ATL_STAEP
ID ATL_STAEP Reviewed; 1335 AA.
AC O33635;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Bifunctional autolysin;
DE AltName: Full=AtlE;
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=atlE;
OS Staphylococcus epidermidis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 303-312, SUBCELLULAR
RP LOCATION, AND INVOLVEMENT IN BIOFILM FORMATION.
RC STRAIN=O47;
RX PubMed=9220008; DOI=10.1046/j.1365-2958.1997.4101774.x;
RA Heilmann C., Hussain M., Peters G., Goetz F.;
RT "Evidence for autolysin-mediated primary attachment of Staphylococcus
RT epidermidis to a polystyrene surface.";
RL Mol. Microbiol. 24:1013-1024(1997).
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). As a bacterial surface-
CC associated protein, mediates attachment to polystyrene surfaces,
CC contributing to biofilm formation. Has also vitronectin-binding
CC activity. {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:0000269|PubMed:9220008}.
CC Note=Secreted, and then anchored on the cell surface at the peripheral
CC cell wall above the completed septum (septal region), for the next cell
CC division cycle.
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; U71377; AAB63571.1; -; Genomic_DNA.
DR PIR; T30211; T30211.
DR RefSeq; WP_001831665.1; NZ_WJUN01000008.1.
DR PDB; 3LAT; X-ray; 1.70 A; A/B=303-515.
DR PDB; 4EPC; X-ray; 2.90 A; A=516-847.
DR PDB; 7KWI; NMR; -; A=696-847.
DR PDBsum; 3LAT; -.
DR PDBsum; 4EPC; -.
DR PDBsum; 7KWI; -.
DR AlphaFoldDB; O33635; -.
DR SMR; O33635; -.
DR CAZy; GH73; Glycoside Hydrolase Family 73.
DR GeneID; 50019110; -.
DR EvolutionaryTrace; O33635; -.
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; Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1335
FT /note="Bifunctional autolysin"
FT /id="PRO_0000045479"
FT DOMAIN 533..610
FT /note="GW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 612..686
FT /note="GW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 700..774
FT /note="GW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 776..850
FT /note="GW 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 868..943
FT /note="GW 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 945..1020
FT /note="GW 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 1023..1096
FT /note="GW 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT REGION 51..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..863
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT REGION 514..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..1335
FT /note="Endo-beta-N-acetylglucosaminidase"
FT COMPBIAS 53..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:3LAT"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:3LAT"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:3LAT"
FT HELIX 371..380
FT /evidence="ECO:0007829|PDB:3LAT"
FT TURN 381..384
FT /evidence="ECO:0007829|PDB:3LAT"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:3LAT"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:3LAT"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:3LAT"
