(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 > Firmicutes: NE > Bacilli: NE > Lactobacillales: NE > Lactobacillaceae: NE > Lactobacillus: NE > Lactobacillus plantarum: NE
6_AlphaBeta_hydrolase : lacpl-LP.1774Lactobacillus plantarum hydrolase (putative). A85-EsteraseD-FGH : lacpl-EST1Lactobacillus plantarum (and strain JDM1) acetylesterase (EC 3.1.-), lacpl-EST2Lactobacillus plantarum, acetylesterase (EC 3.1.-) Acetyl esterase (Promiscuous) estA lp_3505. AlphaBeta_hydrolase : lacpl-LP.0461Lactobacillus plantarum cell surface hydrolase, membrane-bound (putative), lacpl-LP.1124Lactobacillus plantarum cell surface hydrolase, lacpl-LP.2620Lactobacillus plantarum cell surface hydrolase, membrane-bound (putative), lacpl-LP.3265Lactobacillus plantarum cell surface hydrolase, membrane-bound (putative), lacpl-LP.3393Lactobacillus plantarum cell surface hydrolase, membrane-bound (putative). BD-FAE : lacpl-Est.1092Lactobacillus plantarum JDM1 Esterase/lipase, lacpl-LP.1002 Lactobacillus plantarum lipase/esterase (putative), lacpl-LP.3561Lactobacillus plantarum lipase/esterase (putative) LP_3561, lacpl-LP.3562Lactobacillus plantarum lipase/esterase (putative) LP_3562. CarbLipBact_1 : lacpl-LP.0796 Lactobacillus plantarum; Lactobacillus pentosus, carboxylesterase (EC 3.1.1.1). Duf_915 : lacpl-LP.0618Lactobacillus plantarum cell surface hydrolase, membrane-bound (putative), lacpl-LP.1156Lactobacillus plantarum cell surface hydrolase (putative), lacpl-LP.1165 Lactobacillus plantarum WCFS1 cell surface hydrolase (putative), lacpl-LP.1935Lactobacillus plantarum cell surface hydrolase (putative), lacpl-LP.2519Lactobacillus plantarum cell surface hydrolase (putative), lacpl-LP.2586Lactobacillus plantarum cell surface hydrolase, membrane-bound (putative), lacpl-LP.2737Lactobacillus plantarum cell surface hydrolase, membrane-bound (putative), lacpl-LP.3205Lactobacillus plantarum hypothetical protein, lacpl-LP.3341Lactobacillus plantarum cell surface hydrolase, membrane-bound (putative). FAE-Bacterial-promiscuous : lacpl-LP.2953Lactobacillus plantarum esterase (putative). Haloperoxidase : lacpl-HPOLactobacillus plantarum (and strain JDM1) halo peroxidase (EC 1.11.1.-). Hormone-sensitive_lipase_like : lacpl-LP.0973 Lactobacillus plantarum lipase/esterase. Lactobacillus_peptidase : lacpl-pepxLactobacillus plantarum peptidase (x-prolyl-dipeptidyl aminopeptidase) (x-pdap). Proline_iminopeptidase : lacpl-PEPILactobacillus plantarum prolyl aminopeptidase (EC 3.4.11.5), lacpl-PEPR1Lactobacillus plantarum prolyl aminopeptidase (EC 3.4.11.5), lacpl-PEPR2Lactobacillus plantarum (and strains JDM1; DOMLa) prolyl aminopeptidase (EC 3.4.11.5), lacps-e1ttj7Lactobacillus plantarum (strain ST-III). Prolyl aminopeptidase. Tannase_Bact : lacpl-tanL Lactobacillus plantarum Tannase (Tannin acylhydrolase) LP.2956 tanL TanBLp. yjfP_esterase-like : lacpl-LP.1760Lactobacillus plantarum lipase/esterase (putative), lacpl-LP.2631Lactobacillus plantarum lipase/esterase (putative)
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.) Lactobacillus plantarum subsp. plantarum ATCC 14917: N, E.
Lactobacillus plantarum JDM1: N, E.
Lactobacillus plantarum ZJ316: N, E.
Lactobacillus plantarum 2165: N, E.
Lactobacillus plantarum subsp. plantarum P-8: N, E.
Lactobacillus plantarum 16: N, E.
Lactobacillus plantarum 4_3: N, E.
Lactobacillus plantarum 2025: N, E.
Lactobacillus plantarum UCMA 3037: N, E.
Lactobacillus plantarum IPLA88: N, E.
Lactobacillus plantarum WJL: N, E.
Lactobacillus plantarum subsp. plantarum ST-III: N, E.
Lactobacillus plantarum WCFS1: N, E.
Lactobacillus plantarum subsp. plantarum NC8: N, E.
Lactobacillus plantarum subsp. plantarum ATCC 14917 = JCM 1149 = CGMCC 1.2437: N, E.
Lactobacillus plantarum CMPG5300: N, E.
Lactobacillus plantarum DOMLa: N, E.
Lactobacillus plantarum AY01: N, E.
Lactobacillus plantarum EGD-AQ4: N, E.
