CSRA2_PSEPH
ID CSRA2_PSEPH Reviewed; 62 AA.
AC P69920; Q9X6D6;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Translational regulator CsrA2 {ECO:0000255|HAMAP-Rule:MF_00167, ECO:0000305};
DE AltName: Full=Carbon storage regulator 2 {ECO:0000255|HAMAP-Rule:MF_00167};
DE AltName: Full=Regulator of secondary metabolites RsmA {ECO:0000303|PubMed:10570200};
GN Name=csrA2 {ECO:0000255|HAMAP-Rule:MF_00167, ECO:0000305};
GN Synonyms=rsmA {ECO:0000303|PubMed:10570200};
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, 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 [2]
RP FUNCTION, INDUCTION, AND RNA-BINDING.
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 [3]
RP FUNCTION, AND RNA-BINDING.
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 [4]
RP FUNCTION, INDUCTION, 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 [5]
RP FUNCTION, AND RNA-BINDING.
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 [6]
RP FUNCTION.
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).
RN [7]
RP REVIEW.
RX PubMed=25833324; DOI=10.1128/mmbr.00052-14;
RA Vakulskas C.A., Potts A.H., Babitzke P., Ahmer B.M., Romeo T.;
RT "Regulation of bacterial virulence by Csr (Rsm) systems.";
RL Microbiol. Mol. Biol. Rev. 79:193-224(2015).
CC -!- FUNCTION: A translational regulator that binds mRNA to regulate
CC translation initiation and/or mRNA stability. Post-transcriptionally
CC represses the expression of genes controlled by GacA/GacS
CC (PubMed:10570200, PubMed:15601712, PubMed:11807065, PubMed:23635605).
CC Represses expression of hcnA; alterations in the ribosome-binding site
CC relieve the repression (PubMed:10570200). Binds specifically to small
CC RNAs (sRNA) RsmX, RsmZ and RsmY; these sRNAs fold into secondary
CC structures with multiple GGA sequence in loops to which the CsrA
CC proteins bind (PubMed:11807065, PubMed:14622422, PubMed:16286659).
CC Binding to RsmX, RsmY or RsmZ titrates the protein so that it can no
CC longer bind mRNA and repress translation; each sRNA can bind more than
CC one protein (PubMed:14622422, PubMed:16286659). Required for optimal
CC expression and stability of sRNAs RsmX, RsmY and RsmZ (PubMed:15601712,
CC PubMed:16286659). Deletion of rsmY or rsmZ alone has no detectable
CC phenotype, but a double sRNA deletion has a marked decrease in
CC production of secondary metabolites HCN, exoprotease AprA, antifungal
CC agent 2,4-diacetylphloroglucinol and protects cucumber plants from
CC fungal infection less well than wild-type (PubMed:14622422). The triple
CC sRNA deletion has even stronger loss of these phenotypes
CC (PubMed:16286659). {ECO:0000269|PubMed:10570200,
CC ECO:0000269|PubMed:11807065, ECO:0000269|PubMed:14622422,
CC ECO:0000269|PubMed:15601712, ECO:0000269|PubMed:16286659,
CC ECO:0000269|PubMed:23635605}.
CC -!- SUBUNIT: Homodimer; the beta-strands of each monomer intercalate to
CC form a hydrophobic core, while the alpha-helices form wings that extend
CC away from the core. {ECO:0000255|HAMAP-Rule:MF_00167}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00167}.
CC -!- INDUCTION: Active throughout the cell cycle (PubMed:11807065).
CC Expressed during exponential and stationary phases; more protein
CC expressed in stationary phase (at protein level) (PubMed:15601712).
CC Under partial control of the GacA/GacS two-component regulatory system
CC (PubMed:15601712). {ECO:0000269|PubMed:11807065,
CC ECO:0000269|PubMed:15601712}.
CC -!- DISRUPTION PHENOTYPE: Increased expression of aprA (usually repressed
CC by this protein) (PubMed:10570200). Partially suppresses a gacA
CC deletion mutant (PubMed:10570200, PubMed:11807065). Double csrA1-csrA2
CC deletion mutants fully suppress the requirement for GacA/GacS in
CC control of its regulon (PubMed:15601712). Decreased expression and
CC stability of RsmY and RsmZ sRNAs (PubMed:15601712).
CC {ECO:0000269|PubMed:10570200, ECO:0000269|PubMed:11807065}.
CC -!- SIMILARITY: Belongs to the CsrA/RsmA family. {ECO:0000255|HAMAP-
CC Rule:MF_00167}.
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DR EMBL; AF136151; AAD33682.1; -; Genomic_DNA.
DR RefSeq; WP_002554426.1; NZ_LS999205.1.
DR AlphaFoldDB; P69920; -.
DR SMR; P69920; -.
DR STRING; 1124983.PFLCHA0_c45760; -.
DR GeneID; 61870992; -.
DR GeneID; 64464573; -.
DR GeneID; 65075743; -.
DR PATRIC; fig|1124983.3.peg.4603; -.
DR eggNOG; COG1551; Bacteria.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR GO; GO:0045947; P:negative regulation of translational initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0045948; P:positive regulation of translational initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.40.4380; -; 1.
DR HAMAP; MF_00167; CsrA; 1.
DR InterPro; IPR003751; CsrA.
DR InterPro; IPR036107; CsrA_sf.
DR PANTHER; PTHR34984; PTHR34984; 1.
DR Pfam; PF02599; CsrA; 1.
DR SUPFAM; SSF117130; SSF117130; 1.
DR TIGRFAMs; TIGR00202; csrA; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Repressor; RNA-binding; Translation regulation.
FT CHAIN 1..62
FT /note="Translational regulator CsrA2"
FT /id="PRO_0000177081"
SQ SEQUENCE 62 AA; 6953 MW; CE39BBF3118D68CC CRC64;
MLILTRRCAE SLIIGDGEIT VTVLGVKGNQ VRIGVNAPKE VAVHREEIYL RIKKEKDEEP
SH
