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HdeA
crystal structure of e. coli periplasmic protein hdea
Identifiers
Symbol	HdeA
Pfam	PF06411
InterPro	IPR010486
SCOP2	1bg8 / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In molecular biology, the HdeA family of proteins (HNS (histone-like nucleoid structuring)-dependent expression A) is a stress response protein family found in highly acid resistant bacteria such as Shigella flexneri and Escherichia coli, but which is lacking in mildly acid tolerant bacteria such as Salmonella. HdeA is one of the most abundant proteins found in the periplasmic space of E. coli, where it is one of a network of proteins that confer an acid resistance phenotype essential for the pathogenesis of enteric bacteria. HdeA is thought to act as a chaperone, functioning to prevent the aggregation of periplasmic proteins denatured under acidic conditions. The HNS protein, a chromatin-associated protein that influences the gene expression of several environmentally-induced target genes, represses the expression of HdeA. HdeB, which is encoded within the same operon, may form heterodimers with HdeA. HdeA is a single domain protein with an overall fold that is similar to the fold of the N-terminal subdomain of the GluRS anticodon-binding domain.

References

1. Gajiwala KS, Burley SK (January 2000). "HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria". Journal of Molecular Biology. 295 (3): 605–12. doi:10.1006/jmbi.1999.3347. PMID 10623550.
2. Masuda N, Church GM (May 2003). "Regulatory network of acid resistance genes in Escherichia coli". Molecular Microbiology. 48 (3): 699–712. doi:10.1046/j.1365-2958.2003.03477.x. PMID 12694615.

• Protein domains