The domain within your query sequence starts at position 274 and ends at position 664; the E-value for the Acyl_transf_3 domain shown below is 6.8e-24.

RTLNGIRVLSLLWVISGHTSQMTAWLSLDNVLEWKSRVPENPLYLYSRSGPFYLGVDTFF
LISGWLSARSFLKMHQNTSTGITPKVILRYFLKRFTRLQLLHMYSVCLLVGFFSFVPWGP
VWEVAQFHWDNCREVWWTNLLLLNNFLSVQNACNGWTWYLASDFQFHLTTPLIFFVHGKS
KRVFVLLGGLLFLASSTATTLLTLAYKLPVASPAAASEHGTVLYFSEYYTKPYCRCGPFL
VGLFLSMFMHSDHPTDILKTTVQAMLGWTWSLLTLFAVVALAYVLDDTSPTSSVAAAIYQ
ALHRTLWAAAVGWVIFACQEGYGGPVKRMLSWGIWSLPASISYACYLVHPIVIILYNGLQ
ETLIHYTDTNMLYLFFGHCVLTFLGGLVLTL

Acyl_transf_3

Acyl_transf_3
PFAM accession number:PF01757
Interpro abstract (IPR002656):

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) [(PUBMED:16861647), (PUBMED:17676995)]. 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 [(PUBMED:15661003)]. 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 [(PUBMED:10755312)].

GO function:transferase activity, transferring acyl groups other than amino-acyl groups (GO:0016747)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Acyl_transf_3