S-layer
A paracrystalline monomolecular array of one or more (glyco)protein species that self-assemble on the outermost surface of the cell envelope, with oblique, square or hexagonal lattice symmetry. S-layers are common in Archaea, where they are often the sole wall component, and widespread but patchily distributed in Bacteria. [DOI:10.1111/1574-6976.12063]
Image (not hosted — CC_BY_NC_4_0): CaltechDATA qgffm-kzf88 (Atlas of Bacterial and Archaeal Cell Structure, 2.6 Surface layer, file 2_6_Ccrescentus.mp4)
NCBITaxon:155892) · Catherine Oikonomou & Grant Jensen, Atlas of Bacterial and Archaeal Cell Structure (Caltech Library), CC BY-NC 4.0; tomogram collected by Ariane Briegel · CC_BY_NC_4_0 · source: CELL_STRUCTURE_ATLAS CaltechDATA qgffm-kzf88 (Atlas of Bacterial and Archaeal Cell Structure, 2.6 Surface layer, file 2_6_Ccrescentus.mp4) · DOI:10.22002/D1.1355Synonyms: surface layer; crystalline cell surface layer
Xrefs: uniprot.location:SL-0262 — S-layer
Components
| Component | Type | Part of / acts on | Grounding | Genes | Stoichiometry | Essential | Role |
|---|---|---|---|---|---|---|---|
| S-layer protein (SLP) | Protein | part of | typically one dominant protein species; subunits are usually 40–200 kDa | ESSENTIAL | The lattice-forming subunit; self-assembles in vitro.
| ||
| S-layer homology (SLH) domain | Protein | part of | InterPro:IPR001119 | CONDITIONAL | In many Gram-positive bacteria, tandem SLH domains within the S-layer protein anchor it to pyruvylated secondary cell-wall polymer; other lineages use different anchoring modules.
| ||
| secondary cell-wall polymer (SCWP) | Polysaccharide | part of | CONDITIONAL | Peptidoglycan-linked anchor polymer recognised by the SLH domain.
|
Taxonomic distribution
NCBITaxon:2157Archaea — COMMON: Frequently the only envelope layer outside the membrane. [DOI:10.1038/nrmicro2576]NCBITaxon:2Bacteria — VARIABLE: Present across many phyla but a strain-level trait, and readily lost on laboratory passage. [DOI:10.1111/1574-6976.12063]
Canonical examples
NCBITaxon:155892Caulobacter vibrioides — RsaA S-layer; the best-characterised Gram-negative S-layer. [DOI:10.1038/nrmicro3213]NCBITaxon:1422Geobacillus stearothermophilus — SbsA/SbsB S-layers, the classic self-assembly system. [DOI:10.1111/1574-6976.12063]
Functions
- cell shape maintenance and envelope stabilisation — Contributes to shape and osmotic stability, especially in Archaea lacking a rigid wall.
DOI:10.1038/nrmicro2576Albers & Meyer 2011.
- molecular sieving and surface interaction — Lattice pores set a size cut-off; the outer face mediates adhesion and phage or immune interactions.
DOI:10.1038/nrmicro3213Fagan & Fairweather 2014.
Associated traits
- CONFERS
traitmech:000064— S-layer S-layerDOI:10.1038/nrmicro3213Fagan and Fairweather 2014 define and review the bacterial S-layer phenotype.
Physical properties
- THICKNESS: 5-25
UO:0000018[DOI:10.1111/1574-6976.12063]
Mechanism graphs
S-layer proteins self-assemble into a surface lattice (ASSEMBLY)
Secreted S-layer proteins self-assemble into a crystalline two-dimensional lattice that coats the outer face of the cell. In many Gram-positive S-layers, SLH domains within the lattice-forming protein bind secondary cell-wall polymers to retain the lattice on the peptidoglycan-linked envelope surface.
| Subject | Predicate | Object | Evidence |
|---|---|---|---|
| S-layer homology domain | is part of | S-layer (glyco)protein subunit |
|
| S-layer (glyco)protein subunit | self-assembles into | S-layer |
|
| S-layer | coats | cell envelope outer surface |
|
| secondary cell-wall polymer | localizes to | cell envelope outer surface |
|
| S-layer homology domain | binds | secondary cell-wall polymer |
|
| secondary cell-wall polymer | anchors | S-layer |
|
Evidence
DOI:10.1111/1574-6976.12063Sleytr et al. 2014, "S-layers - principles and applications".DOI:10.1038/nrmicro3213Fagan & Fairweather 2014, "Biogenesis and functions of bacterial S-layers".DOI:10.1038/nrmicro2576Albers & Meyer 2011, "The archaeal cell envelope".
Curation history
2026-08-29T00:00:00Zclaude · CREATED_RECORD — Drafted composition, distribution and functions from the cited reviews. No mechanism graph yet. Not yet human-reviewed.2026-08-29T03:00:00Zclaude · ADD_IMAGE — Added link-only Cell Structure Atlas cryo-ET video (CaltechDATA DOI:10.22002/D1.1355, CC BY-NC 4.0, Caulobacter crescentus NCBITaxon:155892); rights verified against the CaltechDATA API.2026-08-30T02:14:17Zuniprot_sl · ADD_UNIPROT_SL_XREF — Added uniprot.location:SL-0262 (S-layer); mapping read from the GO line of UniProt subcell.txt.2026-08-30T19:29:55Zcodex · REVIEW_COMPOSITION_AND_ASSEMBLY — Qualified the definition for one-or-more S-layer protein species; clarified that the SLH entry denotes SLH-domain-containing S-layer proteins rather than a free protein component; added evidence to the TraitMech link and an evidence-backed self-assembly graph.2026-08-31T06:12:34Zclaude · SET_COMPONENT_ROLE — component_role became required (#77) so the constituent/machinery distinction is machine-readable rather than prose. Set per component; ASSOCIATED_MACHINERY only where the protein acts on the already-assembled structure.2026-09-04T01:23:31Zcodex · ENHANCE_CAUSAL_GRAPH — Expanded the S-layer assembly graph with SLH-domain and secondary-cell-wall polymer anchoring nodes and evidence-backed edges.