ID ATL_STAAU Reviewed; 1255 AA. AC P0C5Z8; O32391; P0C1R4; P52081; Q7WTC6; Q7WY94; Q7WY95; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 27-MAR-2024, entry version 70. DE RecName: Full=Bifunctional autolysin; DE Includes: DE RecName: Full=N-acetylmuramoyl-L-alanine amidase; DE EC=3.5.1.28; DE Includes: DE RecName: Full=Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; DE EC=3.2.1.96; DE Flags: Precursor; GN Name=atl; Synonyms=nag; OS Staphylococcus aureus. OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=1280; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=IL-A; RX PubMed=12760894; DOI=10.1128/aac.47.6.2036-2039.2003; RA Boyle-Vavra S., Challapalli M., Daum R.S.; RT "Resistance to autolysis in vancomycin-selected Staphylococcus aureus RT isolates precedes vancomycin-intermediate resistance."; RL Antimicrob. Agents Chemother. 47:2036-2039(2003). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 775-1255. RA Kamitani S., Minamide W., Yutsudo T., Noda M.; RT "Novel cytotoxin in a clinical isolate of methicillin-resistant S. aureus: RT cloning, sequencing and expression."; RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP FUNCTION. RC STRAIN=ATCC 6538P / DSM 346 / JCM 2151 / NBRC 12732 / NCIMB 8625 / RC NCTC 7447 / NRRL B-313 / FDA 209P; RX PubMed=7883705; DOI=10.1128/jb.177.6.1491-1496.1995; RA Sugai M., Komatsuzawa H., Akiyama T., Hong Y.-M., Oshida T., Miyake Y., RA Yamaguchi T., Suginaka H.; RT "Identification of endo-beta-N-acetylglucosaminidase and N-acetylmuramyl-L- RT alanine amidase as cluster-dispersing enzymes in Staphylococcus aureus."; RL J. Bacteriol. 177:1491-1496(1995). RN [4] RP SUBCELLULAR LOCATION, AND SUBUNIT. RC STRAIN=ATCC 6538P / DSM 346 / JCM 2151 / NBRC 12732 / NCIMB 8625 / RC NCTC 7447 / NRRL B-313 / FDA 209P; RX PubMed=8626282; DOI=10.1128/jb.178.6.1565-1571.1996; RA Yamada S., Sugai M., Komatsuzawa H., Nakashima S., Oshida T., Matsumoto A., RA Suginaka H.; RT "An autolysin ring associated with cell separation of Staphylococcus RT aureus."; RL J. Bacteriol. 178:1565-1571(1996). RN [5] RP SUBCELLULAR LOCATION. RC STRAIN=ATCC 6538P / DSM 346 / JCM 2151 / NBRC 12732 / NCIMB 8625 / RC NCTC 7447 / NRRL B-313 / FDA 209P; RX PubMed=9251058; DOI=10.1111/j.1348-0421.1997.tb01880.x; RA Komatsuzawa H., Sugai M., Nakashima S., Yamada S., Matsumoto A., Oshida T., RA Suginaka H.; RT "Subcellular localization of the major autolysin, ATL and its processed RT proteins in Staphylococcus aureus."; RL Microbiol. Immunol. 41:469-479(1997). RN [6] RP SUBCELLULAR LOCATION. RC STRAIN=ATCC 6538P / DSM 346 / JCM 2151 / NBRC 12732 / NCIMB 8625 / RC NCTC 7447 / NRRL B-313 / FDA 209P; RX PubMed=9139914; DOI=10.1128/jb.179.9.2958-2962.1997; RA Sugai M., Yamada S., Nakashima S., Komatsuzawa H., Matsumoto A., Oshida T., RA Suginaka H.; RT "Localized perforation of the cell wall by a major autolysin: atl gene RT products and the onset of penicillin-induced lysis of Staphylococcus RT aureus."; RL J. Bacteriol. 