ID   ATL_STAAN               Reviewed;        1248 AA.
AC   Q99V41;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 120.
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=SA0905;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB42150.1; -; Genomic_DNA.
DR   PIR; C89874; C89874.
DR   RefSeq; WP_001074534.1; NC_002745.2.
DR   AlphaFoldDB; Q99V41; -.
DR   SMR; Q99V41; -.
DR   CAZy; GH73; Glycoside Hydrolase Family 73.
DR   EnsemblBacteria; BAB42150; BAB42150; BAB42150.
DR   KEGG; sau:SA0905; -.
DR   HOGENOM; CLU_005906_0_0_9; -.
DR   Proteomes; UP000000751; 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   Cell wall biogenesis/degradation; Hydrolase; Multifunctional enzyme;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..1248
FT                   /note="Bifunctional autolysin"
FT                   /id="PRO_0000045475"
FT   DOMAIN          435..509
FT                   /note="GW 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          511..585
FT                   /note="GW 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          604..678
FT                   /note="GW 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          680..754
FT                   /note="GW 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          776..851
FT                   /note="GW 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          853..928
FT                   /note="GW 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   DOMAIN          935..1009
FT                   /note="GW 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT   REGION          103..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..767
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT   REGION          768..1248
FT                   /note="Endo-beta-N-acetylglucosaminidase"
SQ   SEQUENCE   1248 AA;  136751 MW;  701B54EE6152275E CRC64;
     MAKKFNYKLP SMVALTLVGS AVTAHQVQAA ETTQDQTTNK NVLDSNKVKA TTEQAKAEVK
     NPTQNISGTQ VYQDPAIVQP KTANNKTGNA QVSQKVDTAQ VNGDTRANQS ATTNNTQPVA
     KSTSTTAPKT NTNVTNAGYS LVDDEDDNSE HQINPELIKS AAKPAALETQ YKAAAPKAKT
     EATPKVTTFS ASAQPRSVAA TPKTSLPKYK PQVNSSINDY IRKNNLKAPK IEEDYTSYFP
     KYAYRNGVGR PEGIVVHDTA NDRSTINGEI SYMKNNYQNA FVHAFVDGDR IIETAPTDYL
     SWGVGAVGNP RFINVEIVHT HDYASFARSM NNYADYAATQ LQYYGLKPDS AEYDGNGTVW
     THYAVSKYLG GTDHADPHGY LRSHNYSYDQ LYDLINEKYL IKMGKVAPWG TQFTTTPTTP
     SKPTTPSKPS TGKLTVAANN GVAQIKPTNS GLYTTVYDKT GKATNEVQKT FAVSKTATLG
     NQKFYLVQDY NSGNKFGWVK EGDVVYNTAK SPVNVNQSYS IKSGTKLYTV PWGTSKQVAG
     SVSGSGNQTF KASKQQQIDK SIYLYGSVNG KSGWVSKAYL VDTAKPTPTP IPKPSTPTTN
     NKLTVSSLNG VAQINAKNNG LFTTVYDKTG KPTKEVQKTF AVTKEASLGG NKFYLVKDYN
     SPTLIGWVKQ GDVIYNNAKS PVNVMQTYTV KPGTKLYSVP WGTYKQEAGA VSGTGNQTFK
     ATKQQQIDKS IYLFGTVNGK SGWVSKAYLA VPAAPKKAVA QPKTAVKAYT VTKPQTTQTV
     SKIAQVKPNN TGIRASVYEK TAKNGAKYAD RTFYVTKERA HGNETYVLLN NTSHNIPLGW
     FNVKDLNVQN LGKEVKTTQK YTVNKSNNGL SMVPWGTKNQ VILTGNNIAQ GTFNATKQVS
     VGKDVYLYGT INNRTGWVNA KDLTAPTAVK PTTSAAKDYN YTYVIKNGNG YYYVTPNSDT
     AKYSLKAFNE QPFAVVKEQV INGQTWYYGK LSNGKLAWIK STDLAKELIK YNQTGMTLNQ
     VAQIQAGLQY KPQVQRVPGK WTDANFNDVK HAMDTKRLAQ DPALKYQFLR LDQPQNISID
     KINQFLKGKG VLENQGAAFN KAAQMYGINE VYLISHALLE TGNGTSQLAK GADVVNNKVV
     TNSNTKYHNV FGIAAYDNDP LREGIKYAKQ AGWDTVSKAI VGGAKFIGNS YVKAGQNTLY
     KMRWNPAHPG THQYATDVDW ANINAKIIKG YYDKIGEVGK YFDIPQYK
//