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P0C5Z8 (ATL_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

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:nag
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length1255 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. Ref.3

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. Ref.4

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.4 Ref.5 Ref.6

Domain

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

Post-translational modification

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

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 caution

The sequence AAP44166.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636 Potential
Chain37 – 12551219Bifunctional autolysin
PRO_0000012114

Regions

Repeat425 – 5891651
Repeat596 – 7581632
Repeat770 – 9321633
Region199 – 775577N-acetylmuramoyl-L-alanine amidase
Region776 – 1255480Endo-beta-N-acetylglucosaminidase

Experimental info

Sequence conflict9321A → R in BAA22600. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P0C5Z8 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 7257DD87168AAE7D

FASTA1,255137,535
        10         20         30         40         50         60 
MLGVINRMAK KFNYKLPSMV ALTLVGSAVT AHQVQAAETT QDQTTNKNVL DSNKVKATTE 

        70         80         90        100        110        120 
QAKAEVKNPT QNISGTQVYQ DPAIVQPKTA NNKTGNAQVS QKVDTAQVNG DTRANQSATT 

       130        140        150        160        170        180 
NNTQPVAKST STTAPKTNTN VTNAGYSLVD DEDDNSEHQI NPELIKSAAK PAALETQYKA 

       190        200        210        220        230        240 
AAPKAKTEAT PKVTTFSASA QPRSVAATPK TSLPKYKPQV NSSINDYIRK NNLKAPKIEE 

       250        260        270        280        290        300 
DYTSYFPKYA YRNGVGRPEG IVVHDTANDR STINGEISYM KNNYQNAFVH AFVDGDRIIE 

       310        320        330        340        350        360 
TAPTDYLSWG VGAVGNPRFI NVEIVHTHDY ASFARSMNNY ADYAATQLQY YGLKPDSAEY 

       370        380        390        400        410        420 
DGNGTVWTHY AVSKYLGGTD HADPHGYLRS HNYSYDQLYD LINEKYLIKM GKVAPWGTQF 

       430        440        450        460        470        480 
TTTPTTPSKP TTPSKPSTGK LTVAANNGVA QIKPTNSGLY TTVYDKTGKA TNEVQKTFAV 

       490        500        510        520        530        540 
SKTATLGNQK FYLVQDYNSG NKFGWVKEGD VVYNTAKSPV NVNQSYSIKS GTKLYTVPWG 

       550        560        570        580        590        600 
TSKQVAGSVS GSGNQTFKAS KQQQIDKSIY LYGSVNGKSG WVSKAYLVDT AKPTPTPIPK 

       610        620        630        640        650        660 
PSTPTTNNKL TVSSLNGVAQ INAKNNGLFT TVYDKTGKPT KEVQKTFAVT KEASLGGNKF 

       670        680        690        700        710        720 
YLVKDYNSPT LIGWVKQGDV IYNNAKSPVN VMQTYTVKPG TKLYSVPWGT YKQEAGAVSG 

       730        740        750        760        770        780 
TGNQTFKATK QQQIDKSIYL FGTVNGKSGW VSKAYLAVPA APKKAVAQPK TAVKAYTVTK 

       790        800        810        820        830        840 
PQTTQTVSKI AQVKPNNTGI RASVYEKTAK NGAKYADRTF YVTKERAHGN ETYVLLNNTS 

       850        860        870        880        890        900 
HNIPLGWFNV KDLNVQNLGK EVKTTQKYTV NKSNNGLSMV PWGTKNQVIL TGNNIAQGTF 

       910        920        930        940        950        960 
NATKQVSVGK DVYLYGTINN RTGWVNAKDL TAPTAVKPTT SAAKDYNYTY VIKNGNGYYY 

       970        980        990       1000       1010       1020 
VTPNSDTAKY SLKAFNEQPF AVVKEQVING QTWYYGKLSN GKLAWIKSTD LAKELIKYNQ 

