(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Proteobacteria: NE > Gammaproteobacteria: NE > Pseudomonadales: NE > Pseudomonadaceae: NE > Pseudomonas: NE > Pseudomonas stutzeri group: NE > Pseudomonas stutzeri subgroup: NE > Pseudomonas stutzeri: 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.) Pseudomonas stutzeri ATCC 14405 = CCUG 16156: N, E.
Pseudomonas stutzeri CCUG 29243: N, E.
Pseudomonas stutzeri TS44: N, E.
Pseudomonas stutzeri DSM 10701: N, E.
Pseudomonas stutzeri RCH2: N, E.
Pseudomonas stutzeri NF13: N, E.
Pseudomonas stutzeri MF28: N, E.
Pseudomonas stutzeri KOS6: N, E.
Pseudomonas stutzeri A1501: N, E.
Pseudomonas stutzeri ATCC 17588 = LMG 11199: N, E.
Pseudomonas stutzeri B1SMN1: N, E.
Pseudomonas stutzeri DSM 4166: N, E.
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 MNSSAACRTIAASSRPWCVARWWTVMASPSTASSSCSRPAFTRRPAAKSS ARRCASSISPRNWTCCNETRCPFSPGAVAGRCGGTSEPGLFPLRRRQRAR VFSRGKRPPKAFASCMPSNCPAAARRLREPFAESLAQLAEAFAEQCRALP NKPLILFGHSLGALLAYETARVLLAKGERPPVQLLVSSRQSPDWLPACAG LPALNDQALRDYLGNLAGTPPEVLQSKAMMDLAVPVLQADLKLILNYQHR HLQPLSIPVLVFGAISDQQVRYESLLSWERISGEGFSLRMIEGGHFAVMQ QPQWVLDQVQTEL
References
Title: Metal chelating properties of pyridine-2,6-bis(thiocarboxylic acid) produced by Pseudomonas spp. and the biological activities of the formed complexes Cortese MS, Paszczynski A, Lewis TA, Sebat JL, Borek V, Crawford RL Ref: Biometals, 15:103, 2002 : PubMed
We evaluated the ability of pyridine-2,6-bis(thiocarboxylic acid) (pdtc) to form complexes with 19 metals and 3 metalloids. Pdtc formed complexes with 14 of the metals. Two of these metal:pdtc complexes, Co:(pdtc)2 and Cu:pdtc, showed the ability to cycle between redox states, bringing to 4 the number of known redox-active pdtc complexes. A precipitant formed when pdtc was added to solutions of As, Cd, Hg, Mn, Pb, and Se. Additionally, 14 of 16 microbial strains tested were protected from Hg toxicity when pdtc was present. Pdtc also mediated protection from the toxic effects of Cd and Te, but for fewer strains. Pdtc by itself does not facilitate iron uptake, but increases the overall level of iron uptake of Pseudomonas stutzeri strain KC and P. putida DSM301. Both these pseudomonads could reduce amorphous Fe(III) oxyhydroxide in culture. In vitro reactions showed that copper and pdtc were required for this activity. This reaction may derive its reducing power from the hydrolysis of the thiocarboxyl groups of pdtc.
        
Title: Antimicrobial properties of pyridine-2,6-dithiocarboxylic acid, a metal chelator produced by Pseudomonas spp Sebat JL, Paszczynski AJ, Cortese MS, Crawford RL Ref: Applied Environmental Microbiology, 67:3934, 2001 : PubMed
Pyridine-2,6-dithiocarboxylic acid (pdtc) is a metal chelator produced by Pseudomonas spp. It has been shown to be involved in the biodegradation of carbon tetrachloride; however, little is known about its biological function. In this study, we examined the antimicrobial properties of pdtc and the mechanism of its antibiotic activity. The growth of Pseudomonas stutzeri strain KC, a pdtc-producing strain, was significantly enhanced by 32 microM pdtc. All nonpseudomonads and two strains of P. stutzeri were sensitive to 16 to 32 microM pdtc. In general, fluorescent pseudomonads were resistant to all concentrations tested. In competition experiments, strain KC demonstrated antagonism toward Escherichia coli. This effect was partially alleviated by 100 microM FeCl3. Less antagonism was observed in mutant derivatives of strain KC (CTN1 and KC657) which lack the ability to produce pdtc. A competitive advantage was restored to strain CTN1 by cosmid pT31, which restores pdtc production. pT31 also enhanced the pdtc resistance of all pdtc-sensitive strains, indicating that this plasmid contains elements responsible for resistance to pdtc. The antimicrobial effect of pdtc was reduced by the addition of Fe(III), Co(III), and Cu(II) and enhanced by Zn(II). Analyses by mass spectrometry determined that Cu(I):pdtc and Co(III):pdtc2 form immediately under our experimental conditions. Our results suggest that pdtc is an antagonist and that metal sequestration is the primary mechanism of its antimicrobial activity. It is also possible that Zn(II), if present, may play a role in pdtc toxicity.
        
Title: A Pseudomonas stutzeri gene cluster encoding the biosynthesis of the CCl4-dechlorination agent pyridine-2,6-bis(thiocarboxylic acid) Lewis TA, Cortese MS, Sebat JL, Green TL, Lee CH, Crawford RL Ref: Environ Microbiol, 2:407, 2000 : PubMed
A spontaneous mutant of Pseudomonas stutzeri strain KC lacked the carbon tetrachloride (CCl4) transformation ability of wild-type KC. Analysis of restriction digests separated by pulsed-field gel electrophoresis (PFGE) indicated that the mutant strain CTN1 differed from strain KC by deletion of approximately 170 kb of chromosomal DNA. CTN1 did not produce pyridine-2,6-bis(thiocarboxylic acid) (PDTC), the agent determined to be responsible for CCl4 dechlorination in cultures of strain KC. Cosmids from a genomic library of strain KC containing DNA from within the deleted region were identified by hybridization with a 148 kb genomic Spel fragment absent in strain CTN1. Several cosmids identified in this manner were further screened for complementation of the PDTC biosynthesis-negative (Pdt -) phenotype. One cosmid (pT31) complemented the Pdt- phenotype of CTN1 and conferred CCl4 transformation activity and PDTC production upon other pseudomonads. Southern analysis showed that none of three other P. stutzeri strains representing three genomovars contained DNA that would hybridize with the 25,746 bp insert of pT31. Transposon mutagenesis of pT31 identified open reading frames (ORFs) whose disruption affected the ability to make PDTC in the strain CTN1 background. These data describe the pdt locus of strain KC as residing in a non-essential region of the chromosome subject to spontaneous deletion. The pdt locus is necessary for PDTC biosynthesis in strain KC and is sufficient for PDTC biosynthesis by other pseudomonads but is not a common feature of P. stutzeri strains.