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Bifunctional autolysin [Includes: N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28); Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase (EC 3.2.1.96)]

 ATL_STAAU               Reviewed;        1255 AA.
P0C5Z8; O32391; P0C1R4; P52081; Q7WTC6; Q7WY94; Q7WY95;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
15-JAN-2008, sequence version 1.
28-MAR-2018, entry version 56.
RecName: Full=Bifunctional autolysin;
Includes:
RecName: Full=N-acetylmuramoyl-L-alanine amidase;
EC=3.5.1.28;
Includes:
RecName: Full=Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase;
EC=3.2.1.96;
Flags: Precursor;
Name=atl; Synonyms=nag;
Staphylococcus aureus.
Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
Staphylococcus.
NCBI_TaxID=1280;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=IL-A;
PubMed=12760894; DOI=10.1128/AAC.47.6.2036-2039.2003;
Boyle-Vavra S., Challapalli M., Daum R.S.;
"Resistance to autolysis in vancomycin-selected Staphylococcus aureus
isolates precedes vancomycin-intermediate resistance.";
Antimicrob. Agents Chemother. 47:2036-2039(2003).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 775-1255.
Kamitani S., Minamide W., Yutsudo T., Noda M.;
"Novel cytotoxin in a clinical isolate of methicillin-resistant S.
aureus: cloning, sequencing and expression.";
Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION.
STRAIN=ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447;
PubMed=7883705; DOI=10.1128/jb.177.6.1491-1496.1995;
Sugai M., Komatsuzawa H., Akiyama T., Hong Y.-M., Oshida T.,
Miyake Y., Yamaguchi T., Suginaka H.;
"Identification of endo-beta-N-acetylglucosaminidase and N-
acetylmuramyl-L-alanine amidase as cluster-dispersing enzymes in
Staphylococcus aureus.";
J. Bacteriol. 177:1491-1496(1995).
[4]
SUBCELLULAR LOCATION, AND SUBUNIT.
STRAIN=ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447;
PubMed=8626282; DOI=10.1128/jb.178.6.1565-1571.1996;
Yamada S., Sugai M., Komatsuzawa H., Nakashima S., Oshida T.,
Matsumoto A., Suginaka H.;
"An autolysin ring associated with cell separation of Staphylococcus
aureus.";
J. Bacteriol. 178:1565-1571(1996).
[5]
SUBCELLULAR LOCATION.
STRAIN=ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447;
PubMed=9251058; DOI=10.1111/j.1348-0421.1997.tb01880.x;
Komatsuzawa H., Sugai M., Nakashima S., Yamada S., Matsumoto A.,
Oshida T., Suginaka H.;
"Subcellular localization of the major autolysin, ATL and its
processed proteins in Staphylococcus aureus.";
Microbiol. Immunol. 41:469-479(1997).
[6]
SUBCELLULAR LOCATION.
STRAIN=ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447;
PubMed=9139914; DOI=10.1128/jb.179.9.2958-2962.1997;
Sugai M., Yamada S., Nakashima S., Komatsuzawa H., Matsumoto A.,
Oshida T., Suginaka H.;
"Localized perforation of the cell wall by a major autolysin: atl gene
products and the onset of penicillin-induced lysis of Staphylococcus
aureus.";
J. Bacteriol. 179:2958-2962(1997).
[7]
ROLE OF REPEATS IN LOCALIZATION AT THE SEPTAL REGION.
STRAIN=OS2;
PubMed=9707423; DOI=10.1093/emboj/17.16.4639;
Baba T., Schneewind O.;
"Targeting of muralytic enzymes to the cell division site of Gram-
positive bacteria: repeat domains direct autolysin to the equatorial
surface ring of Staphylococcus aureus.";
EMBO J. 17:4639-4646(1998).
[8]
BINDING TO THE BACTERIAL CELL WALL.
PubMed=10941929;
Takano M., Oshida T., Yasojima A., Yamada M., Okagaki C., Sugai M.,
Suginaka H., Matsushita T.;
"Modification of autolysis by synthetic peptides derived from the
presumptive binding domain of Staphylococcus aureus autolysin.";
Microbiol. Immunol. 44:463-472(2000).
