The Genome of the marine bacterium Cobetia marina KMM 296 isolated from the mussel Crenomytilus grayanus (Dunker, 1853)

Data supporting functional diversity of the marine bacterium Cobetia amphilecti KMM 296

“…Value of the data Data provides new phenotypic characteristics for the description of a new marine bacterial species, Cobetia amphilecti [2] . Data supports the possibility of inducing of previously described C. amphilecti KMM 296 genes [1] that are known to be involved in different biochemical pathways in response to the change of environmental conditions such as nutrient medium or microbial competitors, leading to change phenotypic characteristics and to significantly higher survival of the marine bacterium. Data includes information on species-dependent decreasing of bacterial cells and biofilms growth under co-culturing conditions with C. amphilecti KMM 296 whose metabolites may be of interest for food industry and medicine protection approaches particularly against P. aeruginosa .…”

“… Data is presented in support of functionality of hyper-diverse protein families encoded by the Cobetia amphilecti KMM 296 (formerly Cobetia marina KMM 296) genome (“The genome of the marine bacterium Cobetia marina KMM 296 isolated from the mussel Crenomytilus grayanus (Dunker, 1853)” [1] ) providing its nutritional versatility, adaptability and biocontrol that could be the basis of the marine bacterium evolutionary and application potential. Presented data include the information of growth and biofilm-forming properties of the food-associated isolates of Pseudomonas, Bacillus, Listeria, Salmonella and Staphylococcus under the conditions of their co-culturing with C. amphilecti KMM 296 to confirm its high inter-species communication and anti-microbial activity.…”

A Novel Alkaline Phosphatase/Phosphodiesterase, CamPhoD, from Marine Bacterium Cobetia amphilecti KMM 296

“…They mimic fibronectin in triggering cell spreading, focal adhesion formation, and activation of several tyrosine kinases during interaction with various mammalian cell lines [39,40]. Thus, the RGD motif of CamPhoD may be a player in pathogenesis or the symbiotic relationships between the bacterium and host mollusk during its shell mineralization [12,36]. The part of the CamPhoD molecule from 149 to 505 aa residues is the PhoD-like phosphatase (pfam09423), with characteristic active and ion-binding sites [38].…”

“…The presence of extracellular alkaline phosphatases of the structural families PhoA (GenBank ID: WP_084589490.1) and PhoD (GenBank ID: WP_043333989.1) in the marine gamma-proteobacterium C. amphilecti KMM 296 may indicate either their distinct or cooperative functions for the hydrolysis of various phosphorus-containing organic molecules, depending on the environmental conditions and cell lifestyle [7,36]. The analogous PhoD enzyme from B. subtilis is thought to target specific phosphate-containing molecules, such as teichoic acids linked to the wall peptidoglycan via phosphodiester bonds.…”

“…The genome sequence analysis of C. amphilecti KMM 296 has shown that the bacterium produces not only the highly active alkaline phosphatase CmAP, belonging to the PhoA family (GenBank ID: WP_084589490.1), but also the functionally active PhoD-like phosphatase/phosphodiesterase (GenBank ID: WP_043333989.1), with a novel structure and properties [6,12,36]. This article presents the results of isolation of the gene encoding for the PhoD-like protein from C. amphilecti KMM 296, and in producing the recombinant enzyme CamPhoD with the alkaline phosphatase and phosphodiesterase activities and properties.…”