(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 putida group: NE > Pseudomonas putida: 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 putida W619: N, E.
Pseudomonas putida DOT-T1E: N, E.
Pseudomonas putida F1: N, E.
Pseudomonas putida TRO1: N, E.
Pseudomonas putida S11: N, E.
Pseudomonas putida CSV86: N, E.
Pseudomonas putida S610: N, E.
Pseudomonas putida S12: N, E.
Pseudomonas putida S13.1.2: N, E.
Pseudomonas putida KG-4: N, E.
Pseudomonas putida LF54: N, E.
Pseudomonas putida KT2440: N, E.
Pseudomonas putida BIRD-1: N, E.
Pseudomonas putida GB-1: N, E.
Pseudomonas sp. ND6: N, E.
Pseudomonas putida H8234: N, E.
Pseudomonas putida HB3267: N, E.
Pseudomonas putida SJ3: N, E.
Pseudomonas putida LS46: N, E.
Pseudomonas putida NBRC 14164: N, E.
Pseudomonas putida S16: N, E.
Pseudomonas putida ND6: N, E.
Pseudomonas putida B6-2: N, E.
Pseudomonas putida SJTE-1: 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 MTDKPAKGSTTLPATRMNVQNAILGLRGRDLLSTLRNVGRHGLRHPLHTA HHLLALGGQLGRVMLGDTPYQPNPRDARFSDPTWSQNPFYRRGLQAYLAW QKQTRQWIDESHLNDDDRARAHFLFNLINDALAPSNSLLNPQAVKGLFNT GGQSLVRGVAHLLDDLRHNDGLPRQVDERAFEVGVNLAATPGAVVFRNEL LELIQYSPMSEKQHARPLLVVPPQINRFYIFDLSATNSFVQYMLKSGLQV FMVSWSNPDPRHREWGLSSYVQALEEALNACRSISGNRDPNLMGACAGGL TMAALQGHLQAKKQLRRVRSATYLVSLLDSKFESPASLFADEQTIEAAKR RSYQRGVLDGGEVARIFAWMRPNDLIWNYWVNNYLLGKTPPAFDILYWNA DSTRLPAALHGDLLEFFKLNPLTYASGLEVCGTPIDLQQVNIDSFTVAGS NDHITPWDAVYRSALLLGGERRFVLANSGHIQSIINPPGNPKAYYLANPK LSSDPRAWFHDAKRSEGSWWPLWLEWITARSGLLKAPRTELGNATYPLLG PAPGTYVLTR
Pseudomonas putida is a metabolically versatile saprophytic soil bacterium that has been certified as a biosafety host for the cloning of foreign genes. The bacterium also has considerable potential for biotechnological applications. Sequence analysis of the 6.18 Mb genome of strain KT2440 reveals diverse transport and metabolic systems. Although there is a high level of genome conservation with the pathogenic Pseudomonad Pseudomonas aeruginosa (85% of the predicted coding regions are shared), key virulence factors including exotoxin A and type III secretion systems are absent. Analysis of the genome gives insight into the non-pathogenic nature of P. putida and points to potential new applications in agriculture, biocatalysis, bioremediation and bioplastic production.
Novel biodegradable bacterial plastics, made up of units of 3-hydroxy-n-phenylalkanoic acids, are accumulated intracellularly by Pseudomonas putida U due to the existence in this bacterium of (i) an acyl-CoA synthetase (encoded by the fadD gene) that activates the aryl-precursors; (ii) a beta-oxidation pathway that affords 3-OH-aryl-CoAs, and (iii) a polymerization-depolymerization system (encoded in the pha locus) integrated by two polymerases (PhaC1 and PhaC2) and a depolymerase (PhaZ). The complete assimilation of these compounds requires two additional routes that specifically catabolize the phenylacetyl-CoA or the benzoyl-CoA generated from these polyesters through beta-oxidation. Genetic studies have allowed the cloning, sequencing, and disruption of the genes included in the pha locus (phaC1, phaC2, and phaZ) as well as those related to the biosynthesis of precursors (fadD) or to the catabolism of their derivatives (acuA, fadA, and paa genes). Additional experiments showed that the blockade of either fadD or phaC1 hindered the synthesis and accumulation of plastic polymers. Disruption of phaC2 reduced the quantity of stored polymers by two-thirds. The blockade of phaZ hampered the mobilization of the polymer and decreased its production. Mutations in the paa genes, encoding the phenylacetic acid catabolic enzymes, did not affect the synthesis or catabolism of polymers containing either 3-hydroxyaliphatic acids or 3-hydroxy-n-phenylalkanoic acids with an odd number of carbon atoms as monomers, whereas the production of polyesters containing units of 3-hydroxy-n-phenylalkanoic acids with an even number of carbon atoms was greatly reduced in these bacteria. Yield-improving studies revealed that mutants defective in the glyoxylic acid cycle (isocitrate lyase(-)) or in the beta-oxidation pathway (fadA), stored a higher amount of plastic polymers (1.4- and 2-fold, respectively), suggesting that genetic manipulation of these pathways could be useful for isolating overproducer strains. The analysis of the organization and function of the pha locus and its relationship with the core of the phenylacetyl-CoA catabolon is reported and discussed.
Title: Investigation of the function of proteins associated to polyhydroxyalkanoate inclusions in Pseudomonas putida BMO1 Valentin HE, Stuart ES, Fuller RC, Lenz RW, Dennis D Ref: J Biotechnol, 64:145, 1998 : PubMed
Polyhydroxyalkanoate (PHA) granule associated proteins from Pseudomonas oleovorans were purified and the N-terminal sequences of two major proteins migrating in sodium dodecyl sulfate polyacrylamide gels with a relative molecular mass of 18 and 43 kDa (GA1 and GA2, respectively) were analyzed. Radiolabeled degenerate probes deduced from these amino acid sequences were used to identify genomic DNA fragments from P. oleovorans and Pseudomonas putida encoding GA1 and GA2. DNA sequence analysis of the fragments obtained from P. putida revealed that the genes encoding these proteins were adjacent to phaC2 and ORF3, the PHA synthase II gene and an open reading frame of unknown function, respectively, found at the P. oleovorans and P. aeruginosa PHA synthase gene locus. The open reading frames encoding GA1, GA2 and ORF3 or smaller fragments beginning at GA1 were inactivated by chromosomal insertion of the Tn5 kanamycin resistance gene block (neo). When these mutants were grown on mineral salts agar media under nitrogen limitation, containing gluconate or decanoate as carbon sources, they appeared more translucent than the wild-type grown under similar conditions. Gas-chromatographic analysis of the cellular dry mass revealed that the mutant strains accumulated 30-50% less PHA than the P. putida wild type.
Pseudomonas putida Pseudomonas sp. B13 dienelactone hydrolase clcD gene