http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID143586
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA. OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane. |
| title | OmpA_C-like |
| isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/17988961 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/21272185 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/25139643 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/26134581 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/17368608 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1652516 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/25391442 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24814590 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30745231 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16033723 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7743817 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
Total number of triples: 18.