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InterPro: IPR001119 S-layer homology domain

Protein matchesHelp
UniProtKB
Matches:
2546 proteins
AccessionHelp IPR001119 S-layer_homology_dom
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR017313 Peptidase S8A, subtilisin-related, clostridia-2
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

S-layers are paracrystalline mono-layered assemblies of (glyco)proteins which coat the surface of bacteria [1, 2]. Several S-layer proteins and some other cell wall proteins contain one or more copies of a domain of about 50-60 residues, which has been called SLH (for S-layer homology). Although it was originally proposed that SLH domains bind to peptidoglycan, it is now evident that pyruvylated secondary cell wall polymers (SCWPs), which are either teichoic acids, teichuronic acids, lipoteichoic acids or lipoglycans, serve as the anchoring structures for SLH motifs in the Gram-positive cell wall [3, 4]. However, the study of S-layer protein SbpA of Bacillus sphaericus revealed that SLH motifs are not sufficient for specific binding to SCWPs. Thus, the molecular basis explaining SLH affinity and specificity of interaction with cell wall polymers are not completely elucidated [5].

Database linksHelp
PDBe-motif: PS01072
PANDIT: PF00395
Blocks: IPB001119

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001119 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P15730 Uncharacterized protein sll0772

P19424 Endoglucanase

Q8YNL5 Uncharacterized protein alr4550

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR001547 Glycoside hydrolase, family 5
IPR005086 Carbohydrate binding domain, family 17/28
IPR007049 Carbohydrate-selective porin OprB
IPR001119 S-layer homology domain
IPR008979 Galactose-binding domain-like
IPR017853 Glycoside hydrolase, catalytic core
IPR018087 Glycoside hydrolase, family 5, conserved site
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Sleytr UB, Beveridge TJ.
Bacterial S-layers.
Trends Microbiol. 7 253-60 1999 [PubMed: 10366863]
http://dx.doi.org/10.1016/S0966-842X(99)01513-9
2. Sara M, Sleytr UB.
S-Layer proteins.
J. Bacteriol. 182 859-68 2000 [PubMed: 10648507]
http://dx.doi.org/10.1128/JB.182.4.859-868.2000
3. Engelhardt H, Peters J.
Structural research on surface layers: a focus on stability, surface layer homology domains, and surface layer-cell wall interactions.
J. Struct. Biol. 124 276-302 1998 [PubMed: 10049812]
http://dx.doi.org/10.1006/jsbi.1998.4070
4. Schaffer C, Messner P.
The structure of secondary cell wall polymers: how Gram-positive bacteria stick their cell walls together.
Microbiology (Reading, Engl.) 151 643-51 2005 [PubMed: 15758211]
http://dx.doi.org/10.1099/mic.0.27749-0
5. Desvaux M, Dumas E, Chafsey I, Hebraud M.
Protein cell surface display in Gram-positive bacteria: from single protein to macromolecular protein structure.
FEMS Microbiol. Lett. 256 1-15 2006 [PubMed: 16487313]
http://dx.doi.org/10.1111/j.1574-6968.2006.00122.x

Additional ReadingHelp
Mesnage S, Fontaine T, Mignot T, Delepierre M, Mock M, Fouet A.
Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation.
EMBO J. 19 2000 4473-84 [PubMed: 10970841]
http://dx.doi.org/10.1093/emboj/19.17.4473
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InterPro 23.1