GACA_PSEPH
ID GACA_PSEPH Reviewed; 213 AA.
AC P32967;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Response regulator GacA;
DE AltName: Full=Global activator;
DE AltName: Full=Global antibiotic and cyanide control protein {ECO:0000303|PubMed:1311842};
GN Name=gacA {ECO:0000303|PubMed:1311842};
OS Pseudomonas protegens (strain DSM 19095 / LMG 27888 / CFBP 6595 / CHA0).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1124983;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=1311842; DOI=10.1073/pnas.89.5.1562;
RA Laville J., Voisard C.P., Keel C., Maurhofer M., Difago G., Haas D.;
RT "Global control in Pseudomonas fluorescens mediating antibiotic synthesis
RT and suppression of black root rot of tobacco.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1562-1566(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BL915;
RX PubMed=8075420; DOI=10.1094/mpmi-7-0455;
RA Gaffney T.D., Lam S.T., Ligon J., Gates K., Frazelle A., Maio J., Hill S.,
RA Goodwin S., Torkewitz N., Allshouse A.M., Kempf H.J., Becker J.O.;
RT "Global regulation of expression of antifungal factors by a Pseudomonas
RT fluorescens biological control strain.";
RL Mol. Plant Microbe Interact. 7:455-463(1994).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=10570200; DOI=10.1073/pnas.96.24.14073;
RA Blumer C., Heeb S., Pessi G., Haas D.;
RT "Global GacA-steered control of cyanide and exoprotease production in
RT Pseudomonas fluorescens involves specific ribosome binding sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:14073-14078(1999).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=11807065; DOI=10.1128/jb.184.4.1046-1056.2002;
RA Heeb S., Blumer C., Haas D.;
RT "Regulatory RNA as mediator in GacA/RsmA-dependent global control of
RT exoproduct formation in Pseudomonas fluorescens CHA0.";
RL J. Bacteriol. 184:1046-1056(2002).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=14622422; DOI=10.1046/j.1365-2958.2003.03774.x;
RA Valverde C., Heeb S., Keel C., Haas D.;
RT "RsmY, a small regulatory RNA, is required in concert with RsmZ for GacA-
RT dependent expression of biocontrol traits in Pseudomonas fluorescens
RT CHA0.";
RL Mol. Microbiol. 50:1361-1379(2003).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=15601712; DOI=10.1128/jb.187.1.276-285.2005;
RA Reimmann C., Valverde C., Kay E., Haas D.;
RT "Posttranscriptional repression of GacS/GacA-controlled genes by the RNA-
RT binding protein RsmE acting together with RsmA in the biocontrol strain
RT Pseudomonas fluorescens CHA0.";
RL J. Bacteriol. 187:276-285(2005).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 19095 / LMG 27888 / CFBP 6595 / CHA0;
RX PubMed=16286659; DOI=10.1073/pnas.0505673102;
RA Kay E., Dubuis C., Haas D.;
RT "Three small RNAs jointly ensure secondary metabolism and biocontrol in
RT Pseudomonas fluorescens CHA0.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17136-17141(2005).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23635605; DOI=10.4161/rna.24771;
RA Lapouge K., Perozzo R., Iwaszkiewicz J., Bertelli C., Zoete V.,
RA Michielin O., Scapozza L., Haas D.;
RT "RNA pentaloop structures as effective targets of regulators belonging to
RT the RsmA/CsrA protein family.";
RL RNA Biol. 10:1031-1041(2013).
CC -!- FUNCTION: Member of the two-component regulatory system GacA/GacS which
CC controls the expression of secondary metabolites and extracellular
CC products. Acts (probably primarily) by activating expression of CsrA1
CC and CsrA2 antagonist small RNAs (sRNA) RsmX, RsmY and RsmZ which bind
CC to and prevent translation repression by CsrA1 and CsrA2
CC (PubMed:11807065, PubMed:14622422, PubMed:15601712, PubMed:16286659).