      1030       1040       1050       1060       1070       1080 
TGMTLNQVAQ IQAGLQYKPQ VQRVPGKWTD ANFNDVKHAM DTKRLAQDPA LKYQFLRLDQ 

      1090       1100       1110       1120       1130       1140 
PQNISIDKIN QFLKGKGVLE NQGAAFNKAA QMYGINEVYL ISHALLETGN GTSQLAKGAD 

      1150       1160       1170       1180       1190       1200 
VVNNKVVTNS NTKYHNVFGI AAYDNDPLRE GIKYAKQAGW DTVSKAIVGG AKFIGNSYVK 

      1210       1220       1230       1240       1250 
AGQNTLYKMR WNPAHPGTHQ YATDVDWANI NAKIIKGYYD KIGEVGKYFD IPQYK 

« Hide

References

[1]"Resistance to autolysis in vancomycin-selected Staphylococcus aureus isolates precedes vancomycin-intermediate resistance."
Boyle-Vavra S., Challapalli M., Daum R.S.
Antimicrob. Agents Chemother. 47:2036-2039(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: IL-A.
[2]"Novel cytotoxin in a clinical isolate of methicillin-resistant S. aureus: cloning, sequencing and expression."
Kamitani S., Minamide W., Yutsudo T., Noda M.
Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 775-1255.
[3]"Identification of endo-beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase as cluster-dispersing enzymes in Staphylococcus aureus."
Sugai M., Komatsuzawa H., Akiyama T., Hong Y.-M., Oshida T., Miyake Y., Yamaguchi T., Suginaka H.
J. Bacteriol. 177:1491-1496(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447.
[4]"An autolysin ring associated with cell separation of Staphylococcus aureus."
Yamada S., Sugai M., Komatsuzawa H., Nakashima S., Oshida T., Matsumoto A., Suginaka H.
J. Bacteriol. 178:1565-1571(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUBUNIT.
Strain: ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447.
[5]"Subcellular localization of the major autolysin, ATL and its processed proteins in Staphylococcus aureus."
Komatsuzawa H., Sugai M., Nakashima S., Yamada S., Matsumoto A., Oshida T., Suginaka H.
Microbiol. Immunol. 41:469-479(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447.
[6]"Localized perforation of the cell wall by a major autolysin: atl gene products and the onset of penicillin-induced lysis of Staphylococcus aureus."
Sugai M., Yamada S., Nakashima S., Komatsuzawa H., Matsumoto A., Oshida T., Suginaka H.
J. Bacteriol. 179:2958-2962(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447.
[7]"Targeting of muralytic enzymes to the cell division site of Gram-positive bacteria: repeat domains direct autolysin to the equatorial surface ring of Staphylococcus aureus."
Baba T., Schneewind O.
EMBO J. 17:4639-4646(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE OF REPEATS IN LOCALIZATION AT THE SEPTAL REGION.
Strain: OS2.
[8]"Modification of autolysis by synthetic peptides derived from the presumptive binding domain of Staphylococcus aureus autolysin."
Takano M., Oshida T., Yasojima A., Yamada M., Okagaki C., Sugai M., Suginaka H., Matsushita T.
Microbiol. Immunol. 44:463-472(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: BINDING TO THE BACTERIAL CELL WALL.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF537210 Genomic DNA. Translation: AAP44166.1. Different initiation.
D42078 Genomic DNA. Translation: BAA22600.1.

3D structure databases

ProteinModelPortalP0C5Z8.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH73. Glycoside Hydrolase Family 73.

Proteomic databases

PRIDEP0C5Z8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG4193.

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...

Entry information

Entry nameATL_STAAU
AccessionPrimary (citable) accession number: P0C5Z8
Secondary accession number(s): O32391 expand/collapse secondary AC list , P0C1R4, P52081, Q7WTC6, Q7WY94, Q7WY95
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: October 16, 2013
This is version 35 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