Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O33635 (ATL_STAEP) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional autolysin
Alternative name(s):
AtlE

Including the following 2 domains:

  1. N-acetylmuramoyl-L-alanine amidase
    EC=3.5.1.28
  2. Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
    EC=3.2.1.96
Gene names
Name:atl
Synonyms:atlE
OrganismStaphylococcus epidermidis
Taxonomic identifier1282 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length1335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Cleaves the peptidoglycan connecting the daughter cells at the end of the cell division cycle, resulting in the separation of the two newly divided cells. Acts as an autolysin in penicillin-induced lysis By similarity. As a bacterial surface-associated protein, mediates attachment to polystyrene surfaces, contributing to biofilm formation. Has also vitronectin-binding activity.

Catalytic activity

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -(Man(GlcNAc)2)Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.

Subunit structure

Oligomer; forms a ring structure at the cell surface which is important for efficient partitioning of daughter cells after cell division By similarity.

Subcellular location

Secreted. Note: Secreted, and then anchored on the cell surface at the peripheral cell wall above the completed septum (septal region), for the next cell division cycle. Ref.1

Domain

The repeat domains R1, R2 and R3 are responsible for directing the proteins to the septal region By similarity.

Post-translational modification

Undergoes proteolytic processing to generate the two extracellular lytic enzymes, probably at the septal region on the cell surface By similarity.

Sequence similarities

In the N-terminal section; belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.

In the C-terminal section; belongs to the glycosyl hydrolase 73 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 13351306Bifunctional autolysin
PRO_0000045479

Regions

Repeat516 – 6811661
Repeat682 – 8451642
Repeat846 – 10151703
Region303 – 863561N-acetylmuramoyl-L-alanine amidase
Region864 – 1335472Endo-beta-N-acetylglucosaminidase

Secondary structure

.............................................................. 1335
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O33635 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 0D8986BCB3DFF0A2

FASTA1,335148,273
        10         20         30         40         50         60 
MAKKFNYKLP SMVALTLFGT AFTAHQANAA EQPQNQSNHK NVLDDQTALK QAEKAKSEVT 

        70         80         90        100        110        120 
QSTTNVSGTQ TYQDPTQVQP KQDTQSTTYD ASLDEMSTYN EISSNQKQQS LSTDDANQNQ 

       130        140        150        160        170        180 
TNSVTKNQQE ETNDLTQEDK TSTDTNQLQE TQSVAKENEK DLGANANNEQ QDKKMTASQP 

       190        200        210        220        230        240 
SENQAIETQT ASNDNESQQK SQQVTSEQNE TATPKVSNTN ASGYNFDYDD EDDDSSTDHL 

       250        260        270        280        290        300 
EPISLNNVNA TSKQTTSYKY KEPAQRVTTN TVKKETASNQ ATIDTKQFTP FSATAQPRTV 

       310        320        330        340        350        360 
YSVSSQKTSS LPKYTPKVNS SINNYIRKKN MKAPRIEEDY TSYFPKYGYR NGVGRPEGIV 

       370        380        390        400        410        420 
VHDTANDNST IDGEIAFMKR NYTNAFVHAF VDGNRIIETA PTDYLSWGAG PYGNQRFINV 

       430        440        450        460        470        480 
EIVHTHDYDS FARSMNNYAD YAATQLQYYN LKPDSAENDG RGTVWTHAAI SNFLGGTDHA 

       490        500        510        520        530        540 
DPHQYLRSHN YSYAELYDLI YEKYLIKTKQ VAPWGTTSTK PSQPSKPSGG TNNKLTVSAN 

       550        560        570        580        590        600 
RGVAQIKPTN NGLYTTVYDS KGHKTDQVQK TLSVTKTATL GNNKFYLVED YNSGKKYGWV 

       610        620        630        640        650        660 
KQGDVVYNTA KAPVKVNQTY NVKAGSTLYT VPWGTPKQVA SKVSGTGNQT FKATKQQQID 

       670        680        690        700        710        720 
KATYLYGTVN GKSGWISKYY LTTASKPSNP TKPSTNNQLT VTNNSGVAQI NAKNSGLYTT 

       730        740        750        760        770        780 
VYDTKGKTTN QIQRTLSVTK AATLGDKKFY LVGDYNTGTN YGWVKQDEVI YNTAKSPVKI 

       790        800        810        820        830        840 
NQTYNVKPGV KLHTVPWGTY NQVAGTVSGK GDQTFKATKQ QQIDKATYLY GTVNGKSGWI 

       850        860        870        880        890        900 
SKYYLTAPSK VQALSTQSTP APKQVKPSTQ TVNQIAQVKA NNSGIRASVY DKTAKSGTKY 

       910        920        930        940        950        960 
ANRTFLINKQ RTQGNNTYVL LQDGTSNTPL GWVNINDVTT QNIGKQTQSI GKYSVKPTNN 

       970        980        990       1000       1010       1020 
GLYSIAWGTK NQQLLAPNTL ANQAFNASKA VYVGKDLYLY GTVNNRTGWI AAKDLIQNST 

      1030       1040       1050       1060       1070       1080 
DAQSTPYNYT FVINNSKSYF YMDPTKANRY SLKPYYEQTF TVIKQKNING VKWYYGQLLD 

      1090       1100       1110       1120       1130       1140 
GKYVWIKSTD LVKEKIKYAY TGMTLNNAIN IQSRLKYKPQ VQNEPLKWSN ANYSQIKNAM 

      1150       1160       1170       1180       1190       1200 
DTKRLANDSS LKYQFLRLDQ PQYLSAQALN KLLKGKGVLE NQGAAFSQAA RKYGLNEIYL 

      1210       1220       1230       1240       1250       1260 
ISHALVETGN GTSQLAKGGD VSKGKFTTKT GHKYHNVFGI GAFDNNALVD GIKYAKNAGW 

      1270       1280       1290       1300       1310       1320 
TSVSKAIIGG AKFIGNSYVK AGQNTLYKMR WNPANPGTHQ YATDINWANV NAQVLKQFYD 

      1330 
KIGEVGKYFE IPTYK 

« Hide

References

[1]"Evidence for autolysin-mediated primary attachment of Staphylococcus epidermidis to a polystyrene surface."
Heilmann C., Hussain M., Peters G., Goetz F.
Mol. Microbiol. 24:1013-1024(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 303-312, SUBCELLULAR LOCATION, INVOLVEMENT IN BIOFILM FORMATION.
Strain: O47.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U71377 Genomic DNA. Translation: AAB63571.1.
PIRT30211.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LATX-ray1.70A/B303-515[»]
4EPCX-ray2.90A516-847[»]
ProteinModelPortalO33635.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH73. Glycoside Hydrolase Family 73.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.80.10. 1 hit.
InterProIPR002502. Amidase_domain.
IPR013338. Lysozyme_dom_subfam2.
IPR002901. Mano_Glyc_endo_b_GlcNAc.
[Graphical view]
PfamPF01510. Amidase_2. 1 hit.
PF01832. Glucosaminidase. 1 hit.
[Graphical view]
SMARTSM00644. Ami_2. 1 hit.
SM00047. LYZ2. 1 hit.
[Graphical view]
SUPFAMSSF55846. SSF55846. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO33635.

Entry information

Entry nameATL_STAEP
AccessionPrimary (citable) accession number: O33635
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 1, 1998
Last modified: October 16, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references