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O33635

- ATL_STAEP

UniProt

O33635 - ATL_STAEP

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Protein

Bifunctional autolysin

Gene
atl, atlE
Organism
Staphylococcus epidermidis
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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.

GO - Molecular functioni

  1. amidase activity Source: InterPro
  2. mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity Source: UniProtKB-EC
  3. N-acetylmuramoyl-L-alanine amidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall macromolecule metabolic process Source: InterPro
  2. peptidoglycan catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Protein family/group databases

CAZyiGH73. Glycoside Hydrolase Family 73.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional autolysin
Alternative name(s):
AtlE
Including the following 2 domains:
N-acetylmuramoyl-L-alanine amidase (EC:3.5.1.28)
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase (EC:3.2.1.96)
Gene namesi
Name:atl
Synonyms:atlE
OrganismiStaphylococcus epidermidis
Taxonomic identifieri1282 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929 Reviewed predictionAdd
BLAST
Chaini30 – 13351306Bifunctional autolysinPRO_0000045479Add
BLAST

Post-translational modificationi

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

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
1335
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi321 – 3288
Beta strandi336 – 3383
Beta strandi358 – 3636
Helixi371 – 38010
Turni381 – 3844
Beta strandi388 – 3914
Beta strandi396 – 3983
Beta strandi407 – 4093
Helixi410 – 4145
Beta strandi417 – 4226
Helixi428 – 44821
Turni457 – 4593
Beta strandi462 – 4665
Helixi467 – 4737
Helixi483 – 4886
Helixi493 – 50715
Beta strandi699 – 7035
Beta strandi706 – 7105
Beta strandi717 – 7204
Beta strandi736 – 7449
Beta strandi747 – 7537
Turni755 – 7573
Beta strandi760 – 7656
Helixi766 – 7683
Beta strandi769 – 7746
Beta strandi778 – 7869
Beta strandi791 – 7955
Helixi800 – 8023
Beta strandi803 – 8064
Beta strandi809 – 8113
Beta strandi813 – 82311
Beta strandi826 – 8338
Beta strandi836 – 8416
Helixi842 – 8443

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LATX-ray1.70A/B303-515[»]
4EPCX-ray2.90A516-847[»]
ProteinModelPortaliO33635.

Miscellaneous databases

EvolutionaryTraceiO33635.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati516 – 6811661Add
BLAST
Repeati682 – 8451642Add
BLAST
Repeati846 – 10151703Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni303 – 863561N-acetylmuramoyl-L-alanine amidaseAdd
BLAST
Regioni864 – 1335472Endo-beta-N-acetylglucosaminidaseAdd
BLAST

Domaini

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

Sequence similaritiesi

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.

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR013338. Lysozyme_subfam2_dom.
IPR002901. MGlyc_endo_b_GlcNAc_like_dom.
[Graphical view]
PfamiPF01510. Amidase_2. 1 hit.
PF01832. Glucosaminidase. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
SM00047. LYZ2. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O33635-1 [UniParc]FASTAAdd to Basket

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MAKKFNYKLP SMVALTLFGT AFTAHQANAA EQPQNQSNHK NVLDDQTALK     50
QAEKAKSEVT QSTTNVSGTQ TYQDPTQVQP KQDTQSTTYD ASLDEMSTYN 100
EISSNQKQQS LSTDDANQNQ TNSVTKNQQE ETNDLTQEDK TSTDTNQLQE 150
TQSVAKENEK DLGANANNEQ QDKKMTASQP SENQAIETQT ASNDNESQQK 200
SQQVTSEQNE TATPKVSNTN ASGYNFDYDD EDDDSSTDHL EPISLNNVNA 250
TSKQTTSYKY KEPAQRVTTN TVKKETASNQ ATIDTKQFTP FSATAQPRTV 300
YSVSSQKTSS LPKYTPKVNS SINNYIRKKN MKAPRIEEDY TSYFPKYGYR 350
NGVGRPEGIV VHDTANDNST IDGEIAFMKR NYTNAFVHAF VDGNRIIETA 400
PTDYLSWGAG PYGNQRFINV EIVHTHDYDS FARSMNNYAD YAATQLQYYN 450
LKPDSAENDG RGTVWTHAAI SNFLGGTDHA DPHQYLRSHN YSYAELYDLI 500
YEKYLIKTKQ VAPWGTTSTK PSQPSKPSGG TNNKLTVSAN RGVAQIKPTN 550
NGLYTTVYDS KGHKTDQVQK TLSVTKTATL GNNKFYLVED YNSGKKYGWV 600
KQGDVVYNTA KAPVKVNQTY NVKAGSTLYT VPWGTPKQVA SKVSGTGNQT 650
FKATKQQQID KATYLYGTVN GKSGWISKYY LTTASKPSNP TKPSTNNQLT 700
VTNNSGVAQI NAKNSGLYTT VYDTKGKTTN QIQRTLSVTK AATLGDKKFY 750
LVGDYNTGTN YGWVKQDEVI YNTAKSPVKI NQTYNVKPGV KLHTVPWGTY 800
NQVAGTVSGK GDQTFKATKQ QQIDKATYLY GTVNGKSGWI SKYYLTAPSK 850
VQALSTQSTP APKQVKPSTQ TVNQIAQVKA NNSGIRASVY DKTAKSGTKY 900
ANRTFLINKQ RTQGNNTYVL LQDGTSNTPL GWVNINDVTT QNIGKQTQSI 950
GKYSVKPTNN GLYSIAWGTK NQQLLAPNTL ANQAFNASKA VYVGKDLYLY 1000
GTVNNRTGWI AAKDLIQNST DAQSTPYNYT FVINNSKSYF YMDPTKANRY 1050
SLKPYYEQTF TVIKQKNING VKWYYGQLLD GKYVWIKSTD LVKEKIKYAY 1100
TGMTLNNAIN IQSRLKYKPQ VQNEPLKWSN ANYSQIKNAM DTKRLANDSS 1150
LKYQFLRLDQ PQYLSAQALN KLLKGKGVLE NQGAAFSQAA RKYGLNEIYL 1200
ISHALVETGN GTSQLAKGGD VSKGKFTTKT GHKYHNVFGI GAFDNNALVD 1250
GIKYAKNAGW TSVSKAIIGG AKFIGNSYVK AGQNTLYKMR WNPANPGTHQ 1300
YATDINWANV NAQVLKQFYD KIGEVGKYFE IPTYK 1335
Length:1,335
Mass (Da):148,273
Last modified:January 1, 1998 - v1
Checksum:i0D8986BCB3DFF0A2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U71377 Genomic DNA. Translation: AAB63571.1.
PIRiT30211.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U71377 Genomic DNA. Translation: AAB63571.1 .
PIRi T30211.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LAT X-ray 1.70 A/B 303-515 [» ]
4EPC X-ray 2.90 A 516-847 [» ]
ProteinModelPortali O33635.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH73. Glycoside Hydrolase Family 73.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei O33635.

Family and domain databases

Gene3Di 3.40.80.10. 1 hit.
InterProi IPR002502. Amidase_domain.
IPR013338. Lysozyme_subfam2_dom.
IPR002901. MGlyc_endo_b_GlcNAc_like_dom.
[Graphical view ]
Pfami PF01510. Amidase_2. 1 hit.
PF01832. Glucosaminidase. 1 hit.
[Graphical view ]
SMARTi SM00644. Ami_2. 1 hit.
SM00047. LYZ2. 1 hit.
[Graphical view ]
SUPFAMi SSF55846. SSF55846. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiATL_STAEP
AccessioniPrimary (citable) accession number: O33635
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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