ATL_STAAS
ID ATL_STAAS Reviewed; 1250 AA.
AC Q6GAG0;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=SAS0988;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
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=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: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; BX571857; CAG42763.1; -; Genomic_DNA.
DR RefSeq; WP_001074541.1; NC_002953.3.
DR AlphaFoldDB; Q6GAG0; -.
DR SMR; Q6GAG0; -.
DR CAZy; GH73; Glycoside Hydrolase Family 73.
DR KEGG; sas:SAS0988; -.
DR HOGENOM; CLU_005906_0_0_9; -.
DR OMA; FPKYGYR; -.
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 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..1250
FT /note="Bifunctional autolysin"
FT /id="PRO_0000045477"
FT DOMAIN 437..511
FT /note="GW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 513..587
FT /note="GW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 606..680
FT /note="GW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 682..756
FT /note="GW 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 778..853
FT /note="GW 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 855..930
FT /note="GW 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 937..1011
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 173..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..769
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT REGION 770..1250
FT /note="Endo-beta-N-acetylglucosaminidase"
FT COMPBIAS 103..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1250 AA; 136868 MW; D8C43606B9374D96 CRC64;
MAKKFNYKLP SMVALTLVGS AVTAHQVQAA ETTQDQTTNK NVLDSNKVKA TTEQAKAEVK
NPTQNISGTQ VYQDPAIVQP KTANNKTGNA QVSQKVDTAQ VNGDTRANQS ATTNNTQPVA
KSTSTTAPKT NTNVTNAGYS LVDDEDDNSE NQINPELIKS AAKPAALETQ YKAAAPKAAT
TSAPKAKTEA TPKVTTFSAS AQPRSVAATP KTSLPKYKPQ VNSSINDYIR KNNLKAPKIE
EDYTSYFPKY AYRNGVGRPE GIVVHDTAND RSTINGEISY MKNNYQNAFV HAFVDGDRII
ETAPTDYLSW GVGAVGNPRF INVEIVHTHD YASFARSMNN YADYAATQLQ YYGLKPDSAE
YDGNGTVWTH YAVSKYLGGT DHADPHGYLR SHNYSYDQLY DLINEKYLIK MGKVAPWGTQ
STTTPTTPSK PSTGKLTVAA NNGVAQIKPT NSGLYTTVYD KTGKATNEVQ KTFAVSKTAT
LGNQKFYLVQ DYNSGNKFGW VKEGDVVYNT AKSPVNVNQS YSIKPGTKLY TVPWGTSKQV
AGSVSGSGNQ TFKASKQQQI DKSIYLYGSV NGKSGWVSKA YLVDTAKPTP TPTPKPSTPT
TNNKLTVSSL NGVAQINAKN NGLFTTVYDK TGKPTKEVQK TFAVTKEASL GGNKFYLVKD
YNSPTLIGWV KQGDVIYNNA KSPVNVMQTY TVKPGTKLYS VPWGTYKQEA GAVSGTGNQT
FKATKQQQID KSIYLFGTVN GKSGWVSKAY LAVPAAPKKA VAQPKTAVKA YTVTKPQTTQ
TVSKIAQVKP NNTGIRASVY EKTAKNGAKY ADRTFYVTKE RAHGNETYVL LNNTSHNIPL
GWFNVKDLNV QNLGKEVKTT QKYTVNKSNN GLSMVPWGTK NQVILTGNNI AQGTFNATKQ
VSVGKDVYLY GTINNRTGWV NAKDLTAPTA VKPTTSAAKD YNYTYVIKNG NGYYYVTPNS
DTAKYSLKAF NEQPFAVVKE QVINEQTWYY GKLSNGKLAW IKSTDLAKEL IKYNQTGMTL
NQVAQIQAGL QYKPQVQRVP GKWTDANFND VKHAMDTKRL AQDPALKYQF LRLDQPQNIS
IDKINQFLKG KGVLENQGAA FNKAAQMYGI NEVYLISHAL LETGNGTSQL AKGADVVNNK
VVTNSNTKYH NVFGIAAYDN DPLREGIKYA KQAGWDTVSK AIVGGAKFIG NSYVKAGQNT
LYKMRWNPAH PGTHQYATDI DWANINAKII KGYYDKIGEV GKYFDIPQYK