CC Involved in the regulation of secondary metabolism and in the synthesis
CC of the antifungal factors cyanide, 2,4-diacetylphloroglucinol and
CC pyoluteorin (PubMed:1311842). Involved in synthesis of the autoinducing
CC signal (unrelated to N-acylhomoserine lactones, induces the Gac/Csr
CC cascade) (PubMed:16286659). Exercises positive post-transcriptional
CC control over the hcnABC and aprA genes; acts upstream of CsrA2 (rsmA)
CC (PubMed:10570200). Controls expression of csrA1 (rsmE) and csrA2
CC (PubMed:15601712). {ECO:0000269|PubMed:10570200,
CC ECO:0000269|PubMed:11807065, ECO:0000269|PubMed:1311842,
CC ECO:0000269|PubMed:14622422, ECO:0000269|PubMed:15601712,
CC ECO:0000269|PubMed:16286659, ECO:0000269|PubMed:23635605}.
CC -!- INDUCTION: Increases 2-fold from exponential to stationary phase (at
CC protein level). {ECO:0000269|PubMed:1311842}.
CC -!- PTM: Phosphorylated by GacS (Probable). {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No longer produces the secondary metabolites
CC diacetylphloroglucinol (Phl) or pyoluteorin (2 antifungals) or HCN
CC (PubMed:1311842). No longer protects tobacco plants from attack by the
CC black root rot-causing fungus Thielaviopsis basicola (PubMed:1311842).
CC 50-fold decrease in expression of hcnA (PubMed:10570200). Greatly
CC decreased expression of genes controlled by this two-component system
CC such as aprA, hcnA, phlA and pltA (PubMed:10570200, PubMed:11807065,
CC PubMed:14622422, PubMed:15601712, PubMed:23635605). Loss of expression
CC of small RNAs (sRNA) RsmX, RsmY and RsmZ (PubMed:14622422,
CC PubMed:16286659). Loss of the autoinducing signal (which is unrelated
CC to N-acylhomoserine lactones and induces the Gac/Csr cascade)
CC (PubMed:16286659). Its deletion is suppressed by overexpression of
CC sRNAs RsmZ, RsmY or by RsmX (PubMed:11807065, PubMed:14622422,
CC PubMed:16286659). Decreased expression of translational regulators
CC CsrA1 (rsmE) and CsrA2 (rsmA) (PubMed:15601712).
CC {ECO:0000269|PubMed:10570200, ECO:0000269|PubMed:11807065,
CC ECO:0000269|PubMed:1311842, ECO:0000269|PubMed:14622422,
CC ECO:0000269|PubMed:15601712, ECO:0000269|PubMed:16286659,
CC ECO:0000269|PubMed:23635605}.
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DR EMBL; M80913; AAA25821.1; -; Genomic_DNA.
DR EMBL; L29642; AAA98759.1; -; Genomic_DNA.
DR AlphaFoldDB; P32967; -.
DR SMR; P32967; -.
DR STRING; 1124983.PFLCHA0_c36050; -.
DR eggNOG; COG2197; Bacteria.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd06170; LuxR_C_like; 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 Pfam; PF00196; GerE; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00421; HTH_LUXR; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS00622; HTH_LUXR_1; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Phosphoprotein; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..213
FT /note="Response regulator GacA"
FT /id="PRO_0000081288"
FT DOMAIN 3..119
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 142..207
FT /note="HTH luxR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT DNA_BIND 166..185
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT VARIANT 90
FT /note="P -> L (in the spontaneous pleiotropic mutant BL915-
FT 1)"
FT VARIANT 182
FT /note="T -> I (in the spontaneous pleiotropic mutant BL915-
FT 2)"
FT CONFLICT 49
FT /note="Y -> D (in Ref. 2; AAA98759)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="L -> A (in Ref. 2; AAA98759)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 213 AA; 23454 MW; 868824FEF8CF4999 CRC64;
MIRVLVVDDH DLVRTGITRM LADIDGLQVV GQAESGEESL LKARELKPYV VLMDVKMPGI
GGLEATRKLL RSHPDIKVVA VTVCEEDPFP TRLLQAGAAG YLTKGAGLNE MVQAIRLVFA
GQRYISPQIA QQLVFKSFQP SSDSPFDALS EREIQIALMI VGCQKVQIIS DKLCLSPKTV
NTYRYRIFEK LSISSDVELT LLAVRHGMVD ASL
