Paracoccus pantotrophus – NBRC 102493

Paracoccus pantotrophus, Sulfur oxidation, thiol-disulfide oxidoreductase

Paracoccus pantotrophus

NBRC No. NBRC 102493
Scientific Name of this Strain Paracoccus pantotrophus (Robertson and Kuenen 1984) Rainey et al. 1999
Synonymous Name
Type Strain type
Accepted Date 2007/01/23
Isolated Year 1981
Deposited Year 2006
History IAM 15022 <- NCCB 82005 <- LMD 82.5 <- L.A. Robertson, GB17
Other Culture Collection No. IAM 15022=NCCB 82005=LMD 82.5=ATCC 35512=CIP 106514=DSM 2944=JCM 21485=KACC 12253=BCRC 14341=KCTC 12140=NCIMB 13217
Other No. GB17
Rehydration Fluid 805
Medium 805
Cultivation Temp. 37 C
Oxygen Relationship
Source of Isolation Waste treatment plant
Locality of Source Delft
Country of Origin Netherlands
Biosafety Level
Mating Type
Genetic Marker
Plant Quarantine No.
Animal Quarantine No.
Herbarium No.
References 740,4773,4774,4775
Sequences 16S rDNA
Shipping as Glass ampoule (L-dried)

Paracoccus is also a genus of insects in family Pseudococcidae. In taxonomy, Paracoccus is a genus of the Rhodobacteraceae.

Related Paper: “Sulfur oxidation of Paracoccus pantotrophus: the sulfur-binding protein SoxYZ is the target of the periplasmic thiol-disulfide oxidoreductase SoxS.”

Microbiology. 2008 Jul;154(Pt 7):1980-8. doi: 10.1099/mic.0.2008/018655-0.

The periplasmic thiol-disulfide oxidoreductase SoxS is essential for chemotrophic growth of Paracoccus pantotrophus with thiosulfate. To trap its periplasmic partner, the cysteine residues of the CysXaaXaaCys motif of SoxS (11 kDa) were changed to alanine by site-directed mutagenesis. The disrupted soxS gene of the homogenote mutant G OmegaS was complemented with plasmids carrying the mutated soxS[C13A] or soxS[C16A] gene. Strain G OmegaS(pRD179.6[C16A](S)) displayed a marginal thiosulfate-oxidizing activity, suggesting that Cys13(S) binds the target protein. Evidence is presented that SoxS specifically binds SoxY. (i) Immunoblot analysis using non-reducing SDS gel electrophoresis and anti-SoxS and anti-SoxYZ antibodies identified the respective antigens of strain G OmegaS(pRD179.6[C16A](S)) at the 25 kDa position, suggesting an adduct of about 14 kDa, close to the value expected for SoxY migration. (ii) A mutant unable to produce SoxYZ, such as strain G OmegaX(pRD187.7[C16A](S)), did not form a SoxS(C16A) adduct, while addition of homogeneous SoxYZ resulted in the 25 kDa adduct. (iii) The SoxY and SoxZ subunits were distinguished by site-directed mutagenesis of the cysteine residue in SoxZ. SoxYZ(C53S) formed the 25 kDa adduct with SoxS(C16A). These results demonstrate that the target of SoxS is the sulfur-binding protein SoxY of the SoxYZ complex. As SoxYZ is reversibly inactivated, SoxS may activate SoxYZ as a crucial function for chemotrophy of P. pantotrophus.