(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Actinobacteria [phylum]: NE > Actinobacteria [class]: NE > Corynebacteriales: NE > Nocardiaceae: NE > Rhodococcus: NE > Rhodococcus erythropolis: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acid identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Rhodococcus erythropolis SK121: N, E.
Rhodococcus erythropolis CCM2595: N, E.
Rhodococcus erythropolis PR4: N, E.
Rhodococcus erythropolis DN1: N, E.
Rhodococcus erythropolis R138: N, E.
MTANGDVRQPDARTYFTHQHPADYHADWKGYYERALVSRARSMERFAHEL
DIRYGTDPHQILNVFRAADTRSAPVIIYFHGGRWREGHPAFYDHLADTWA
ADGAVFVSAGYRLTPEHSIADSVADAWAVTDWVVRNIAAYGGDPSRITVA
GHSSGGHLASMVALTDNCAVSIVGLVCMSAPVDLRTLGFWDDDTLSPHLQ
ISRVPRRVVVSFGDPEPNRKGDDALRLTREGQMLADSLVAYGASLRTVVL
PNADHVRTATAFADRQSPLFGAAHSVIFGDSTEDRSAPRSPHFQEEKQSC
PE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MTANGDVRQPDARTYFTHQHPADYHADWKGYYERALVSRARSMERFAHEL DIRYGTDPHQILNVFRAADTRSAPVIIYFHGGRWREGHPAFYDHLADTWA ADGAVFVSAGYRLTPEHSIADSVADAWAVTDWVVRNIAAYGGDPSRITVA GHSSGGHLASMVALTDNCAVSIVGLVCMSAPVDLRTLGFWDDDTLSPHLQ ISRVPRRVVVSFGDPEPNRKGDDALRLTREGQMLADSLVAYGASLRTVVL PNADHVRTATAFADRQSPLFGAAHSVIFGDSTEDRSAPRSPHFQEEKQSC PE
Rhodococcus erythropolis BG43 is able to degrade the Pseudomonas aeruginosa quorum sensing signal molecules PQS (Pseudomonas quinolone signal) [2-heptyl-3-hydroxy-4(1H)-quinolone] and HHQ [2-heptyl-4(1H)-quinolone] to anthranilic acid. Based on the hypothesis that degradation of HHQ might involve hydroxylation to PQS followed by dioxygenolytic cleavage of the heterocyclic ring and hydrolysis of the resulting N-octanoylanthranilate, the genome was searched for corresponding candidate genes. Two gene clusters, aqdA1B1C1 and aqdA2B2C2, each predicted to code for a hydrolase, a flavin monooxygenase, and a dioxygenase related to 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase, were identified on circular plasmid pRLCBG43 of strain BG43. Transcription of all genes was upregulated by PQS, suggesting that both gene clusters code for alkylquinolone-specific catabolic enzymes. An aqdR gene encoding a putative transcriptional regulator, which was also inducible by PQS, is located adjacent to the aqdA2B2C2 cluster. Expression of aqdA2B2C2 in Escherichia coli conferred the ability to degrade HHQ and PQS to anthranilic acid; however, for E. coli transformed with aqdA1B1C1, only PQS degradation was observed. Purification of the recombinant AqdC1 protein verified that it catalyzes the cleavage of PQS to form N-octanoylanthranilic acid and carbon monoxide and revealed apparent Km and kcat values for PQS of approximately 27 muM and 21 s(-1), respectively. Heterologous expression of the PQS dioxygenase gene aqdC1 or aqdC2 in P. aeruginosa PAO1 quenched the production of the virulence factors pyocyanin and rhamnolipid and reduced the synthesis of the siderophore pyoverdine. Thus, the toolbox of quorum-quenching enzymes is expanded by new PQS dioxygenases.
Rhodococcus erythropolis BG43 was isolated from soil and characterized as a degrader of the quorum sensing signal molecules 2-heptyl-3-hydroxy-4(1H)-quinolone (the Pseudomonas quinolone signal, PQS) and 2-heptyl-4(1H)-quinolone, produced by Pseudomonas aeruginosa. The complete genome of R. erythropolis BG43 consists of a circular chromosome and three plasmids, one of them circular and two linear ones. In total, 6158 protein-coding regions were identified. With this genome sequence, the genetic basis of its quorum-quenching ability and possible biotechnological applications can be explored further.
