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O33635

- ATL_STAEP

UniProt

O33635 - ATL_STAEP

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Protein

Bifunctional autolysin

Gene

atl

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.By similarity

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 organization Source: UniProtKB-KW
  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 1 Publication
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.

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
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 – 3288Combined sources
Beta strandi336 – 3383Combined sources
Beta strandi358 – 3636Combined sources
Helixi371 – 38010Combined sources
Turni381 – 3844Combined sources
Beta strandi388 – 3914Combined sources
Beta strandi396 – 3983Combined sources
Beta strandi407 – 4093Combined sources
Helixi410 – 4145Combined sources
Beta strandi417 – 4226Combined sources
Helixi428 – 44821Combined sources
Turni457 – 4593Combined sources
Beta strandi462 – 4665Combined sources
Helixi467 – 4737Combined sources
Helixi483 – 4886Combined sources
Helixi493 – 50715Combined sources
Beta strandi699 – 7035Combined sources
Beta strandi706 – 7105Combined sources
Beta strandi717 – 7204Combined sources
Beta strandi736 – 7449Combined sources
Beta strandi747 – 7537Combined sources
Turni755 – 7573Combined sources
Beta strandi760 – 7656Combined sources
Helixi766 – 7683Combined sources
Beta strandi769 – 7746Combined sources
Beta strandi778 – 7869Combined sources
Beta strandi791 – 7955Combined sources
Helixi800 – 8023Combined sources
Beta strandi803 – 8064Combined sources
Beta strandi809 – 8113Combined sources
Beta strandi813 – 82311Combined sources
Beta strandi826 – 8338Combined sources
Beta strandi836 – 8416Combined sources
Helixi842 – 8443Combined sources

3D structure databases

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

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

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

« Hide

        10         20         30         40         50
MAKKFNYKLP SMVALTLFGT AFTAHQANAA EQPQNQSNHK NVLDDQTALK
60 70 80 90 100
QAEKAKSEVT QSTTNVSGTQ TYQDPTQVQP KQDTQSTTYD ASLDEMSTYN
110 120 130 140 150
EISSNQKQQS LSTDDANQNQ TNSVTKNQQE ETNDLTQEDK TSTDTNQLQE
160 170 180 190 200
TQSVAKENEK DLGANANNEQ QDKKMTASQP SENQAIETQT ASNDNESQQK
210 220 230 240 250
SQQVTSEQNE TATPKVSNTN ASGYNFDYDD EDDDSSTDHL EPISLNNVNA
260 270 280 290 300
TSKQTTSYKY KEPAQRVTTN TVKKETASNQ ATIDTKQFTP FSATAQPRTV
310 320 330 340 350
YSVSSQKTSS LPKYTPKVNS SINNYIRKKN MKAPRIEEDY TSYFPKYGYR
360 370 380 390 400
NGVGRPEGIV VHDTANDNST IDGEIAFMKR NYTNAFVHAF VDGNRIIETA
410 420 430 440 450
PTDYLSWGAG PYGNQRFINV EIVHTHDYDS FARSMNNYAD YAATQLQYYN
460 470 480 490 500
LKPDSAENDG RGTVWTHAAI SNFLGGTDHA DPHQYLRSHN YSYAELYDLI
510 520 530 540 550
YEKYLIKTKQ VAPWGTTSTK PSQPSKPSGG TNNKLTVSAN RGVAQIKPTN
560 570 580 590 600
NGLYTTVYDS KGHKTDQVQK TLSVTKTATL GNNKFYLVED YNSGKKYGWV
610 620 630 640 650
KQGDVVYNTA KAPVKVNQTY NVKAGSTLYT VPWGTPKQVA SKVSGTGNQT
660 670 680 690 700
FKATKQQQID KATYLYGTVN GKSGWISKYY LTTASKPSNP TKPSTNNQLT
710 720 730 740 750
VTNNSGVAQI NAKNSGLYTT VYDTKGKTTN QIQRTLSVTK AATLGDKKFY
760 770 780 790 800
LVGDYNTGTN YGWVKQDEVI YNTAKSPVKI NQTYNVKPGV KLHTVPWGTY
810 820 830 840 850
NQVAGTVSGK GDQTFKATKQ QQIDKATYLY GTVNGKSGWI SKYYLTAPSK
860 870 880 890 900
VQALSTQSTP APKQVKPSTQ TVNQIAQVKA NNSGIRASVY DKTAKSGTKY
910 920 930 940 950
ANRTFLINKQ RTQGNNTYVL LQDGTSNTPL GWVNINDVTT QNIGKQTQSI
960 970 980 990 1000
GKYSVKPTNN GLYSIAWGTK NQQLLAPNTL ANQAFNASKA VYVGKDLYLY
1010 1020 1030 1040 1050
GTVNNRTGWI AAKDLIQNST DAQSTPYNYT FVINNSKSYF YMDPTKANRY
1060 1070 1080 1090 1100
SLKPYYEQTF TVIKQKNING VKWYYGQLLD GKYVWIKSTD LVKEKIKYAY
1110 1120 1130 1140 1150
TGMTLNNAIN IQSRLKYKPQ VQNEPLKWSN ANYSQIKNAM DTKRLANDSS
1160 1170 1180 1190 1200
LKYQFLRLDQ PQYLSAQALN KLLKGKGVLE NQGAAFSQAA RKYGLNEIYL
1210 1220 1230 1240 1250
ISHALVETGN GTSQLAKGGD VSKGKFTTKT GHKYHNVFGI GAFDNNALVD
1260 1270 1280 1290 1300
GIKYAKNAGW TSVSKAIIGG AKFIGNSYVK AGQNTLYKMR WNPANPGTHQ
1310 1320 1330
YATDINWANV NAQVLKQFYD KIGEVGKYFE IPTYK
Length:1,335
Mass (Da):148,273
Last modified:January 1, 1998 - v1
Checksum:i0D8986BCB3DFF0A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U71377 Genomic DNA. Translation: AAB63571.1.
PIRiT30211.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U71377 Genomic DNA. Translation: AAB63571.1 .
PIRi T30211.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 64 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