ATL_STAA8
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 03-AUG-2022, entry version 98.
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; Firmicutes; 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=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; 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; 1280.SAXN108_1050; -.
DR CAZy; GH73; Glycoside Hydrolase Family 73.
DR EnsemblBacteria; ABD30118; ABD30118; SAOUHSC_00994.
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 OMA; FPKYGYR; -.
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; 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 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
