type IVb pili major subunit flp
CC       pilin, adhesin bapA or cupE fimbriae (PubMed:19151143,
CC       PubMed:23209420, PubMed:21091863, PubMed:31492668). Modulates also
CC       quorum-sensing signal production acting on both negative and
CC       positive modulators (PubMed:15882421). Functions as a
CC       transcription regulator by direct binding to promoter regions
CC       (PubMed:12499175, PubMed:19151143). Negatively regulates its own
CC       transcription (PubMed:31492668). {ECO:0000269|PubMed:12499175,
CC       ECO:0000269|PubMed:15882421, ECO:0000269|PubMed:19151143,
CC       ECO:0000269|PubMed:21091863, ECO:0000269|PubMed:23209420,
CC       ECO:0000269|PubMed:31492668}.
CC   -!- INDUCTION: By carbon starvation. This increased expression is
CC       controlled by RpoS. {ECO:0000269|PubMed:31492668}.
CC   -!- PTM: Phosphorylated by PprA. {ECO:0000269|PubMed:12499175}.
CC   -!- DISRUPTION PHENOTYPE: Deficiency shows a reduced swimming and
CC       swarming capacity and loss of extracellular virulence protease
CC       production (PubMed:15882421). In addition, expression of flp is
CC       completely lost upon carbon starvation (PubMed:15882421).
CC       {ECO:0000269|PubMed:15882421}.
DR   EMBL; AE004091; AAG07684.1; -; Genomic_DNA.
DR   PIR; G83107; G83107.
DR   RefSeq; NP_252986.1; NC_002516.2.
DR   RefSeq; WP_003114985.1; NZ_QZGE01000034.1.
DR   SMR; Q9HWA4; -.
DR   PaxDb; Q9HWA4; -.
DR   PRIDE; Q9HWA4; -.
DR   EnsemblBacteria; AAG07684; AAG07684; PA4296.
DR   GeneID; 881658; -.
DR   KEGG; pae:PA4296; -.
DR   PATRIC; fig|208964.12.peg.4498; -.
DR   PseudoCAP; PA4296; -.
DR   eggNOG; ENOG4106WFW; Bacteria.
DR   eggNOG; ENOG410Y893; LUCA.
DR   HOGENOM; HOG000034813; -.
DR   OMA; QIACELG; -.
DR   PhylomeDB; Q9HWA4; -.
DR   BioCyc; PAER208964:G1FZ6-4380-MONOMER; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IDA:PseudoCAP.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:PseudoCAP.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IMP:PseudoCAP.
DR   GO; GO:1900233; P:positive regulation of single-species biofilm formation on inanimate substrate; IMP:PseudoCAP.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd06170; LuxR_C_like; 1.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF00196; GerE; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00038; HTHLUXR.
DR   SMART; SM00421; HTH_LUXR; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS50043; HTH_LUXR_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; DNA-binding; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation;
KW   Two-component regulatory system.
FT   CHAIN         1    275       Two-component response regulator PprB.
FT                                /FTId=PRO_0000448554.
FT   DOMAIN       10    128       Response regulatory.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00169}.
FT   DOMAIN      200    265       HTH luxR-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00411}.
FT   DNA_BIND    224    243       H-T-H motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00411}.
FT   MOD_RES      60     60       4-aspartylphosphate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00169}.
FT   MUTAGEN      60     60       D->A: No change in transcriptional
FT                                regulatory activity.
FT                                {ECO:0000269|PubMed:31492668}.
SQ   SEQUENCE   275 AA;  30558 MW;  7C2DEB7CD823FCA5 CRC64;
     MDKPASRHFS VLIIDDEPQV TSELRELLEN SGYRCVTSTH RESAIASFQA DPNIGLVICD
     LYLGQDNGIR LIESLKEVAG NGRFFESIIL TGHDGRQEVI EAMRVGAADY YQKPVAPQEL
     LHGLERLESR LHERVRSQLS LSHVNQRLEY LAESLNSIYR DIHKIKYEVH GNSQPSALRS
     EDSQPSAPPA PVAESQVSPS NPLFGKLSPR QQAVARLVSK GLTNYQIAYE LGITENTVKL
     YVSQVLRLMH MHNRTQLALA LSPAAMQQGS GAVVH
//
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