FT HELIX 410..414
FT /evidence="ECO:0007829|PDB:3LAT"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:3LAT"
FT HELIX 428..448
FT /evidence="ECO:0007829|PDB:3LAT"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:3LAT"
FT STRAND 462..466
FT /evidence="ECO:0007829|PDB:3LAT"
FT HELIX 467..473
FT /evidence="ECO:0007829|PDB:3LAT"
FT HELIX 483..488
FT /evidence="ECO:0007829|PDB:3LAT"
FT HELIX 493..507
FT /evidence="ECO:0007829|PDB:3LAT"
FT STRAND 699..701
FT /evidence="ECO:0007829|PDB:4EPC"
FT STRAND 706..710
FT /evidence="ECO:0007829|PDB:4EPC"
FT STRAND 717..720
FT /evidence="ECO:0007829|PDB:4EPC"
FT STRAND 736..744
FT /evidence="ECO:0007829|PDB:4EPC"
FT STRAND 750..753
FT /evidence="ECO:0007829|PDB:4EPC"
FT TURN 755..757
FT /evidence="ECO:0007829|PDB:4EPC"
FT STRAND 760..764
FT /evidence="ECO:0007829|PDB:4EPC"
FT HELIX 766..768
FT /evidence="ECO:0007829|PDB:7KWI"
FT STRAND 769..775
FT /evidence="ECO:0007829|PDB:4EPC"
FT STRAND 782..786
FT /evidence="ECO:0007829|PDB:4EPC"
FT STRAND 793..795
FT /evidence="ECO:0007829|PDB:4EPC"
FT HELIX 800..802
FT /evidence="ECO:0007829|PDB:4EPC"
FT STRAND 809..811
FT /evidence="ECO:0007829|PDB:4EPC"
FT STRAND 813..823
FT /evidence="ECO:0007829|PDB:4EPC"
FT STRAND 827..833
FT /evidence="ECO:0007829|PDB:4EPC"
FT STRAND 836..841
FT /evidence="ECO:0007829|PDB:4EPC"
FT TURN 842..844
FT /evidence="ECO:0007829|PDB:7KWI"
SQ SEQUENCE 1335 AA; 148273 MW; 0D8986BCB3DFF0A2 CRC64;
MAKKFNYKLP SMVALTLFGT AFTAHQANAA EQPQNQSNHK NVLDDQTALK QAEKAKSEVT
QSTTNVSGTQ TYQDPTQVQP KQDTQSTTYD ASLDEMSTYN EISSNQKQQS LSTDDANQNQ
TNSVTKNQQE ETNDLTQEDK TSTDTNQLQE TQSVAKENEK DLGANANNEQ QDKKMTASQP
SENQAIETQT ASNDNESQQK SQQVTSEQNE TATPKVSNTN ASGYNFDYDD EDDDSSTDHL
EPISLNNVNA TSKQTTSYKY KEPAQRVTTN TVKKETASNQ ATIDTKQFTP FSATAQPRTV
YSVSSQKTSS LPKYTPKVNS SINNYIRKKN MKAPRIEEDY TSYFPKYGYR NGVGRPEGIV
VHDTANDNST IDGEIAFMKR NYTNAFVHAF VDGNRIIETA PTDYLSWGAG PYGNQRFINV
EIVHTHDYDS FARSMNNYAD YAATQLQYYN LKPDSAENDG RGTVWTHAAI SNFLGGTDHA
DPHQYLRSHN YSYAELYDLI YEKYLIKTKQ VAPWGTTSTK PSQPSKPSGG TNNKLTVSAN
RGVAQIKPTN NGLYTTVYDS KGHKTDQVQK TLSVTKTATL GNNKFYLVED YNSGKKYGWV
KQGDVVYNTA KAPVKVNQTY NVKAGSTLYT VPWGTPKQVA SKVSGTGNQT FKATKQQQID
KATYLYGTVN GKSGWISKYY LTTASKPSNP TKPSTNNQLT VTNNSGVAQI NAKNSGLYTT
VYDTKGKTTN QIQRTLSVTK AATLGDKKFY LVGDYNTGTN YGWVKQDEVI YNTAKSPVKI
NQTYNVKPGV KLHTVPWGTY NQVAGTVSGK GDQTFKATKQ QQIDKATYLY GTVNGKSGWI
SKYYLTAPSK VQALSTQSTP APKQVKPSTQ TVNQIAQVKA NNSGIRASVY DKTAKSGTKY
ANRTFLINKQ RTQGNNTYVL LQDGTSNTPL GWVNINDVTT QNIGKQTQSI GKYSVKPTNN
GLYSIAWGTK NQQLLAPNTL ANQAFNASKA VYVGKDLYLY GTVNNRTGWI AAKDLIQNST
DAQSTPYNYT FVINNSKSYF YMDPTKANRY SLKPYYEQTF TVIKQKNING VKWYYGQLLD
GKYVWIKSTD LVKEKIKYAY TGMTLNNAIN IQSRLKYKPQ VQNEPLKWSN ANYSQIKNAM
DTKRLANDSS LKYQFLRLDQ PQYLSAQALN KLLKGKGVLE NQGAAFSQAA RKYGLNEIYL
ISHALVETGN GTSQLAKGGD VSKGKFTTKT GHKYHNVFGI GAFDNNALVD GIKYAKNAGW
TSVSKAIIGG AKFIGNSYVK AGQNTLYKMR WNPANPGTHQ YATDINWANV NAQVLKQFYD
KIGEVGKYFE IPTYK
