true2006-01-102024-03-27103ATL_STAASComplete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance.Holden M.T.G.Feil E.J.Lindsay J.A.Peacock S.J.Day N.P.J.Enright M.C.Foster T.J.Moore C.E.Hurst L.Atkin R.Barron A.Bason N.Bentley S.D.Chillingworth C.Chillingworth T.Churcher C.Clark L.Corton C.Cronin A.Doggett J.Dowd L.Feltwell T.Hance Z.Harris B.Hauser H.Holroyd S.Jagels K.James K.D.Lennard N.Line A.Mayes R.Moule S.Mungall K.Ormond D.Quail M.A.Rabbinowitsch E.Rutherford K.M.Sanders M.Sharp S.Simmonds M.Stevens K.Whitehead S.Barrell B.G.Spratt B.G.Parkhill J.doi:10.1073/pnas.04025211012004Proc. Natl. Acad. Sci. U.S.A.1019786-9791NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]MSSA476Glycoside Hydrolase Family 73PGRPPeptidoglycan recognition protein-likeAmidase/PGRP_sfAmidase_domainGW_domGW_dom_sfMGlyc_endo_b_GlcNAc-like_domAmidase_2GlucosaminidaseGWAmi_2LYZ2N-acetylmuramoyl-L-alanine amidase-likeProkaryotic SH3-related domainGWBifunctional autolysinN-acetylmuramoyl-L-alanine amidase3.5.1.28Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase3.2.1.96atlnagSAS0988Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Cleaves the peptidoglycan connecting the daughter cells at the end of the cell division cycle, resulting in the separation of the two newly divided cells. Acts as an autolysin in penicillin-induced lysis (By similarity).Oligomer; forms a ring structure at the cell surface which is important for efficient partitioning of daughter cells after cell division.Secreted, and then anchored on the cell surface at the peripheral cell wall above the completed septum (septal region), for the next cell division cycle.The GW domains are responsible for directing the proteins to the septal region.Undergoes proteolytic processing to generate the two extracellular lytic enzymes, probably at the septal region on the cell surface.In the N-terminal section; belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.In the C-terminal section; belongs to the glycosyl hydrolase 73 family.129Bifunctional autolysin133781301250GW 1437511GW 2513587GW 3606680GW 4682756GW 5778853GW 6855930GW 79371011Disordered103151Disordered173219N-acetylmuramoyl-L-alanine amidase199769Endo-beta-N-acetylglucosaminidase770Polar residues139Polar residues1842004-07-191true1368686ec90fc2f647f0aea99ffe7387dfe8b7MAKKFNYKLPSMVALTLVGSAVTAHQVQAAETTQDQTTNKNVLDSNKVKATTEQAKAEVKNPTQNISGTQVYQDPAIVQPKTANNKTGNAQVSQKVDTAQVNGDTRANQSATTNNTQPVAKSTSTTAPKTNTNVTNAGYSLVDDEDDNSENQINPELIKSAAKPAALETQYKAAAPKAATTSAPKAKTEATPKVTTFSASAQPRSVAATPKTSLPKYKPQVNSSINDYIRKNNLKAPKIEEDYTSYFPKYAYRNGVGRPEGIVVHDTANDRSTINGEISYMKNNYQNAFVHAFVDGDRIIETAPTDYLSWGVGAVGNPRFINVEIVHTHDYASFARSMNNYADYAATQLQYYGLKPDSAEYDGNGTVWTHYAVSKYLGGTDHADPHGYLRSHNYSYDQLYDLINEKYLIKMGKVAPWGTQSTTTPTTPSKPSTGKLTVAANNGVAQIKPTNSGLYTTVYDKTGKATNEVQKTFAVSKTATLGNQKFYLVQDYNSGNKFGWVKEGDVVYNTAKSPVNVNQSYSIKPGTKLYTVPWGTSKQVAGSVSGSGNQTFKASKQQQIDKSIYLYGSVNGKSGWVSKAYLVDTAKPTPTPTPKPSTPTTNNKLTVSSLNGVAQINAKNNGLFTTVYDKTGKPTKEVQKTFAVTKEASLGGNKFYLVKDYNSPTLIGWVKQGDVIYNNAKSPVNVMQTYTVKPGTKLYSVPWGTYKQEAGAVSGTGNQTFKATKQQQIDKSIYLFGTVNGKSGWVSKAYLAVPAAPKKAVAQPKTAVKAYTVTKPQTTQTVSKIAQVKPNNTGIRASVYEKTAKNGAKYADRTFYVTKERAHGNETYVLLNNTSHNIPLGWFNVKDLNVQNLGKEVKTTQKYTVNKSNNGLSMVPWGTKNQVILTGNNIAQGTFNATKQVSVGKDVYLYGTINNRTGWVNAKDLTAPTAVKPTTSAAKDYNYTYVIKNGNGYYYVTPNSDTAKYSLKAFNEQPFAVVKEQVINEQTWYYGKLSNGKLAWIKSTDLAKELIKYNQTGMTLNQVAQIQAGLQYKPQVQRVPGKWTDANFNDVKHAMDTKRLAQDPALKYQFLRLDQPQNISIDKINQFLKGKGVLENQGAAFNKAAQMYGINEVYLISHALLETGNGTSQLAKGADVVNNKVVTNSNTKYHNVFGIAAYDNDPLREGIKYAKQAGWDTVSKAIVGGAKFIGNSYVKAGQNTLYKMRWNPAHPGTHQYATDIDWANINAKIIKGYYDKIGEVGKYFDIPQYKtruetruetruetrue