ID   ATL_STAA8               Reviewed;        1256 AA.
AC   Q2FZK7; O32391; P52081; Q7WTC6; Q7WY94; Q7WY95;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, 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=SAOUHSC_00994;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 205-214 AND
RP   776-792.
RX   PubMed=7816834; DOI=10.1073/pnas.92.1.285;
RA   Oshida T., Sugai M., Komatsuzawa H., Hong Y.-M., Suginaka H., Tomasz A.;
RT   "A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine
RT   amidase domain and an endo-beta-N-acetylglucosaminidase domain: cloning,
RT   sequence analysis, and characterization.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:285-289(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Foster S.J.;
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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; D17366; BAA04185.1; -; Genomic_DNA.
DR   EMBL; L41499; AAA99982.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD30118.1; -; Genomic_DNA.
DR   RefSeq; WP_001074547.1; NZ_LS483365.1.
DR   RefSeq; YP_499546.1; NC_007795.1.
DR   PDB; 4KNK; X-ray; 1.12 A; A/B=198-421.
DR   PDB; 4KNL; X-ray; 1.55 A; A/B/C/D=198-421.
DR   PDBsum; 4KNK; -.
DR   PDBsum; 4KNL; -.
DR   AlphaFoldDB; Q2FZK7; -.
DR   SMR; Q2FZK7; -.
DR   STRING; 93061.SAOUHSC_00994; -.
DR   CAZy; GH73; Glycoside Hydrolase Family 73.
DR   PaxDb; 1280-SAXN108_1050; -.
DR   GeneID; 3920394; -.
DR   KEGG; sao:SAOUHSC_00994; -.
DR   PATRIC; fig|93061.5.peg.912; -.
DR   eggNOG; COG3266; Bacteria.
DR   eggNOG; COG4193; Bacteria.
DR   eggNOG; COG5632; Bacteria.
DR   HOGENOM; CLU_005906_0_0_9; -.
DR   OrthoDB; 9816557at2; -.
DR   Proteomes; UP000008816; 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   1: Evidence at protein level;
KW   3D-structure; Cell wall biogenesis/degradation; Direct protein sequencing;
KW   Hydrolase; Multifunctional enzyme; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..1256
FT                   /note="Bifunctional autolysin"
FT                   /id="PRO_0000247668"
FT   DOMAIN          443..517
FT                   /note="GW 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          519..593
FT                   /note="GW 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          612..686
FT                   /note="GW 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          688..762
FT                   /note="GW 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          784..859
FT                   /note="GW 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          861..936
FT                   /note="GW 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          943..1017
FT                   /note="GW 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   REGION          103..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..775
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT   REGION          419..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          776..1256
FT                   /note="Endo-beta-N-acetylglucosaminidase"
FT   COMPBIAS        103..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           224..231
FT                   /evidence="ECO:0007829|PDB:4KNK"
FT   STRAND          239..241
FT                   /evidence="ECO:0007829|PDB:4KNK"
FT   STRAND          261..266
FT                   /evidence="ECO:0007829|PDB:4KNK"
FT   HELIX           274..284
FT                   /evidence="ECO:0007829|PDB:4KNK"
FT   TURN            285..287
FT                   /evidence="ECO:0007829|PDB:4KNK"
FT   STRAND          291..294
FT                   /evidence="ECO:0007829|PDB:4KNK"
FT   STRAND          299..301
FT                   /evidence="ECO:0007829|PDB:4KNK"
FT   STRAND          310..312
FT                   /evidence="ECO:0007829|PDB:4KNK"
FT   HELIX           313..316
FT                   /evidence="ECO:0007829|PDB:4KNK"
FT   TURN            317..319
FT                   /evidence="ECO:0007829|PDB:4KNK"
FT   STRAND          320..325
FT                   /evidence="ECO:0007829|PDB:4KNK"
FT   HELIX           331..352
FT                   /evidence="ECO:0007829|PDB:4KNK"
FT   TURN            360..362
FT                   /evidence="ECO:0007829|PDB:4KNK"
FT   STRAND          365..369
FT                   /evidence="ECO:0007829|PDB:4KNK"
FT   HELIX           370..376
FT                   /evidence="ECO:0007829|PDB:4KNK"
FT   HELIX           386..391
FT                   /evidence="ECO:0007829|PDB:4KNK"
FT   HELIX           396..410
FT                   /evidence="ECO:0007829|PDB:4KNK"
SQ   SEQUENCE   1256 AA;  137384 MW;  2BB76CAA292FDD20 CRC64;
     MAKKFNYKLP SMVALTLVGS AVTAHQVQAA ETTQDQTTNK NVLDSNKVKA TTEQAKAEVK
     NPTQNISGTQ VYQDPAIVQP KTANNKTGNA QVSQKVDTAQ VNGDTRANQS ATTNNTQPVA
     KSTSTTAPKT NTNVTNAGYS LVDDEDDNSE NQINPELIKS AAKPAALETQ YKTAAPKAAT
     TSAPKAKTEA TPKVTTFSAS AQPRSVAATP KTSLPKYKPQ VNSSINDYIC KNNLKAPKIE
     EDYTSYFPKY AYRNGVGRPE GIVVHDTAND RSTINGEISY MKNNYQNAFV HAFVDGDRII
     ETAPTDYLSW GVGAVGNPRF INVEIVHTHD YASFARSMNN YADYAATQLQ YYGLKPDSAE
     YDGNGTVWTH YAVSKYLGGT DHADPHGYLR SHNYSYDQLY DLINEKYLIK MGKVAPWGTQ
     STTTPTTPSK PTTPSKPSTG KLTVAANNGV AQIKPTNSGL YTTVYDKTGK ATNEVQKTFA
     VSKTATLGNQ KFYLVQDYNS GNKFGWVKEG DVVYNTAKSP VNVNQSYSIK PGTKLYTVPW
     GTSKQVAGSV SGSGNQTFKA SKQQQIDKSI YLYGSVNGKS GWVSKAYLVD TAKPTPTPTP
     KPSTPTTNNK LTVSSLNGVA QINAKNNGLF TTVYDKTGKP TKEVQKTFAV TKEASLGGNK
     FYLVKDYNSP TLIGWVKQGD VIYNNAKSPV NVMQTYTVKP GTKLYSVPWG TYKQEAGAVS
     GTGNQTFKAT KQQQIDKSIY LFGTVNGKSG WVSKAYLAVP AAPKKAVAQP KTAVKAYTVT
     KPQTTQTVSK IAQVKPNNTG IRASVYEKTA KNGAKYADRT FYVTKERAHG NETYVLLNNT
     SHNIPLGWFN VKDLNVQNLG KEVKTTQKYT VNKSNNGLSM VPWGTKNQVI LTGNNIAQGT
     FNATKQVSVG KDVYLYGTIN NRTGWVNAKD LTAPTAVKPT TSAAKDYNYT YVIKNGNGYY
     YVTPNSDTAK YSLKAFNEQP FAVVKEQVIN GQTWYYGKLS NGKLAWIKST DLAKELIKYN
     QTGMTLNQVA QIQAGLQYKP QVQRVPGKWT DAKFNDVKHA MDTKRLAQDP ALKYQFLRLD
     QPQNISIDKI NQFLKGKGVL ENQGAAFNKA AQMYGINEVY LISHALLETG NGTSQLAKGA
     DVVNNKVVTN SNTKYHNVFG IAAYDNDPLR EGIKYAKQAG WDTVSKAIVG GAKFIGNSYV
     KAGQNTLYKM RWNPAHPGTH QYATDVDWAN INAKIIKGYY DKIGEVGKYF DIPQYK
//