ID   ATL_STAAR               Reviewed;        1257 AA.
AC   Q6GI31;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 105.
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; OrderedLocusNames=SAR1026;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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 (By similarity). {ECO:0000250}.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted, and then
CC       anchored on the cell surface at the peripheral cell wall above the
CC       completed septum (septal region), for the next cell division cycle.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The GW domains are responsible for directing the proteins to
CC       the septal region. {ECO:0000250}.
CC   -!- PTM: Undergoes proteolytic processing to generate the two extracellular
CC       lytic enzymes, probably at the septal region on the cell surface.
CC       {ECO:0000250}.
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}.
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DR   EMBL; BX571856; CAG40030.1; -; Genomic_DNA.
DR   RefSeq; WP_001074519.1; NC_002952.2.
DR   AlphaFoldDB; Q6GI31; -.
DR   SMR; Q6GI31; -.
DR   CAZy; GH73; Glycoside Hydrolase Family 73.
DR   KEGG; sar:SAR1026; -.
DR   HOGENOM; CLU_005906_0_0_9; -.
DR   Proteomes; UP000000596; Chromosome.
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   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Hydrolase; Multifunctional enzyme;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..1257
FT                   /note="Bifunctional autolysin"
FT                   /id="PRO_0000045476"
FT   DOMAIN          444..518
FT                   /note="GW 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          520..594
FT                   /note="GW 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          613..687
FT                   /note="GW 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          689..763
FT                   /note="GW 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          785..860
FT                   /note="GW 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          862..937
FT                   /note="GW 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          944..1018
FT                   /note="GW 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   REGION          99..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..776
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT   REGION          417..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          777..1257
FT                   /note="Endo-beta-N-acetylglucosaminidase"
FT   COMPBIAS        99..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1257 AA;  137528 MW;  8CEB3DB932B1720D CRC64;
     MAKKFNYKLP SMVALTLVGS AVTAHQVQAA ETTQDQTTNK NVLDSNKVKA TTEQAKAEVK
     NPTQNISGTQ VYQDPAIVQP KAANKTGNAQ VNQKVDTTQV NGDTRATQST TSNNAKPVTK
     STNTTAPKTN NNVTSAGYSL VDDEDDNSEN QINPELIKSA AKPAALETQY KAAAPKATPV
     APKAKTEATP KVTTFSASAQ PRSAAAAPKT SLPKYKPQVN SSINDYIRKN NLKAPKIEED
     YTSYFPKYAY RNGVGRPEGI VVHDTANDRS TINGEISYMK NNYQNAFVHA FVDGDRIIET
     APTDYLSWGV GAVGNPRFIN VEIVHTHDYA SFARSMNNYA DYAATQLQYY GLKPDSAEYD
     GNGTVWTHYA VSKYLGGTDH ADPHGYLRSH NYSYDQLYDL INEKYLIKMG KVAPWGTQST
     TTPTTPSKPS TPSKPSTPST GKLTVAANNG VAQIKPTNSG LYTTVYDKTG KATNEVQKTF
     AVSKTATLGN QKFYLVQDYN SGNKFGWVKE GDVVYNTAKS PVNVNQSYSI KPGTKLYTVP
     WGTSKQVAGS VSGSGNQTFK ASKQQQIDKS IYLYGSVNGK SGWVSKAYLV DTAKPTPTPT
     PKPSTPTTNN KLTVSSLNGV AQINAKNNGL FTTVYDKTGK PTKEVQKTFA VTKEASLGGN
     KFYLVKDYNS PTLIGWVKQG DVIYNNAKSP VNVMQTYTVK PGTKLYSVPW GTYKQEAGAV
     SGTGNQTFKA TKQQQIDKSI YLYGTVNGKS GWISKAYLAV PAAPKKAVAQ PKTAVKAYAV
     TKPQTTQTVS KIAQVKPNNT GIRASVYEKT AKNGAKYADR TFYVTKERAH GNETYVLLNN
     TSHNIPLGWF NVKDLNVQNL GKEVKTTQKY TVNRSNNGLS MVPWGTKNQV ILTGNNIAQG
     TFNATKQVSV GKDVYLYGTI NNRTGWVNSK DLTAPTAVKP TTSAAKDYNY TYVIKNGNGY
     YYVTPNSDTA KYSLKAFNEQ PFAVVKEQVI NGQTWYYGKL SNGKLAWIKS TDLAKELIKY
     NQIGMTLNQV AQIQAGLQYK PQVQRVPGKW TDANFNDVKH AMDTKRLAQD PALKYQFLRL
     DQPQNISIDK INQFLKGKGV LENQGAAFNK AAQMYGINEV YLISHALLET GNGTSQLAKG
     ADVVNNKVVT NSNTKYHNVF GIAAYDNDPL REGIKYAKQA GWDTVSKAIV GGAKFIGNSY
     VKAGQNTLYK MRWNPAHPGT HQYATDVDWA NINAKIIKGY YDKIGEVGKY FDIPQYK
//