mycolate outer membrane
A mycolic-acid-rich cell outer membrane in mycobacteria and related Corynebacteriales, containing a lipid bilayer and covalently linked long-chain mycolic acids attached to peptidoglycan through an arabinogalactan network. [GO:0036407]
Synonyms: MOM; mycobacterial outer membrane; mycomembrane
Components
| Component | Type | Part of / acts on | Grounding | Genes | Stoichiometry | Essential | Role |
|---|---|---|---|---|---|---|---|
| mycolic acid | Lipid | part of | CHEBI:25438 | ESSENTIAL | Forms the mycolate-rich hydrophobic membrane layer and creates the covalently attached inner leaflet when esterified to arabinogalactan.
| ||
| extractable mycomembrane lipids | Lipid | part of | Reviewed label only (reviewed name; no accession asserted) | CONDITIONAL | Intercalate with covalently attached mycolates to fill the outer leaflet and tune the hydrophobic surface of the mycomembrane.
| ||
| mycolate outer membrane proteins | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | CONDITIONAL | Provide proteinaceous routes for hydrophilic solute uptake and envelope transport across the mycolate-rich permeability barrier.
|
Taxonomic distribution
NCBITaxon:2Bacteria — VARIABLE: Mycolate outer membranes occur in mycobacteria and related corynebacteria rather than being shared by all bacteria. [DOI:10.1016/j.tim.2009.12.005]NCBITaxon:1763Mycobacterium — COMMON: Mycobacteria are the canonical organisms for the mycolic-acid-rich mycomembrane. [DOI:10.1016/j.tim.2009.12.005]
Canonical examples
NCBITaxon:1772Mycobacterium smegmatis — Fast-growing mycobacterial model used to dissect native mycomembrane composition and mycolate-rich cell-envelope architecture. [DOI:10.1038/s41598-017-12718-4]NCBITaxon:1718Corynebacterium glutamicum — Corynebacterial model in which cryo-electron microscopy directly visualized an outer membrane related to the mycobacterial mycomembrane. [DOI:10.1128/JB.01919-07]
Functions
- mycomembrane permeability barrier — The mycolate-rich membrane creates a low-permeability hydrophobic barrier at the outside of the envelope.
DOI:10.1016/j.tim.2009.12.005Niederweis et al. 2010 review the mycobacterial outer membrane as a permeability barrier.
- porin-mediated hydrophilic uptake — Outer-membrane proteins form channels that let selected hydrophilic solutes cross the otherwise lipid-rich mycolate outer membrane.
DOI:10.1016/j.tim.2009.12.005Niederweis et al. 2010 review porins as uptake channels through mycobacterial outer membranes.
Mechanism graphs
Mycolates form a covalently anchored outer membrane (ASSEMBLY)
Long-chain mycolic acids are esterified to arabinogalactan, which links the hydrophobic mycolate layer to peptidoglycan. Extractable lipids and outer-membrane proteins pack into that mycolate-rich membrane to form a low-permeability envelope boundary.
| Subject | Predicate | Object | Evidence |
|---|---|---|---|
| mycolic acid | esterifies to | arabinogalactan |
|
| arabinogalactan | anchors to | peptidoglycan-based cell wall |
|
| mycolic acid | forms hydrophobic layer of | mycolate outer membrane |
|
| extractable mycomembrane lipids | pack into | mycolate outer membrane |
|
| mycolate outer membrane proteins | embed in | mycolate outer membrane |
|
| mycolate outer membrane | enables | mycomembrane permeability barrier |
|
Discussions
- CURATION_TODO (RESOLVED): Keep the mycolate outer membrane separate from the whole mycolyl-arabinogalactan-peptidoglycan cell-wall core. GO:0036407 denotes the mycolate-rich outer membrane rather than the full peptidoglycan-arabinogalactan-mycolate cell-wall skeleton. Arabinogalactan and peptidoglycan are therefore graph nodes that explain covalent anchoring, not local component entries for the outer membrane itself.
Evidence
GO:0036407Gene Ontology cellular-component term for the mycolate outer membrane.DOI:10.1073/pnas.0709530105Hoffmann et al. 2008, Disclosure of the mycobacterial outer membrane: cryo-electron tomography and vitreous sections reveal the lipid bilayer structure, Proceedings of the National Academy of Sciences USA.DOI:10.1128/JB.01919-07Zuber et al. 2008, Direct visualization of the outer membrane of mycobacteria and corynebacteria in their native state, Journal of Bacteriology.DOI:10.1016/j.tim.2009.12.005Niederweis et al. 2010, Mycobacterial outer membranes: in search of proteins, Trends in Microbiology.DOI:10.1101/cshperspect.a021113Alderwick et al. 2015, The mycobacterial cell wall: peptidoglycan and arabinogalactan, Cold Spring Harbor Perspectives in Medicine.DOI:10.1016/j.chembiol.2013.11.011Marrakchi, Lanéelle and Daffé 2014, Mycolic acids: structures, biosynthesis, and beyond, Chemistry and Biology.
Curation history
2026-09-11T04:39:44Zcodex · CREATED_RECORD — Scaffolded by scripts/new_record.py2026-09-11T04:41:56Zcodex · EXPANDED_RECORD — Added GO-backed mycomembrane synonymy, cell outer membrane parentage, mycolic-acid, extractable-lipid, and outer-membrane protein components, bacterial and mycobacterial taxonomy, M. tuberculosis and C. glutamicum examples, permeability functions, DOI/GO evidence, an anchored mycolate membrane graph, and a cell-wall core boundary discussion.2026-09-11T04:49:06Zcodex · TIGHTENED_DISCUSSION_ANCHOR — Changed the cell-wall core boundary discussion from a broad components anchor to explicit mycolic-acid and extractable-lipid component anchors.2026-09-11T04:53:59Zcodex · ADDRESS_REVIEW — Resolved PR #412 issues #413 and #414 by citing the Bacteria distribution from the mycomembrane literature and replacing the M. tuberculosis canonical example with a directly supported M. smegmatis example.
Source: data/structures/envelope/mycolate_outer_membrane.yaml