(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 > Streptococcaceae: NE > Streptococcus: NE > Streptococcus mutans: 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.) Streptococcus mutans serotype c: N, E.
Streptococcus mutans NN2025: N, E.
Streptococcus mutans UA159: N, E.
Streptococcus mutans NLML1: N, E.
Molecular evidence
Database
No mutation 1 structure: 4L9A: Crystal structure of Smu.1393c from Streptococcus mutans UA159 (3L80 superceded by 4L9A) No kinetic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 MAALNKEMVNTLLGPIYTCHREGNPCFVFLSGAGFFSTADNFANIIDKLP DSIGILTIDAPNSGYSPVSNQANVGLRDWVNAILMIFEHFKFQSYLLCVH SIGGFAALQIMNQSSKACLGFIGLEPTTVMIYRAGFSSDLYPQLALRRQK LKTAADRLNYLKDLSRSHFSSQQFKQLWRGYDYCQRQLNDVQSLPDFKIR LALGEEDFKTGISEKIPSIVFSESFREKEYLESEYLNKHTQTKLILCGQH HYLHWSETNSILEKVEQLLSNHEKL
References
Title: Harnessing Nature's Diversity: Discovering organophosphate bioscavenger characteristics among low molecular weight proteins Jacob RB, Michaels KC, Anderson CJ, Fay JM, Dokholyan NV Ref: Sci Rep, 6:37175, 2016 : PubMed
Organophosphate poisoning can occur from exposure to agricultural pesticides or chemical weapons. This exposure inhibits acetylcholinesterase resulting in increased acetylcholine levels within the synaptic cleft causing loss of muscle control, seizures, and death. Mitigating the effects of organophosphates in our bodies is critical and yet an unsolved challenge. Here, we present a computational strategy that integrates structure mining and modeling approaches, using which we identify novel candidates capable of interacting with a serine hydrolase probe (with equilibrium binding constants ranging from 4 to 120 muM). One candidate Smu. 1393c catalyzes the hydrolysis of the organophosphate omethoate (kcat/Km of (2.0 +/- 1.3) x 10-1 M-1s-1) and paraoxon (kcat/Km of (4.6 +/- 0.8) x 103 M-1s-1), V- and G-agent analogs respectively. In addition, Smu. 1393c protects acetylcholinesterase activity from being inhibited by two organophosphate simulants. We demonstrate that the utilized approach is an efficient and highly-extendable framework for the development of prophylactic therapeutics against organophosphate poisoning and other important targets. Our findings further suggest currently unknown molecular evolutionary rules governing natural diversity of the protein universe, which make it capable of recognizing previously unseen ligands.
Title: Structural and functional characterization of a novel alpha/beta hydrolase from cariogenic pathogen Streptococcus mutans Wang Z, Li L, Su XD Ref: Proteins, 82:695, 2014 : PubMed
The protein Smu.1393c from Streptococcus mutans is annotated as a putative alpha/beta hydrolase, but it has low sequence identity to the structure-known alpha/beta hydrolases. Here we present the crystal structure of Smu.1393c at 2.0 A resolution. Smu.1393c has a fully open alkaline substrate pocket, whose conformation is unique among other similar hydrolase structures. Three residues, Ser101, His251, and Glu125, were identified as the active center of Smu.1393c. By screening a series of artificial hydrolase substrates, we demonstrated Smu.1393c had low carboxylesterase activity towards short-chain carboxyl esters, which provided a clue for exploring the in vivo function of Smu.1393c. Proteins 2014; 82:695-700. (c) 2013 Wiley Periodicals, Inc.
Streptococcus mutans is the leading cause of dental caries (tooth decay) worldwide and is considered to be the most cariogenic of all of the oral streptococci. The genome of S. mutans UA159, a serotype c strain, has been completely sequenced and is composed of 2,030,936 base pairs. It contains 1,963 ORFs, 63% of which have been assigned putative functions. The genome analysis provides further insight into how S. mutans has adapted to surviving the oral environment through resource acquisition, defense against host factors, and use of gene products that maintain its niche against microbial competitors. S. mutans metabolizes a wide variety of carbohydrates via nonoxidative pathways, and all of these pathways have been identified, along with the associated transport systems whose genes account for almost 15% of the genome. Virulence genes associated with extracellular adherent glucan production, adhesins, acid tolerance, proteases, and putative hemolysins have been identified. Strain UA159 is naturally competent and contains all of the genes essential for competence and quorum sensing. Mobile genetic elements in the form of IS elements and transposons are prominent in the genome and include a previously uncharacterized conjugative transposon and a composite transposon containing genes for the synthesis of antibiotics of the gramicidin/bacitracin family; however, no bacteriophage genomes are present.
Streptococcus mutans conserved hypothetical protein
