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

Outer and inner membrane proteins compose an arginine-agmatine exchange system in Chlamydophila pneumoniae.

Journal of bacteriology - 1 Nov 2008

Smith Conor B, Graham David E

Abstract excerpt

Most chlamydial strains have a pyruvoyl-dependent decarboxylase protein that converts L-arginine to agmatine. However, chlamydiae do not produce arginine, so they must import it from their host. Chlamydophila pneumoniae has a gene cluster encoding a putative outer membrane porin (CPn1033 or aaxA)...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Blotting, Western
Share to Carboxy-Lyases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Centrifugation, Density Gradient

Share to Gene Expression Regulation, Bacterial

Share to Hydrogen-Ion Concentration

Share to Protein Transport

Share to Tandem Mass Spectrometry

Source

Open in PubMed Open full text

Identifiers

PMID: 18790867
DOI: 10.1128/JB.00652-08
PMCID: PMC2576674

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-18790867-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Outer and inner membrane proteins compose an arginine-agmatine exchange system in Chlamydophila pneumoniae.PMID 18790867Read ↗

Identification of a novel subfamily of bacterial AAT-fold basic amino acid decarboxylases and functional characterization of its first representative: <i>Pseudomonas aeruginosa</i> LdcASemantic proximity Read ↗

YjdE (AdiC) is the arginine:agmatine antiporter essential for arginine-dependent acid resistance in Escherichia coli.Semantic proximity Read ↗

Citrulline protects Streptococcus pyogenes from acid stress using the arginine deiminase pathway and the F1Fo-ATPase.Semantic proximity Read ↗

Polyamine biosynthesis and transport mechanisms are crucial for fitness and pathogenesis of Streptococcus pneumoniae.Semantic proximity Read ↗

Functional and biochemical analysis of Chlamydia trachomatis MurC, an enzyme displaying UDP-N-acetylmuramate:amino acid ligase activity.Semantic proximity Read ↗

The role of OmpC and OmpF in acidic resistance in Escherichia coli.Semantic proximity Read ↗

An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae.Semantic proximity Read ↗

CcpA regulates arginine biosynthesis in Staphylococcus aureus through repression of proline catabolism.Semantic proximity Read ↗

A putative transport protein is involved in citrulline excretion and re-uptake during arginine deiminase pathway activity by Lactobacillus sakei.Semantic proximity Read ↗

AdiY Acts as a Cytoplasmic pH-Sensor via Histidine Protonation to Regulate Acid Stress Adaptation in <i>Escherichia coli</i>Semantic proximity Read ↗

The ARG11 gene of Saccharomyces cerevisiae encodes a mitochondrial integral membrane protein required for arginine biosynthesis.Semantic proximity Read ↗

The arc operon for anaerobic arginine catabolism in Pseudomonas aeruginosa contains an additional gene, arcD, encoding a membrane protein.Semantic proximity Read ↗

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