Sequence analysis of pDN571, a plasmid encoding novel bacteriocin production in M-type 57 Streptococcus pyogenes. 2004

Nicholas C K Heng, and Grace A Burtenshaw, and Ralph W Jack, and John R Tagg
Department of Microbiology and Immunology, University of Otago, P.O. Box 56, Dunedin, New Zealand. nicholas.heng@stonebow.otago.ac.nz

Production of the novel bacteriocin streptococcin A-M57 (SA-M57) by Streptococcus pyogenes strains of M-protein type 57 is plasmid-associated. Plasmid pDN571 (3351bp) harbored by S. pyogenes 71-724, the prototype M-type 57 strain, has been completely sequenced and contains three putative open reading frames (repA, scnM57 and ORF3). In addition, the double-strand and single-strand (SSO) origins of replication were identified. Analysis of the replication-associated genetic elements places pDN571 in the ubiquitous pC194/pUB110 family of rolling-circle plasmids. The SSO of pDN571 is of the ssoA type. SA-M57 (encoded by scnM57) is synthesized as a secreted 179-amino acid polypeptide with a 27-residue secretion signal peptide and has no homology to proteins of known function.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010957 Plasmids Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS. Episomes,Episome,Plasmid
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001430 Bacteriocins Substances elaborated by specific strains of bacteria that are lethal against other strains of the same or related species. They are protein or lipopolysaccharide-protein complexes used in taxonomy studies of bacteria. Bacteriocin,Lantibiotic,Lantibiotics
D013297 Streptococcus pyogenes A species of gram-positive, coccoid bacteria isolated from skin lesions, blood, inflammatory exudates, and the upper respiratory tract of humans. It is a group A hemolytic Streptococcus that can cause SCARLET FEVER and RHEUMATIC FEVER. Flesh-Eating Bacteria,Streptococcus Group A,Bacteria, Flesh-Eating
D015183 Restriction Mapping Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA. Endonuclease Mapping, Restriction,Enzyme Mapping, Restriction,Site Mapping, Restriction,Analysis, Restriction Enzyme,Enzyme Analysis, Restriction,Restriction Enzyme Analysis,Analyses, Restriction Enzyme,Endonuclease Mappings, Restriction,Enzyme Analyses, Restriction,Enzyme Mappings, Restriction,Mapping, Restriction,Mapping, Restriction Endonuclease,Mapping, Restriction Enzyme,Mapping, Restriction Site,Mappings, Restriction,Mappings, Restriction Endonuclease,Mappings, Restriction Enzyme,Mappings, Restriction Site,Restriction Endonuclease Mapping,Restriction Endonuclease Mappings,Restriction Enzyme Analyses,Restriction Enzyme Mapping,Restriction Enzyme Mappings,Restriction Mappings,Restriction Site Mapping,Restriction Site Mappings,Site Mappings, Restriction
D016366 Open Reading Frames A sequence of successive nucleotide triplets that are read as CODONS specifying AMINO ACIDS and begin with an INITIATOR CODON and end with a stop codon (CODON, TERMINATOR). ORFs,Protein Coding Region,Small Open Reading Frame,Small Open Reading Frames,sORF,Unassigned Reading Frame,Unassigned Reading Frames,Unidentified Reading Frame,Coding Region, Protein,Frame, Unidentified Reading,ORF,Open Reading Frame,Protein Coding Regions,Reading Frame, Open,Reading Frame, Unassigned,Reading Frame, Unidentified,Region, Protein Coding,Unidentified Reading Frames

Related Publications

Nicholas C K Heng, and Grace A Burtenshaw, and Ralph W Jack, and John R Tagg
October 1983, Canadian journal of microbiology,
Nicholas C K Heng, and Grace A Burtenshaw, and Ralph W Jack, and John R Tagg
October 1984, The Journal of hygiene,
Nicholas C K Heng, and Grace A Burtenshaw, and Ralph W Jack, and John R Tagg
November 1986, FEBS letters,
Nicholas C K Heng, and Grace A Burtenshaw, and Ralph W Jack, and John R Tagg
December 1988, The Journal of infectious diseases,
Nicholas C K Heng, and Grace A Burtenshaw, and Ralph W Jack, and John R Tagg
January 2020, The Lancet. Infectious diseases,
Nicholas C K Heng, and Grace A Burtenshaw, and Ralph W Jack, and John R Tagg
May 1978, Infection and immunity,
Nicholas C K Heng, and Grace A Burtenshaw, and Ralph W Jack, and John R Tagg
August 2014, Genome announcements,
Nicholas C K Heng, and Grace A Burtenshaw, and Ralph W Jack, and John R Tagg
January 1976, Allergie und Immunologie,
Nicholas C K Heng, and Grace A Burtenshaw, and Ralph W Jack, and John R Tagg
April 1999, Antonie van Leeuwenhoek,
Nicholas C K Heng, and Grace A Burtenshaw, and Ralph W Jack, and John R Tagg
August 2023, The Journal of biological chemistry,
Copied contents to your clipboard!