ATL_STAAR
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 03-AUG-2022, entry version 101.
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; Firmicutes; 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=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; 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 OMA; FPKYGYR; -.
DR OrthoDB; 682655at2; -.
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; 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..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
