HmuY proteins of the <i>Porphyromonas</i> genus show diversity in heme-binding properties.

ABSTRACT:

Introduction

Bacteria of the Porphyromonas genus, belonging to the Bacteroidota phylum, colonize various host niches in health and disease. As heme auxotrophs, they rely on heme uptake for iron and protoporphyrin IX. A key heme acquisition system in Porphyromonas gingivalis is the Hmu system, where the hemophore-like HmuY^Pg protein plays a major role. HmuY^Pg coordinates heme-iron using two histidines, whereas other known HmuY proteins produced by other Bacteroidota members prefer a pair of histidine-methionine or two methionines. Some of them bind heme via the protoporphyrin ring without heme-iron coordination, similar to the P. gingivalis HusA protein.

Methods

This study used bioinformatics, spectroscopic, and electrophoreti

SUBMITTER: Smiga M 

PROVIDER: S-EPMC12106395 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature