| UniProt functional annotation for P0DPC3 | |||
| UniProt code: P0DPC3. |
| Organism: | Pseudomonas protegens (strain DSM 19095 / LMG 27888 / CHA0). | |
| Taxonomy: | Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas. | |
| Function: | A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability (PubMed:17704818, PubMed:23635605). Post-transcriptionally represses the expression of genes controlled by GacA/GacS (PubMed:15601712, PubMed:23635605). Binds the 5' UTR of mRNA; the mRNA binds to the outside edge to each monomer and each dimer could bind the same mRNA twice (PubMed:17704818). Recognizes a (A/U)CANGGANG(U/A) consensus, binds to GGA (part of the Shine-Dalgarno sequence) in the 5' UTR loop, which prevents ribosome binding (PubMed:17704818, PubMed:24561806, PubMed:23635605). Overexpression represses target protein expression; mutating nucleotides in the 5' UTR abolishes repression in vivo (PubMed:17704818, PubMed:23635605). Binds specifically to small RNAs (sRNA) RsmX, RsmZ and RsmY; these sRNAs fold into secondary structures with multiple GGA sequences in loops to which the CsrA proteins bind (PubMed:15601712, PubMed:16286659, PubMed:24828038). Binding to RsmX, RsmY or RsmZ titrates the protein so that it can no longer bind mRNA and repress translation (PubMed:15601712, PubMed:24828038). RsmZ can bind up to 5 CsrA1 (rsmE) dimers; they bind cooperatively to GGA sequences in RsmZ in a defined order (PubMed:24828038, PubMed:24561806). Required for optimal expression and stability of sRNAs RsmX, RsmY and RsmZ (PubMed:15601712, PubMed:16286659). Four CsrA1 dimers maximally protect RsmZ from RNase activity (PubMed:24828038). Deletion of rsmX, rsmY or rsmZ alone has no detectable phenotype, but a double rsmY-rsmZ deletion has a marked decrease in production of secondary metabolites HCN, exoprotease AprA, antifungal agent 2,4-diacetylphloroglucinol and swarming motility, and protects cucumber plants from fungal infection less well than wild- type; the triple sRNA deletion has even stronger loss of these phenotypes (PubMed:16286659). {ECO:0000269|PubMed:15601712, ECO:0000269|PubMed:16286659, ECO:0000269|PubMed:17704818, ECO:0000269|PubMed:23635605, ECO:0000269|PubMed:24561806, ECO:0000269|PubMed:24828038}. | |
| Subunit: | Homodimer (PubMed:23635605, PubMed:17704818, PubMed:24828038, PubMed:24561806). The beta-strands of each monomer intercalate to form a hydrophobic core while the alpha-helices form wings that extend away from the core (PubMed:17704818, PubMed:24828038, PubMed:24561806). {ECO:0000269|PubMed:17704818, ECO:0000269|PubMed:23635605, ECO:0000269|PubMed:24561806, ECO:0000269|PubMed:24828038}. | |
| Subcellular location: | Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00167}. | |
| Induction: | Expressed at low levels during exponential growth, considerably more protein expressed in stationary phase (at protein level) (PubMed:15601712). Positively controlled by GacA and negatively regulated by CsrA1 and CsrA2 (PubMed:15601712). {ECO:0000269|PubMed:15601712}. | |
| Domain: | Residues in the N-terminus (2-4) and C-terminus (37-44) help recognize the GGA loop in a mRNA stem-loop; recognition mostly occurs via the protein main chain carbonyl oxygens and amides (PubMed:17704818). Similar interactions occur with fragments of sRNA RsmZ; the binding affinity for GGA-containing RsmZ fragments can vary from 10 nM to 3 mM depending on the sequence and structural context (PubMed:24561806). {ECO:0000269|PubMed:17704818, ECO:0000269|PubMed:24561806}. | |
| Disruption phenotype: | Increased expression of genes controlled by GacA/GacS (aprA, hcnA, phlA), partially suppresses a gacS deletion mutant (PubMed:15601712). Double csrA1-csrA2 deletion mutants fully suppress the requirement for GacA/GacS in control of its regulon (PubMed:15601712). Decreased expression and stability of RsmY and RsmZ sRNAs (PubMed:15601712). {ECO:0000269|PubMed:15601712}. | |
| Similarity: | Belongs to the CsrA/RsmA family. {ECO:0000255|HAMAP- Rule:MF_00167}. | |
Annotations taken from UniProtKB at the EBI.