ATL_STAAM
ID ATL_STAAM Reviewed; 1248 AA.
AC Q931U5; Q7WY94; Q7WY95;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 115.
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=SAV1052;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 785-1248.
RA Wootton M., Avison M.B., Bennett P.M., Howe R.A., MacGowan A.P.,
RA Walsh T.R.;
RT "Genetic analysis of seventeen genes in Staphylococcus aureus with reduced
RT susceptibility to vancomycin (VRSA) and heteroVRSA (hVRSA).";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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; BA000017; BAB57214.2; -; Genomic_DNA.
DR EMBL; AJ567416; CAD98826.1; -; Genomic_DNA.
DR RefSeq; WP_001074534.1; NC_002758.2.
DR PDB; 6FXO; X-ray; 2.28 A; A=1007-1248.
DR PDBsum; 6FXO; -.
DR AlphaFoldDB; Q931U5; -.
DR SMR; Q931U5; -.
DR CAZy; GH73; Glycoside Hydrolase Family 73.
DR PaxDb; Q931U5; -.
DR EnsemblBacteria; BAB57214; BAB57214; SAV1052.
DR KEGG; sav:SAV1052; -.
DR HOGENOM; CLU_005906_0_0_9; -.
DR OMA; FPKYGYR; -.
DR BioCyc; SAUR158878:SAV_RS05680-MON; -.
DR Proteomes; UP000002481; 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; Hydrolase;
KW Multifunctional enzyme; Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1248
FT /note="Bifunctional autolysin"
FT /id="PRO_0000045474"
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 /evidence="ECO:0000250"
FT REGION 768..1248
FT /note="Endo-beta-N-acetylglucosaminidase"
FT /evidence="ECO:0000250"
FT STRAND 1008..1013
FT /evidence="ECO:0007829|PDB:6FXO"
FT HELIX 1018..1026
FT /evidence="ECO:0007829|PDB:6FXO"
FT HELIX 1046..1053
FT /evidence="ECO:0007829|PDB:6FXO"
FT HELIX 1055..1060
FT /evidence="ECO:0007829|PDB:6FXO"
FT HELIX 1064..1068
FT /evidence="ECO:0007829|PDB:6FXO"
FT HELIX 1079..1086
FT /evidence="ECO:0007829|PDB:6FXO"
FT HELIX 1096..1106
FT /evidence="ECO:0007829|PDB:6FXO"
FT HELIX 1110..1120
FT /evidence="ECO:0007829|PDB:6FXO"
FT TURN 1121..1125
FT /evidence="ECO:0007829|PDB:6FXO"
FT HELIX 1127..1130
FT /evidence="ECO:0007829|PDB:6FXO"
FT STRAND 1156..1158
FT /evidence="ECO:0007829|PDB:6FXO"
FT HELIX 1162..1170
FT /evidence="ECO:0007829|PDB:6FXO"
FT HELIX 1176..1184
FT /evidence="ECO:0007829|PDB:6FXO"
FT TURN 1185..1195
FT /evidence="ECO:0007829|PDB:6FXO"
FT HELIX 1199..1204
FT /evidence="ECO:0007829|PDB:6FXO"
FT HELIX 1220..1235
FT /evidence="ECO:0007829|PDB:6FXO"
FT STRAND 1241..1246
FT /evidence="ECO:0007829|PDB:6FXO"
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