Molecular evidence
Database
No mutation 5 structures(e.g. : 3BXP, 3D3N, 4BZW... more)(less) 3BXP: Crystal structure of putative carboxylesterase (NP_786266.1) from Lactobacillus plantarum at 1.70 A resolution, 3D3N: Crystal structure of lipase/esterase (lp_2923) from Lactobacillus plantarum, Northeast Structural Genomics Consortium Target LpR108., 4BZW: Complete crystal structure of the carboxylesterase Cest-2923 (lp_2923) from Lactobacillus plantarum WCFS1 native, 4BZZ: Complete crystal structure of carboxylesterase Cest-2923 from Lactobacillus plantarum WCFS1 soaked in isoprenyl acetate, 4C01: Complete crystal structure of carboxylesterase Cest-2923 (lp_2923) from Lactobacillus plantarum WCFS1 soaked in phenyl acetate No kinetic
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 MQVEQRTLNTAAHPFQITAYWLDQISDFETAVDYPIMIICPGGGFTYHSG REEAPIATRMMAAGMHTVVLNYQLIVGDQSVYPWALQQLGATIDWITTQA SAHHVDCQRIILAGFSAGGHVVATYNGVATQPELRTRYHLDHYQGQHAAI ILGYPVIDLTAGFPTTSAARNQITTDARLWAAQRLVTPASKPAFVWQTAT DESVPPINSLKYVQAMLQHQVATAYHLFGSGIHGLALANHVTQKPGKDKY LNDQAAIWPQLALRWLQEQGLLAGNY
The hydrolase fold is one of the most versatile structures in the protein realm according to the diversity of sequences adopting such a three-dimensional architecture. In the present study, we clarified the crystal structure of the carboxylesterase Cest-2923 from the lactic acid bacterium Lactobacillus plantarum WCFS1 refined to 2.1 A resolution, determined its main biochemical characteristics and also carried out an analysis of its associative behaviour in solution. We found that the versatility of a canonical alpha/beta hydrolase fold, the basic framework of the crystal structure of Cest-2923, also extends to its oligomeric behaviour in solution. Thus, we discovered that Cest-2923 exhibits a pH-dependent pleomorphic behaviour in solution involving monomers, canonical dimers and tetramers. Although, at neutral pH, the system is mainly shifted to dimeric species, under acidic conditions, tetrameric species predominate. Despite these tetramers resulting from the association of canonical dimers, as is commonly found in many other carboxylesterases from the hormone-sensitive lipase family, they can be defined as 'noncanonical' because they represent a different association mode. We identified this same type of tetramer in the closest relative of Cest-2923 that has been structurally characterized: the sugar hydrolase YeeB from Lactococcus lactis. The observed associative behaviour is consistent with the different crystallographic results for Cest-2923 from structural genomics consortia. Finally, the presence of sulfate or acetate molecules (depending on the crystal form analysed) in the close vicinity of the nucleophile Ser116 allows us to identify interactions with the putative oxyanion hole and deduce the existence of hydrolytic activity within Cest-2923 crystals. STRUCTURED DIGITAL ABSTRACT: Cest-2923 and Cest-2923 bind by x-ray crystallography (1, 2) Cest-2923 and Cest-2923 bind by cosedimentation in solution (1, 2) DATABASE: The atomic coordinates and structure factors have been deposited in the Protein Data Bank with accession numbers: 4BZW for Cest-2923 from native crystals not soaked with substrates (P63 22 space group); 4C01 for Cest-2923 from crystals soaked with phenyl acetate (C2 space group); 4BZZ for Cest-2923 from crystals soaked with isopropenyl acetate (P622 space group).
Lactobacillus plantarum is a lactic acid bacterium (LAB) species commonly used as a probiotic. We have sequenced the genome of Lactobacillus plantarum JDM1, which is a Chinese commercial LAB with several probiotic functions, using a GS 20 system. We recommend that each commercial probiotic strain should undergo complete genome sequencing to ensure safety and stability.
The 3,308,274-bp sequence of the chromosome of Lactobacillus plantarum strain WCFS1, a single colony isolate of strain NCIMB8826 that was originally isolated from human saliva, has been determined, and contains 3,052 predicted protein-encoding genes. Putative biological functions could be assigned to 2,120 (70%) of the predicted proteins. Consistent with the classification of L. plantarum as a facultative heterofermentative lactic acid bacterium, the genome encodes all enzymes required for the glycolysis and phosphoketolase pathways, all of which appear to belong to the class of potentially highly expressed genes in this organism, as was evident from the codon-adaptation index of individual genes. Moreover, L. plantarum encodes a large pyruvate-dissipating potential, leading to various end-products of fermentation. L. plantarum is a species that is encountered in many different environmental niches, and this flexible and adaptive behavior is reflected by the relatively large number of regulatory and transport functions, including 25 complete PTS sugar transport systems. Moreover, the chromosome encodes >200 extracellular proteins, many of which are predicted to be bound to the cell envelope. A large proportion of the genes encoding sugar transport and utilization, as well as genes encoding extracellular functions, appear to be clustered in a 600-kb region near the origin of replication. Many of these genes display deviation of nucleotide composition, consistent with a foreign origin. These findings suggest that these genes, which provide an important part of the interaction of L. plantarum with its environment, form a lifestyle adaptation region in the chromosome.
Lactobacillus plantarum Cest-2923 (lp_2923) lipase/esterase
