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InterPro: IPR002656 Acyltransferase 3

Protein matchesHelp
UniProtKB
Matches:
4070 proteins
AccessionHelp IPR002656 Acyl_transf_3
TypeHelp Domain
SignaturesHelp
GO Term annotationHelp
Function GO:0016747 transferase activity, transferring acyl groups other than amino-acyl groups
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This entry contains a range of acyltransferase enzymes as well as yet uncharacterised proteins from Caenorhabditis elegans. It also includes the protein OatA. The pathogenic bacteria, Staphylococcus aureus, is able to cause persistent infections due to its ability to resist the immune defence system. Lysozyme, a cell wall-lytic enzyme, is one of the first defence compounds induced in serum and tissues after the onset of infection.

S. aureus has complete resistance to lysozyme action by O-acetylating its peptidoglycan (PG) by O-acetyltransferase (OatA) [1, 2]. Staphylococcus bacteria are one of the only bacterial genera that are resistant to lysozyme and tend to colonise the skin and mucosa of humans and animals [3]. OatA is an integral membrane protein. This entry also includes NolL proteins. NolL-dependent acetylation is specific for the fucosyl penta-N-acetylglucosamine species. In addition, the NolL protein caused elevated production of lipo-chitin oligosaccharides (LCOs). The NolL protein obtained from Rhizobium loti (Mesorhizobium loti) functions as an acetyl transferase [4].

Database linksHelp
Enzyme: EC:2
PANDIT: PF01757
Blocks: IPB002656

Taxonomic coverageHelp

Example proteinsHelp
A1A9U5 Glucans biosynthesis protein C

P23214 O-acetyl transferase

Q09225 Nose resistant to fluoxetine protein 6

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR002656 Acyltransferase 3
IPR006621 Nose resistant to fluoxetine protein, N-terminal
ModBase

PublicationsHelp
1. Bera A, Biswas R, Herbert S, Gotz F.
The presence of peptidoglycan O-acetyltransferase in various staphylococcal species correlates with lysozyme resistance and pathogenicity.
Infect. Immun. 74 4598-604 2006 [PubMed: 16861647]
http://dx.doi.org/10.1128/IAI.00301-06
2. Herbert S, Bera A, Nerz C, Kraus D, Peschel A, Goerke C, Meehl M, Cheung A, Gotz F.
Molecular basis of resistance to muramidase and cationic antimicrobial peptide activity of lysozyme in staphylococci.
PLoS Pathog. 3 e102 2007 [PubMed: 17676995]
http://dx.doi.org/10.1371/journal.ppat.0030102
3. Bera A, Herbert S, Jakob A, Vollmer W, Gotz F.
Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus.
Mol. Microbiol. 55 778-87 2005 [PubMed: 15661003]
http://dx.doi.org/10.1111/j.1365-2958.2004.04446.x
4. Pacios Bras C, Jorda MA, Wijfjes AH, Harteveld M, Stuurman N, Thomas-Oates JE, Spaink HP.
A Lotus japonicus nodulation system based on heterologous expression of the fucosyl transferase NodZ and the acetyl transferase NoIL in Rhizobium leguminosarum.
Mol. Plant Microbe Interact. 13 475-9 2000 [PubMed: 10755312]

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InterPro 23.1