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

Q6GAG0 (ATL_STAAS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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
Ordered Locus Names:SAS0988
OrganismStaphylococcus aureus (strain MSSA476) [Complete proteome] [HAMAP]
Taxonomic identifier282459 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length1250 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

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 By similarity. 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 By similarity.

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 – 12501221Bifunctional autolysin
PRO_0000045477

Regions

Repeat425 – 5831591
Repeat590 – 7521632
Repeat764 – 9261633
Region199 – 769571N-acetylmuramoyl-L-alanine amidase
Region770 – 1250481Endo-beta-N-acetylglucosaminidase

Sequences

Sequence LengthMass (Da)Tools
Q6GAG0 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: D8C43606B9374D96

FASTA1,250136,868
        10         20         30         40         50         60 
MAKKFNYKLP SMVALTLVGS AVTAHQVQAA ETTQDQTTNK NVLDSNKVKA TTEQAKAEVK 

        70         80         90        100        110        120 
NPTQNISGTQ VYQDPAIVQP KTANNKTGNA QVSQKVDTAQ VNGDTRANQS ATTNNTQPVA 

       130        140        150        160        170        180 
KSTSTTAPKT NTNVTNAGYS LVDDEDDNSE NQINPELIKS AAKPAALETQ YKAAAPKAAT 

       190        200        210        220        230        240 
TSAPKAKTEA TPKVTTFSAS AQPRSVAATP KTSLPKYKPQ VNSSINDYIR KNNLKAPKIE 

       250        260        270        280        290        300 
EDYTSYFPKY AYRNGVGRPE GIVVHDTAND RSTINGEISY MKNNYQNAFV HAFVDGDRII 

       310        320        330        340        350        360 
ETAPTDYLSW GVGAVGNPRF INVEIVHTHD YASFARSMNN YADYAATQLQ YYGLKPDSAE 

       370        380        390        400        410        420 
YDGNGTVWTH YAVSKYLGGT DHADPHGYLR SHNYSYDQLY DLINEKYLIK MGKVAPWGTQ 

       430        440        450        460        470        480 
STTTPTTPSK PSTGKLTVAA NNGVAQIKPT NSGLYTTVYD KTGKATNEVQ KTFAVSKTAT 

       490        500        510        520        530        540 
LGNQKFYLVQ DYNSGNKFGW VKEGDVVYNT AKSPVNVNQS YSIKPGTKLY TVPWGTSKQV 

       550        560        570        580        590        600 
AGSVSGSGNQ TFKASKQQQI DKSIYLYGSV NGKSGWVSKA YLVDTAKPTP TPTPKPSTPT 

       610        620        630        640        650        660 
TNNKLTVSSL NGVAQINAKN NGLFTTVYDK TGKPTKEVQK TFAVTKEASL GGNKFYLVKD 

       670        680        690        700        710        720 
YNSPTLIGWV KQGDVIYNNA KSPVNVMQTY TVKPGTKLYS VPWGTYKQEA GAVSGTGNQT 

       730        740        750        760        770        780 
FKATKQQQID KSIYLFGTVN GKSGWVSKAY LAVPAAPKKA VAQPKTAVKA YTVTKPQTTQ 

       790        800        810        820        830        840 
TVSKIAQVKP NNTGIRASVY EKTAKNGAKY ADRTFYVTKE RAHGNETYVL LNNTSHNIPL 

       850        860        870        880        890        900 
GWFNVKDLNV QNLGKEVKTT QKYTVNKSNN GLSMVPWGTK NQVILTGNNI AQGTFNATKQ 

       910        920        930        940        950        960 
VSVGKDVYLY GTINNRTGWV NAKDLTAPTA VKPTTSAAKD YNYTYVIKNG NGYYYVTPNS 

       970        980        990       1000       1010       1020 
DTAKYSLKAF NEQPFAVVKE QVINEQTWYY GKLSNGKLAW IKSTDLAKEL IKYNQTGMTL 

      1030       1040       1050       1060       1070       1080 
NQVAQIQAGL QYKPQVQRVP GKWTDANFND VKHAMDTKRL AQDPALKYQF LRLDQPQNIS 

      1090       1100       1110       1120       1130       1140 
IDKINQFLKG KGVLENQGAA FNKAAQMYGI NEVYLISHAL LETGNGTSQL AKGADVVNNK 

      1150       1160       1170       1180       1190       1200 
VVTNSNTKYH NVFGIAAYDN DPLREGIKYA KQAGWDTVSK AIVGGAKFIG NSYVKAGQNT 

      1210       1220       1230       1240       1250 
LYKMRWNPAH PGTHQYATDI DWANINAKII KGYYDKIGEV GKYFDIPQYK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571857 Genomic DNA. Translation: CAG42763.1.
RefSeqYP_043113.1. NC_002953.3.

3D structure databases

ProteinModelPortalQ6GAG0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING282459.SAS0988.

Protein family/group databases

CAZyGH73. Glycoside Hydrolase Family 73.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2862752.
KEGGsas:SAS0988.
PATRIC19551413. VBIStaAur96780_1024.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4193.
HOGENOMHOG000279968.
KOK13714.
OMAKSGWISK.
OrthoDBEOG6GXTN7.

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_STAAS
AccessionPrimary (citable) accession number: Q6GAG0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: July 19, 2004
Last modified: May 14, 2014
This is version 64 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