Evidence map›Paper›PMID 40135891›Full record

ArticleJournal of bacteriology2025

A SecA-associated protease modulates the extent of surface display of staphylococcal protein A.

Muhammad S Azam, Amany M Ibrahim, Owen Leddy, So-Young Oh, Olaf Schneewind, Dominique Missiakas

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of bacteriology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Role of staphylococcal EzrA as a molecular organizer of cell division.bioRxiv : the preprint server for biology · 2026
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Muhammad S AzamHoward Taylor Ricketts Laboratory, Department of Microbiology, The University of Chicago, Chicago, Illinois, USA.
Amany M IbrahimHoward Taylor Ricketts Laboratory, Department of Microbiology, The University of Chicago, Chicago, Illinois, USA.
Owen LeddyHoward Taylor Ricketts Laboratory, Department of Microbiology, The University of Chicago, Chicago, Illinois, USA.
So-Young OhHoward Taylor Ricketts Laboratory, Department of Microbiology, The University of Chicago, Chicago, Illinois, USA.
Olaf SchneewindHoward Taylor Ricketts Laboratory, Department of Microbiology, The University of Chicago, Chicago, Illinois, USA.
Dominique MissiakasHoward Taylor Ricketts Laboratory, Department of Microbiology, The University of Chicago, Chicago, Illinois, USA.ORCID 0000-0001-6482-9633

Funding

TRAINING GRANTS IN ENVIROMENTAL TOXICOLOGYT32ES007020 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ESSIGMANN, JOHN M · 1985 to 2024
$13.1M
Surface Proteins of Gram-Positive BacteriaR01AI038897 · NIAID · UNIVERSITY OF CHICAGO · PI MISSIAKAS, DOMINIQUE M. · 1996 to 2024
$8.9M
National Institute of Allergy and Infectious Diseases 038897NIAID NIH HHS R01 AI038897NIEHS NIH HHS T32 ES007020
6 · The paper itself

Abstract

In bacteria, signal peptides direct pre-proteins to the SecYEG secretion channel and are typically cleaved by signal peptidases during translocation across the membrane. In gram-positive bacteria, such as IMPORTANCE: The "signal hypothesis" proposed that N-terminal sequences of secretory proteins contain targeting cues directing nascent polypeptides to the endoplasmic reticulum. This concept was later confirmed as broadly applicable, even to prokaryotes with a single membrane. In gram-positive bacteria, signal sequences bearing the YSIRK/GXXS motif are necessary and sufficient to direct precursors to septal membranes. However, trans-acting factors involved in this spatially restricted targeting remain largely unknown. Here, we identify a member of the M20 metalloprotease family as a potential contributor to the septal surface display of proteins containing YSIRK/GXXS signal peptides.

Indexed as

Bacterial ProteinsSecA ProteinsStaphylococcal Protein AStaphylococcus aureusGene Expression Regulation, BacterialProtein Sorting SignalsProtein TransportSEC Translocation ChannelsBacterial ProteinsProtein Sorting SignalsSecA ProteinsSEC Translocation ChannelsStaphylococcal Protein Across-wallPepVprotein secretionstaphylococcal protein AStaphylococcus aureusYSIRK secretion motif

Identifiers

PMID40135891
PMCPMC12004944

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.