Chlamydia cysteine-rich outer membrane protein 6 (IPR003506)

Short name: Chlam_OMP6

Overlapping homologous superfamilies


Family relationships



Three cysteine-rich proteins (also believed to be lipoproteins) make up the extracellular matrix of the Chlamydial outer membrane [PMID: 2287277]. They are involved in the essential structural integrity of both the elementary body (EB) and recticulate body (RB) phase. As these bacteria lack the peptidoglycan layer common to most Gram-negative microbes, such proteins are highly important in the pathogenicity of the organism.

The largest of these is the major outer membrane protein (MOMP), and constitutes around 60% of the total protein for the membrane [PMID: 8477811]. OMP6 is the second largest, with a molecular mass of 58kDa, while the OMP3 protein is ~15kDa [PMID: 2287277]. MOMP is believed to elicit the strongest immune response, and has recently been linked to heart disease through its sequence similarity to a murine heart-muscle specific alpha myosin [PMID: 10037605].

The OMP6 family plays a structural role in the outer membrane during the EB stage of the Chlamydial cell, and different biovars show a small, yet highly significant, change at peptide charge level [PMID: 2287277]. Members of this family include Chlamydia trachomatis, Chlamydia pneumoniae and Chlamydia psittaci.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0005201 extracellular matrix structural constituent

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.