Staphylococcus saprophyticus strain UTI-035
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ABSTRACT:
PROVIDER: PRJEB96262 | ENA |
REPOSITORIES: ENA
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Project description:Biodegradation of Navy N5RL1, a widely used acidic azo dye in carpet industry, was studied by bacterial strain isolated from the dye-contaminated soil collected from a carpet industry premises located in Bhadohi, Sant Ravidas Nagar and Uttar Pradesh, India. The isolated strain was identified as Staphylococcus saprophyticus BHUSS X3 on the basis of morphological, biochemical and 16S rRNA gene sequencing analysis. The strain BHUSS X3 decolorized 95.7 % of dye (100 mg/l) within 6 h at optimum pH 8, temperature 35 °C, inoculum 4.0 % under static condition during 24 h incubation. The isolated bacterial strain BHUSS X3 can toralate dye concentration upto 1,000 mg/l. The dye degradation metabolites were confirmed by analysis of degraded products using UV-Vis spectrophotometric, HPLC and FTIR technique. The phytotoxicity analysis was also conducted on Phaseolus aureus and enhanced seed germination was recorded.
| S-EPMC4569626 | biostudies-literature
Project description:A gene encoding a serine-aspartate repeat protein of Staphylococcus saprophyticus, an important cause of urinary tract infections in young women, has been cloned and sequenced. In contrast to other SD repeat proteins, SdrI carries 21 additional N-terminal repeats with a consensus sequence of (P/A)ATKE(K/E)A(A/V)(T/I)(A/T/S)EE and has the longest SD(AD)(1-5) repetitive region (854 amino acids) described so far. This highly repetitive sequence contains only the amino acids serine, asparagine, and a distinctly greater amount of alanine (37%) than all other known SD repeat proteins (2.3 to 4.4%). In addition, it is a collagen-binding protein of S. saprophyticus and the second example in this organism of a surface protein carrying the LPXTG motif. We constructed an isogenic sdrI knockout mutant that showed decreased binding to immobilized collagen compared with wild-type S. saprophyticus strain 7108. Binding could be reconstituted by complementation. Collagen binding is specifically caused by SdrI, and the recently described UafA protein, the only LPXTG-containing protein in the genome sequence of the type strain, is not involved in this trait. Our experiments suggest that, as in other staphylococci, the presence of different LPXTG-anchored cell wall proteins is common in S. saprophyticus and support the notion that the presence of matrix-binding surface proteins is common in staphylococci.
| S-EPMC1539602 | biostudies-literature
Project description:Staphylococcus saprophyticus surface-associated protein (Ssp) was the first surface protein described for this organism. Ssp-positive strains display a fuzzy layer of surface-associated material in electron micrographs, whereas Ssp-negative strains appear to be smooth. The physiologic function of Ssp, however, has remained elusive. To clone the associated gene, we determined the N-terminal sequence, as well as an internal amino acid sequence, of the purified protein. We derived two degenerate primers from these peptide sequences, which we used to identify the ssp gene from genomic DNA of S. saprophyticus 7108. The gene was cloned by PCR techniques and was found to be homologous to genes encoding staphylococcal lipases. In keeping with this finding, strains 7108 and 9325, which are Ssp positive, showed lipase activity on tributyrylglycerol agar plates, whereas the Ssp-negative strain CCM883 did not. Association of enzyme activity with the cloned DNA was proven by introducing the gene into Staphylococcus carnosus TM300. When wild-type strain 7108 and an isogenic mutant were analyzed by transmission electron microscopy, strain 7108 exhibited the fuzzy surface layer, whereas the mutant appeared to be smooth. Lipase activity and the surface appendages could be restored by reintroduction of the cloned gene into the mutant. Experiments using immobilized collagen type I did not provide evidence for the involvement of Ssp in adherence to this matrix protein. Our experiments thus provided evidence that Ssp is a surface-associated lipase of S. saprophyticus.
| S-EPMC1230896 | biostudies-literature
Project description:Staphylococcus saprophyticus Genome sequencing and assembly
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| PRJNA1086054 | ENA
Project description:fosfomycin resistance of Staphylococcus saprophyticus under urine physicochemical conditions
| PRJNA905386 | ENA
Project description:Commensal Staphylococcal species that can cause acute urinary tract infections
| PRJNA35739 | ENA
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| PRJNA700496 | ENA