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P0C5Z8

- ATL_STAAU

UniProt

P0C5Z8 - ATL_STAAU

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Protein

Bifunctional autolysin

Gene
atl, nag
Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 5 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.1 Publication

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
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:nag
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [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.3 Publications

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 – 3636 Reviewed predictionAdd
BLAST
Chaini37 – 12551219Bifunctional autolysinPRO_0000012114Add
BLAST

Post-translational modificationi

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

Proteomic databases

PRIDEiP0C5Z8.

Interactioni

Subunit structurei

Oligomer; forms a ring structure at the cell surface which is important for efficient partitioning of daughter cells after cell division.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP0C5Z8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati425 – 5891651Add
BLAST
Repeati596 – 7581632Add
BLAST
Repeati770 – 9321633Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni199 – 775577N-acetylmuramoyl-L-alanine amidaseAdd
BLAST
Regioni776 – 1255480Endo-beta-N-acetylglucosaminidaseAdd
BLAST

Domaini

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

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

Phylogenomic databases

eggNOGiCOG4193.

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.

P0C5Z8-1 [UniParc]FASTAAdd to Basket

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MLGVINRMAK KFNYKLPSMV ALTLVGSAVT AHQVQAAETT QDQTTNKNVL     50
DSNKVKATTE QAKAEVKNPT QNISGTQVYQ DPAIVQPKTA NNKTGNAQVS 100
QKVDTAQVNG DTRANQSATT NNTQPVAKST STTAPKTNTN VTNAGYSLVD 150
DEDDNSEHQI NPELIKSAAK PAALETQYKA AAPKAKTEAT PKVTTFSASA 200
QPRSVAATPK TSLPKYKPQV NSSINDYIRK NNLKAPKIEE DYTSYFPKYA 250
YRNGVGRPEG IVVHDTANDR STINGEISYM KNNYQNAFVH AFVDGDRIIE 300
TAPTDYLSWG VGAVGNPRFI NVEIVHTHDY ASFARSMNNY ADYAATQLQY 350
YGLKPDSAEY DGNGTVWTHY AVSKYLGGTD HADPHGYLRS HNYSYDQLYD 400
LINEKYLIKM GKVAPWGTQF TTTPTTPSKP TTPSKPSTGK LTVAANNGVA 450
QIKPTNSGLY TTVYDKTGKA TNEVQKTFAV SKTATLGNQK FYLVQDYNSG 500
NKFGWVKEGD VVYNTAKSPV NVNQSYSIKS GTKLYTVPWG TSKQVAGSVS 550
GSGNQTFKAS KQQQIDKSIY LYGSVNGKSG WVSKAYLVDT AKPTPTPIPK 600
PSTPTTNNKL TVSSLNGVAQ INAKNNGLFT TVYDKTGKPT KEVQKTFAVT 650
KEASLGGNKF YLVKDYNSPT LIGWVKQGDV IYNNAKSPVN VMQTYTVKPG 700
TKLYSVPWGT YKQEAGAVSG TGNQTFKATK QQQIDKSIYL FGTVNGKSGW 750
VSKAYLAVPA APKKAVAQPK TAVKAYTVTK PQTTQTVSKI AQVKPNNTGI 800
RASVYEKTAK NGAKYADRTF YVTKERAHGN ETYVLLNNTS HNIPLGWFNV 850
KDLNVQNLGK EVKTTQKYTV NKSNNGLSMV PWGTKNQVIL TGNNIAQGTF 900
NATKQVSVGK DVYLYGTINN RTGWVNAKDL TAPTAVKPTT SAAKDYNYTY 950
VIKNGNGYYY VTPNSDTAKY SLKAFNEQPF AVVKEQVING QTWYYGKLSN 1000
GKLAWIKSTD LAKELIKYNQ TGMTLNQVAQ IQAGLQYKPQ VQRVPGKWTD 1050
ANFNDVKHAM DTKRLAQDPA LKYQFLRLDQ PQNISIDKIN QFLKGKGVLE 1100
NQGAAFNKAA QMYGINEVYL ISHALLETGN GTSQLAKGAD VVNNKVVTNS 1150
NTKYHNVFGI AAYDNDPLRE GIKYAKQAGW DTVSKAIVGG AKFIGNSYVK 1200
AGQNTLYKMR WNPAHPGTHQ YATDVDWANI NAKIIKGYYD KIGEVGKYFD 1250
IPQYK 1255
Length:1,255
Mass (Da):137,535
Last modified:January 15, 2008 - v1
Checksum:i7257DD87168AAE7D
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti932 – 9321A → R in BAA22600. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF537210 Genomic DNA. Translation: AAP44166.1. Different initiation.
D42078 Genomic DNA. Translation: BAA22600.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF537210 Genomic DNA. Translation: AAP44166.1 . Different initiation.
D42078 Genomic DNA. Translation: BAA22600.1 .

3D structure databases

ProteinModelPortali P0C5Z8.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH73. Glycoside Hydrolase Family 73.

Proteomic databases

PRIDEi P0C5Z8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG4193.

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. "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.

Entry informationi

Entry nameiATL_STAAU
AccessioniPrimary (citable) accession number: P0C5Z8
Secondary accession number(s): O32391
, P0C1R4, P52081, Q7WTC6, Q7WY94, Q7WY95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: September 3, 2014
This is version 37 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

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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