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

The streptococcal lipoprotein rotamase A (SlrA) is a functional peptidyl-prolyl isomerase involved in pneumococcal colonization.

The Journal of biological chemistry - 13 Jan 2006

Hermans Peter W M, Adrian Peter V, Albert Christa, Estevão Silvia, Hoogenboezem Theo, Luijendijk Ingrid H T, Kamphausen Thilo, Hammerschmidt Sven

Abstract excerpt

Streptococcus pneumoniae expresses two surface-exposed lipoproteins, PpmA and SlrA, which share homology with distinct families of peptidyl-prolyl isomerases (PPIases). In this study, we demonstrated for the first time that the lipoprotein cyclophilin, SlrA, can catalyze the cis-trans isomerization of proline containing tetrapeptides and that SlrA contributes to pneumococcal colonization. The substrate...

Read the complete abstract on PubMed

Topics

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

Share to Cyclophilin A
Share to Cyclophilins

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

Share to Endothelium, Vascular

Share to Lipoproteins

Share to Peptidylprolyl Isomerase

Share to Phagocytosis

Share to Pneumonia

Share to Streptococcus pneumoniae

Source

Identifiers

PMID: 16260779
DOI: 10.1074/jbc.M510014200

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

The streptococcal lipoprotein rotamase A (SlrA) is a functional peptidyl-prolyl isomerase involved in pneumococcal colonization.PMID 16260779Read ↗

Surface-associated lipoprotein PpmA of Streptococcus pneumoniae is involved in colonization in a strain-specific mannerSemantic proximity Read ↗

The Peptidyl-Prolyl Isomerase Motif Is Lacking in PmpA, the PrsA-Like Protein Involved in the Secretion Machinery of Lactococcus lactisSemantic proximity Read ↗

Small proline-rich proteins (SPRRs) are epidermally produced antimicrobial proteins that defend the cutaneous barrier by direct bacterial membrane disruptionSemantic proximity Read ↗

Microbial Peptidyl-Prolyl <i>cis</i> / <i>trans</i> Isomerases (PPIases): Virulence Factors and Potential Alternative Drug TargetsSemantic proximity Read ↗

Maturation of <i>Streptococcus pneumoniae</i> lipoproteins by a type II signal peptidase is required for ABC transporter function and full virulenceSemantic proximity Read ↗

The putative proteinase maturation protein A of Streptococcus pneumoniae is a conserved surface protein with potential to elicit protective immune responses.Semantic proximity Read ↗

Development of a non-invasive murine infection model for acute otitis media.Semantic proximity Read ↗

An Intracellular Peptidyl-Prolyl cis/trans Isomerase Is Required for Folding and Activity of the Staphylococcus aureus Secreted Virulence Factor Nuclease.Semantic proximity Read ↗

Fine‐tuning cellular levels of DprA ensures transformant fitness in the human pathogen Streptococcus pneumoniaeSemantic proximity Read ↗

The Spl Serine Proteases Modulate Staphylococcus aureus Protein Production and Virulence in a Rabbit Model of PneumoniaSemantic proximity Read ↗

The effect of MurM and a branched cell wall structure on penicillin resistance in <i>Streptococcus pneumoniae</i>Semantic proximity Read ↗

Substrate Recognition Properties of Oligopeptidase B fromSalmonella entericaSerovar TyphimuriumSemantic proximity Read ↗

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