-!- FUNCTION: Endohydrolysis 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.
{ECO:0000269|PubMed:7883705}.
-!- CATALYTIC ACTIVITY: Hydrolyzes the link between N-acetylmuramoyl
residues and L-amino acid residues in certain cell-wall
glycopeptides.
-!- CATALYTIC ACTIVITY: Endohydrolysis of the N,N'-diacetylchitobiosyl
unit in high-mannose glycopeptides and glycoproteins containing
the -(Man(GlcNAc)(2))Asn-structure. One N-acetyl-D-glucosamine
residue remains attached to the protein; the rest of the
oligosaccharide is released intact.
-!- SUBUNIT: Oligomer; forms a ring structure at the cell surface
which is important for efficient partitioning of daughter cells
after cell division. {ECO:0000269|PubMed:8626282}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8626282,
ECO:0000269|PubMed:9139914, ECO:0000269|PubMed:9251058}.
Note=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.
-!- DOMAIN: The GW domains are responsible for directing the proteins
to the septal region. {ECO:0000269|PubMed:9707423}.
-!- PTM: Undergoes proteolytic processing to generate the two
extracellular lytic enzymes, probably at the septal region on the
cell surface.
-!- SIMILARITY: In the N-terminal section; belongs to the N-
acetylmuramoyl-L-alanine amidase 2 family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
hydrolase 73 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAP44166.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF537210; AAP44166.1; ALT_INIT; Genomic_DNA.
EMBL; D42078; BAA22600.1; -; Genomic_DNA.
ProteinModelPortal; P0C5Z8; -.
SMR; P0C5Z8; -.
CAZy; GH73; Glycoside Hydrolase Family 73.
eggNOG; ENOG4108FQ0; Bacteria.
eggNOG; COG4193; LUCA.
eggNOG; COG5632; LUCA.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004040; F:amidase activity; IEA:InterPro.
GO; GO:0033925; F:mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity; IEA:UniProtKB-EC.
GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
CDD; cd06583; PGRP; 1.
Gene3D; 2.30.30.170; -; 7.
Gene3D; 3.40.80.10; -; 1.
InterPro; IPR036505; Amidase/PGRP_sf.
InterPro; IPR002502; Amidase_domain.
InterPro; IPR025987; GW_dom.
InterPro; IPR038200; GW_dom_sf.
InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
Pfam; PF01832; Glucosaminidase; 1.
Pfam; PF13457; SH3_8; 6.
SMART; SM00644; Ami_2; 1.
SMART; SM00047; LYZ2; 1.
SUPFAM; SSF55846; SSF55846; 1.
PROSITE; PS51780; GW; 7.
1: Evidence at protein level;
Cell wall biogenesis/degradation; Hydrolase; Multifunctional enzyme;
Repeat; Secreted; Signal.
SIGNAL 1 36 {ECO:0000255}.
CHAIN 37 1255 Bifunctional autolysin.
/FTId=PRO_0000012114.
DOMAIN 442 516 GW 1. {ECO:0000255|PROSITE-
ProRule:PRU01116}.
DOMAIN 518 592 GW 2. {ECO:0000255|PROSITE-
ProRule:PRU01116}.
DOMAIN 611 685 GW 3. {ECO:0000255|PROSITE-
ProRule:PRU01116}.
DOMAIN 687 761 GW 4. {ECO:0000255|PROSITE-
ProRule:PRU01116}.
DOMAIN 783 858 GW 5. {ECO:0000255|PROSITE-
ProRule:PRU01116}.
DOMAIN 860 935 GW 6. {ECO:0000255|PROSITE-
ProRule:PRU01116}.
DOMAIN 942 1016 GW 7. {ECO:0000255|PROSITE-
ProRule:PRU01116}.
REGION 199 775 N-acetylmuramoyl-L-alanine amidase.
REGION 776 1255 Endo-beta-N-acetylglucosaminidase.
CONFLICT 932 932 A -> R (in Ref. 2; BAA22600).
{ECO:0000305}.
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


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