179:2958-2962(1997). RN [7] RP ROLE OF REPEATS IN LOCALIZATION AT THE SEPTAL REGION. RC STRAIN=OS2; RX PubMed=9707423; DOI=10.1093/emboj/17.16.4639; RA Baba T., Schneewind O.; RT "Targeting of muralytic enzymes to the cell division site of Gram-positive RT bacteria: repeat domains direct autolysin to the equatorial surface ring of RT Staphylococcus aureus."; RL EMBO J. 17:4639-4646(1998). RN [8] RP BINDING TO THE BACTERIAL CELL WALL. RX PubMed=10941929; DOI=10.1111/j.1348-0421.2000.tb02521.x; RA Takano M., Oshida T., Yasojima A., Yamada M., Okagaki C., Sugai M., RA Suginaka H., Matsushita T.; RT "Modification of autolysis by synthetic peptides derived from the RT presumptive binding domain of Staphylococcus aureus autolysin."; RL Microbiol. Immunol. 44:463-472(2000). CC -!- FUNCTION: Endohydrolysis of the di-N-acetylchitobiosyl unit in high- CC mannose glycopeptides and glycoproteins containing the CC -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue CC remains attached to the protein; the rest of the oligosaccharide is CC released intact. Cleaves the peptidoglycan connecting the daughter CC cells at the end of the cell division cycle, resulting in the CC separation of the two newly divided cells. Acts as an autolysin in CC penicillin-induced lysis. {ECO:0000269|PubMed:7883705}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L- CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28; CC -!- CATALYTIC ACTIVITY: CC Reaction=an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta- CC D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl- CC [protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]- CC beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L- CC asparaginyl-[protein]; Xref=Rhea:RHEA:73067, Rhea:RHEA-COMP:12603, CC Rhea:RHEA-COMP:18176, ChEBI:CHEBI:15377, ChEBI:CHEBI:132248, CC ChEBI:CHEBI:192714, ChEBI:CHEBI:192715; EC=3.2.1.96; CC -!- SUBUNIT: Oligomer; forms a ring structure at the cell surface which is CC important for efficient partitioning of daughter cells after cell CC division. {ECO:0000269|PubMed:8626282}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8626282, CC ECO:0000269|PubMed:9139914, ECO:0000269|PubMed:9251058}. Note=Secreted, CC and then anchored on the cell surface at the peripheral cell wall above CC the completed septum (septal region), for the next cell division cycle. CC -!- DOMAIN: The GW domains are responsible for directing the proteins to CC the septal region. {ECO:0000269|PubMed:9707423}. CC -!- PTM: Undergoes proteolytic processing to generate the two extracellular CC lytic enzymes, probably at the septal region on the cell surface. CC -!- SIMILARITY: In the N-terminal section; belongs to the N-acetylmuramoyl- CC L-alanine amidase 2 family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl CC hydrolase 73 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAP44166.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF537210; AAP44166.1; ALT_INIT; Genomic_DNA. DR EMBL; D42078; BAA22600.1; -; Genomic_DNA. DR AlphaFoldDB; P0C5Z8; -. DR SMR; P0C5Z8; -. DR CAZy; GH73; Glycoside Hydrolase Family 73. