ATL_STAAU
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 03-AUG-2022, entry version 66.
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; Firmicutes; 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 / NCTC
RC 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 / NCTC
RC 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 / NCTC
RC 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 / NCTC
RC 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=Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-
CC mannose glycopeptides and glycoproteins containing the
CC -[Man(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.; 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};
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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; 2.30.30.170; -; 7.
DR Gene3D; 3.40.80.10; -; 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 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; SSF55846; 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
