Biomaterial Database

Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpF gene, which codes for a putative class A high-molecular-weight penicillin-binding protein. 1993

D L Popham, and P Setlow

Department of Biochemistry, University of Connecticut Health Center, Farmington 06032.

The partial nucleotide sequence of a gene encoding a Bacillus subtilis homolog to the Escherichia coli ponA gene, encoding penicillin-binding protein 1A, was previously reported. The remaining part of this gene, termed pbpF, was isolated, and its nucleotide sequence was completed. Deletion of this gene did not alter the profile of B. subtilis penicillin-binding proteins observed after gel electrophoresis and resulted in no observable phenotype. A transcriptional pbpF-lacZ fusion was weakly expressed during vegetative growth. Expression diminished during the first hours of sporulation but was slightly induced in the forespore compartment during late sporulation. This sporulation expression was dependent on spoIIIG, which encodes the forespore-specific transcription factor sigma G. A single transcription start site which was apparently directly dependent on E sigma A was detected in vegetative cells.

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
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
D010406	Penicillins	A group of antibiotics that contain 6-aminopenicillanic acid with a side chain attached to the 6-amino group. The penicillin nucleus is the chief structural requirement for biological activity. The side-chain structure determines many of the antibacterial and pharmacological characteristics. (Goodman and Gilman's The Pharmacological Basis of Therapeutics, 8th ed, p1065)	Antibiotics, Penicillin,Penicillin,Penicillin Antibiotics
D010458	Peptidyl Transferases	Acyltransferases that use AMINO ACYL TRNA as the amino acid donor in formation of a peptide bond. There are ribosomal and non-ribosomal peptidyltransferases.	Peptidyl Transferase,Peptidyl Translocase,Peptidyl Translocases,Peptidyltransferase,Transpeptidase,Transpeptidases,Peptidyltransferases,Transferase, Peptidyl,Transferases, Peptidyl,Translocase, Peptidyl,Translocases, Peptidyl
D002267	Muramoylpentapeptide Carboxypeptidase	Enzyme which catalyzes the peptide cross-linking of nascent CELL WALL; PEPTIDOGLYCAN.	Carboxypeptidase Transpeptidase,Carboxypeptidase, Muramoylpentapeptide,Transpeptidase, Carboxypeptidase
D002352	Carrier Proteins	Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes.	Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D003001	Cloning, Molecular	The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.	Molecular Cloning
D005798	Genes, Bacterial	The functional hereditary units of BACTERIA.	Bacterial Gene,Bacterial Genes,Gene, Bacterial
D006602	Hexosyltransferases	Enzymes that catalyze the transfer of hexose groups. EC 2.4.1.-.
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