Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Biochimica et biophysica acta - 15 Aug 1996

Gilbert M, Ostiguy S, Kluepfel D, Morosoli R

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Bacterial Proteins
Share to Base Sequence

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cloning, Molecular

Share to Escherichia coli

Share to Molecular Sequence Data

Share to Mutation

Share to Restriction Mapping

Source

Identifiers

PMID: 8765222
DOI: 10.1016/0167-4838(96)00075-1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cloning of a secA homolog from Streptomyces lividans 1326 and overexpression in both S. lividans and Escherichia coli.PMID 8765222Read ↗

Characterization of the secA gene of Streptomyces lividans encoding a protein translocase which complements and Escherichia coli mutant defective in the ATPase activity of SecA.Semantic proximity Read ↗

Cloning and characterization of a gene encoding a secreted tripeptidyl aminopeptidase from Streptomyces lividans 66.Semantic proximity Read ↗

Exploring the Feasibility of the Sec Route to Secrete Proteins Using the Tat Route in Streptomyces lividans.Semantic proximity Read ↗

The importance of the Tat-dependent protein secretion pathway in Streptomyces as revealed by phenotypic changes in tat deletion mutants and genome analysis.Semantic proximity Read ↗

Protein secretion in Streptomyces griseus N2-3-11: characterization of the secA gene and its growth phase-dependent expression.Semantic proximity Read ↗

Increase in xylanase production by Streptomyces lividans through simultaneous use of the Sec- and Tat-dependent protein export systems.Semantic proximity Read ↗

Functional characterization of the Staphylococcus carnosus SecA protein in Escherichia coli and Bacillus subtilis secA mutant strains.Semantic proximity Read ↗

Cloning, sequencing, and expression of a Thermomonospora fusca protease gene in Streptomyces lividans.Semantic proximity Read ↗

Effect of signal peptide alterations and replacement on export of xylanase A in Streptomyces lividans.Semantic proximity Read ↗

Lysine 106 of the putative catalytic ATP-binding site of the Bacillus subtilis SecA protein is required for functional complementation of Escherichia coli secA mutants in vivo.Semantic proximity Read ↗

Functional analysis of TatA and TatB in Streptomyces lividans.Semantic proximity Read ↗

Cloning and nucleotide sequencing of the secA gene from coryneform bacteria.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.