⊟Summary[edit | edit source]
- pan ID?: SAUPAN005022000
- symbol?: —
- synonym:
- ⊟description?: peptidoglycan hydrolase
- peptidoglycan hydrolase
- amidase
- truncated amidase
- truncated phage amidase
- amidase (fragment)
- pseudogene
- SH3 domain-containing protein
- SH3 domain protein
- SH3 type 3 domain-containing protein
- Truncated amidase, phage associated
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 5195189..5195485
- synteny block?: BlockID0039030
- occurrence?: in 44% of 34 strains
sdp : prophage-encoded truncated SH3-domain protein [1]
Truncated SH3-domain protein (SDP) is a component of the immune evasion module found on hlb-converting prophage that is a major contributor to human pathogenic potential. However, unlike other immune evasion module proteins, the role and activities of SDP remain unclear. SH3b domains bind to proline-rich or hydrophobic domain proteins such as fibronectin or bacterial cell wall components and are often found linked to amidase domains in endolysins, explaining SDP's frequent misannotation as a peptidoglycan hydrolase (it isn't - SDP lacks any amidase-like domain). Supporting its location in an immune evasion cluster, short polymers from trimers to dodecamers are immunostimulatory, although monomers, dimers and larger polymers are not. They may sequester released peptidoglycan fragments, preventing immunostimulation. Alternatively, SH3b mRNA binds to the global regulatory small RNA RsaA which may modulate its activity. At this point, not enough is known about SDP to characterize it as an immune evasion protein despite its location in the immune evasion module.
⊟Orthologs[edit | edit source]
⊟Genome Viewer[edit | edit source]
| NCTC8325 | |
| Newman | |
| USA300_FPR3757 |
⊟Alignments[edit | edit source]
- ⊞alignment of orthologues:
- ↑ P Moreillon, P A Majcherczyk
Proinflammatory activity of cell-wall constituents from gram-positive bacteria.
Scand J Infect Dis: 2003, 35(9);632-41
[PubMed:14620147] [WorldCat.org] [DOI] (P p)Bénédicte Fournier, Dana J Philpott
Recognition of Staphylococcus aureus by the innate immune system.
Clin Microbiol Rev: 2005, 18(3);521-40
[PubMed:16020688] [WorldCat.org] [DOI] (P p)Paweł Mitkowski, Elżbieta Jagielska, Elżbieta Nowak, Janusz M Bujnicki, Filip Stefaniak, Dorota Niedziałek, Matthias Bochtler, Izabela Sabała
Structural bases of peptidoglycan recognition by lysostaphin SH3b domain.
Sci Rep: 2019, 9(1);5965
[PubMed:30979923] [WorldCat.org] [DOI] (I e)Luz S Gonzalez-Delgado, Hannah Walters-Morgan, Bartłomiej Salamaga, Angus J Robertson, Andrea M Hounslow, Elżbieta Jagielska, Izabela Sabała, Mike P Williamson, Andrew L Lovering, Stéphane Mesnage
Two-site recognition of Staphylococcus aureus peptidoglycan by lysostaphin SH3b.
Nat Chem Biol: 2020, 16(1);24-30
[PubMed:31686030] [WorldCat.org] [DOI] (I p)Stuart W McKellar, Ivayla Ivanova, Pedro Arede, Rachel L Zapf, Noémie Mercier, Liang-Cui Chu, Daniel G Mediati, Amy C Pickering, Paul Briaud, Robert G Foster, Grzegorz Kudla, J Ross Fitzgerald, Isabelle Caldelari, Ronan K Carroll, Jai J Tree, Sander Granneman
RNase III CLASH in MRSA uncovers sRNA regulatory networks coupling metabolism to toxin expression.
Nat Commun: 2022, 13(1);3560
[PubMed:35732654] [WorldCat.org] [DOI] (I e)Chrispin Chaguza, Joshua T Smith, Spencer A Bruce, Robert Gibson, Isabella W Martin, Cheryl P Andam
Prophage-encoded immune evasion factors are critical for Staphylococcus aureus host infection, switching, and adaptation.
Cell Genom: 2022, 2(11);
[PubMed:36465278] [WorldCat.org] [DOI] (I p)