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004040; F:amidase activity; IEA:InterPro. DR GO; GO:0033925; F:mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity; IEA:UniProtKB-EC. DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro. DR CDD; cd06583; PGRP; 1. DR Gene3D; 1.10.530.10; -; 1. DR Gene3D; 2.30.30.170; -; 7. DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1. DR InterPro; IPR036505; Amidase/PGRP_sf. DR InterPro; IPR002502; Amidase_domain. DR InterPro; IPR025987; GW_dom. DR InterPro; IPR038200; GW_dom_sf. DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom. DR PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1. DR PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1. DR Pfam; PF01510; Amidase_2; 1. DR Pfam; PF01832; Glucosaminidase; 1. DR Pfam; PF13457; GW; 6. DR SMART; SM00644; Ami_2; 1. DR SMART; SM00047; LYZ2; 1. DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1. DR SUPFAM; SSF82057; Prokaryotic SH3-related domain; 1. DR PROSITE; PS51780; GW; 7. PE 1: Evidence at protein level; KW Cell wall biogenesis/degradation; Hydrolase; Multifunctional enzyme; KW Repeat; Secreted; Signal. FT SIGNAL 1..36 FT /evidence="ECO:0000255" FT CHAIN 37..1255 FT /note="Bifunctional autolysin" FT /id="PRO_0000012114" FT DOMAIN 442..516 FT /note="GW 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116" FT DOMAIN 518..592 FT /note="GW 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116" FT DOMAIN 611..685 FT /note="GW 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116" FT DOMAIN 687..761 FT /note="GW 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116" FT DOMAIN 783..858 FT /note="GW 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116" FT DOMAIN 860..935 FT /note="GW 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116" FT DOMAIN 942..1016 FT /note="GW 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116" FT REGION 110..141 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 193..218 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 199..775 FT /note="N-acetylmuramoyl-L-alanine amidase" FT REGION 776..1255 FT /note="Endo-beta-N-acetylglucosaminidase" FT CONFLICT 932 FT /note="A -> R (in Ref. 2; BAA22600)" FT /evidence="ECO:0000305" SQ SEQUENCE 1255 AA; 137535 MW; 7257DD87168AAE7D CRC64; MLGVINRMAK KFNYKLPSMV ALTLVGSAVT AHQVQAAETT QDQTTNKNVL DSNKVKATTE QAKAEVKNPT QNISGTQVYQ DPAIVQPKTA NNKTGNAQVS QKVDTAQVNG DTRANQSATT NNTQPVAKST STTAPKTNTN VTNAGYSLVD DEDDNSEHQI NPELIKSAAK PAALETQYKA AAPKAKTEAT PKVTTFSASA QPRSVAATPK TSLPKYKPQV NSSINDYIRK NNLKAPKIEE DYTSYFPKYA YRNGVGRPEG IVVHDTANDR STINGEISYM KNNYQNAFVH AFVDGDRIIE TAPTDYLSWG VGAVGNPRFI NVEIVHTHDY ASFARSMNNY ADYAATQLQY YGLKPDSAEY DGNGTVWTHY AVSKYLGGTD HADPHGYLRS HNYSYDQLYD LINEKYLIKM GKVAPWGTQF TTTPTTPSKP TTPSKPSTGK LTVAANNGVA QIKPTNSGLY TTVYDKTGKA TNEVQKTFAV SKTATLGNQK FYLVQDYNSG NKFGWVKEGD VVYNTAKSPV NVNQSYSIKS GTKLYTVPWG TSKQVAGSVS GSGNQTFKAS KQQQIDKSIY LYGSVNGKSG WVSKAYLVDT AKPTPTPIPK PSTPTTNNKL TVSSLNGVAQ INAKNNGLFT TVYDKTGKPT KEVQKTFAVT KEASLGGNKF YLVKDYNSPT LIGWVKQGDV IYNNAKSPVN VMQTYTVKPG TKLYSVPWGT YKQEAGAVSG TGNQTFKATK QQQIDKSIYL FGTVNGKSGW VSKAYLAVPA APKKAVAQPK TAVKAYTVTK PQTTQTVSKI AQVKPNNTGI RASVYEKTAK NGAKYADRTF YVTKERAHGN ETYVLLNNTS HNIPLGWFNV KDLNVQNLGK EVKTTQKYTV NKSNNGLSMV PWGTKNQVIL TGNNIAQGTF NATKQVSVGK DVYLYGTINN RTGWVNAKDL TAPTAVKPTT SAAKDYNYTY VIKNGNGYYY VTPNSDTAKY SLKAFNEQPF AVVKEQVING QTWYYGKLSN GKLAWIKSTD LAKELIKYNQ TGMTLNQVAQ IQAGLQYKPQ VQRVPGKWTD ANFNDVKHAM DTKRLAQDPA LKYQFLRLDQ PQNISIDKIN QFLKGKGVLE NQGAAFNKAA QMYGINEVYL ISHALLETGN GTSQLAKGAD VVNNKVVTNS NTKYHNVFGI AAYDNDPLRE GIKYAKQAGW DTVSKAIVGG AKFIGNSYVK AGQNTLYKMR WNPAHPGTHQ YATDVDWANI NAKIIKGYYD KIGEVGKYFD IPQYK //