Biomaterial Database

Cloning of a secA homolog from Streptomyces lividans 1326 and overexpression in both S. lividans and Escherichia coli. 1996

M Gilbert, and S Ostiguy, and D Kluepfel, and R Morosoli

Centre de recherche en microbiologic appliquèe, Institut Armand-Frappier, Universitè du Quèbec, Canada.

We cloned a gene encoding a SecA homolog from Streptomyces lividans 1326, a Gram-positive bacterium known to produce large amounts of extracellular proteins. A protein sequence alignment with the other bacterial SecA homologs revealed that S. lividans SecA shares from 39.5 to 44% identity with them, while it shares 34.2 to 37.2% identity with SecA homologs from plastids of algae and plants. We overexpressed the secA gene in S. lividans 1326 and Escherichia coli MM52 and in both cases we observed the production of a protein with an apparent molecular mass of 117.4 kDa. Although S. lividans SecA is similar to E. coli SecA, it does not complement a thermosensitive mutation in the E. coli secA gene. However, a hybrid polypeptide consisting of the N-terminal portion (first 242 amino acids) of the S. lividans SecA and the C-terminal portion (657 a.a.) of the wild-type E. coli SecA was able to complement this mutant.

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
D009154	Mutation	Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.	Mutations
D011994	Recombinant Proteins	Proteins prepared by recombinant DNA technology.	Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
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
D004926	Escherichia coli	A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.	Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D005816	Genetic Complementation Test	A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.	Allelism Test,Cis Test,Cis-Trans Test,Complementation Test,Trans Test,Allelism Tests,Cis Tests,Cis Trans Test,Cis-Trans Tests,Complementation Test, Genetic,Complementation Tests,Complementation Tests, Genetic,Genetic Complementation Tests,Trans Tests
D000069816	SEC Translocation Channels	Universally conserved multiprotein complexes that form the protein transport channel of the general secretory (SEC) pathway. The SEC translocase is present in all bacteria, archaea, and eukaryotes. It is in the ENDOPLASMIC RETICULUM membrane of eukaryotic cells, in the THYLAKOID MEMBRANE in CHLOROPLASTS and in some protozoa in the INNER MITOCHONDRIAL MEMBRANE.	SEC Translocation Channel,SEC Translocon,SEC61 Translocation Channel,Sec Protein Translocation System,SecYEG Protein,SecYEG Translocation Channel,SEC Complexes,SEC Translocase,SEC Translocons,SEC61 Protein,SEC61 Proteins,SEC61 Translocase,SEC61 Translocation Channels,SEC61 Translocon,Sec Protein Translocation Systems,Sec61 Complex,Sec61 Protein Translocation System,SecY Translocase,SecYEG Complex,SecYEG Complexes,SecYEG Protein Translocation System,SecYEG Proteins,SecYEG Translocation Channels,SecYEG Translocon,Channel, SEC Translocation,Channel, SEC61 Translocation,Channel, SecYEG Translocation,Channels, SEC Translocation,Channels, SEC61 Translocation,Channels, SecYEG Translocation,Complex, Sec61,Complex, SecYEG,Complexes, SEC,Complexes, SecYEG,Protein, SEC61,Protein, SecYEG,Proteins, SEC61,Proteins, SecYEG,Translocase, SEC,Translocase, SEC61,Translocase, SecY,Translocation Channel, SEC,Translocation Channel, SEC61,Translocation Channel, SecYEG,Translocation Channels, SEC,Translocation Channels, SEC61,Translocation Channels, SecYEG,Translocon, SEC,Translocon, SEC61,Translocon, SecYEG,Translocons, SEC
D000081416	SecA Proteins	ATPases that provide energy for the translocation of proteins across bacterial PLASMA MEMBRANES and THYLAKOID membranes, by the SEC TRANSLOCATION CHANNELS. SecA is a component of the bacterial preprotein translocase which is comprised of SecA, the SECYEG TRANSLOCON, and the accessory domain proteins SecD, SecF, YajC, and YidC.	SecA Protein,Protein, SecA,Proteins, SecA
D000251	Adenosine Triphosphatases	A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.	ATPases,Adenosinetriphosphatase,ATPase,ATPase, DNA-Dependent,Adenosine Triphosphatase,DNA-Dependent ATPase,DNA-Dependent Adenosinetriphosphatases,ATPase, DNA Dependent,Adenosinetriphosphatases, DNA-Dependent,DNA Dependent ATPase,DNA Dependent Adenosinetriphosphatases,Triphosphatase, Adenosine
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