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Q6GI31 (ATL_STAAR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:SAR1026
OrganismStaphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP]
Taxonomic identifier282458 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length1257 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 – 12571228Bifunctional autolysin
PRO_0000045476

Regions

Repeat423 – 5901681
Repeat597 – 7591632
Repeat771 – 9331633
Region197 – 776580N-acetylmuramoyl-L-alanine amidase
Region777 – 1257481Endo-beta-N-acetylglucosaminidase

Sequences

Sequence LengthMass (Da)Tools
Q6GI31 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 8CEB3DB932B1720D

FASTA1,257137,528
        10         20         30         40         50         60 
MAKKFNYKLP SMVALTLVGS AVTAHQVQAA ETTQDQTTNK NVLDSNKVKA TTEQAKAEVK 

        70         80         90        100        110        120 
NPTQNISGTQ VYQDPAIVQP KAANKTGNAQ VNQKVDTTQV NGDTRATQST TSNNAKPVTK 

       130        140        150        160        170        180 
STNTTAPKTN NNVTSAGYSL VDDEDDNSEN QINPELIKSA AKPAALETQY KAAAPKATPV 

       190        200        210        220        230        240 
APKAKTEATP KVTTFSASAQ PRSAAAAPKT SLPKYKPQVN SSINDYIRKN NLKAPKIEED 

       250        260        270        280        290        300 
YTSYFPKYAY RNGVGRPEGI VVHDTANDRS TINGEISYMK NNYQNAFVHA FVDGDRIIET 

       310        320        330        340        350        360 
APTDYLSWGV GAVGNPRFIN VEIVHTHDYA SFARSMNNYA DYAATQLQYY GLKPDSAEYD 

       370        380        390        400        410        420 
GNGTVWTHYA VSKYLGGTDH ADPHGYLRSH NYSYDQLYDL INEKYLIKMG KVAPWGTQST 

       430        440        450        460        470        480 
TTPTTPSKPS TPSKPSTPST GKLTVAANNG VAQIKPTNSG LYTTVYDKTG KATNEVQKTF 

       490        500        510        520        530        540 
AVSKTATLGN QKFYLVQDYN SGNKFGWVKE GDVVYNTAKS PVNVNQSYSI KPGTKLYTVP 

       550        560        570        580        590        600 
WGTSKQVAGS VSGSGNQTFK ASKQQQIDKS IYLYGSVNGK SGWVSKAYLV DTAKPTPTPT 

       610        620        630        640        650        660 
PKPSTPTTNN KLTVSSLNGV AQINAKNNGL FTTVYDKTGK PTKEVQKTFA VTKEASLGGN 

       670        680        690        700        710        720 
KFYLVKDYNS PTLIGWVKQG DVIYNNAKSP VNVMQTYTVK PGTKLYSVPW GTYKQEAGAV 

       730        740        750        760        770        780 
SGTGNQTFKA TKQQQIDKSI YLYGTVNGKS GWISKAYLAV PAAPKKAVAQ PKTAVKAYAV 

       790        800        810        820        830        840 
TKPQTTQTVS KIAQVKPNNT GIRASVYEKT AKNGAKYADR TFYVTKERAH GNETYVLLNN 

       850        860        870        880        890        900 
TSHNIPLGWF NVKDLNVQNL GKEVKTTQKY TVNRSNNGLS MVPWGTKNQV ILTGNNIAQG 

       910        920        930        940        950        960 
TFNATKQVSV GKDVYLYGTI NNRTGWVNSK DLTAPTAVKP TTSAAKDYNY TYVIKNGNGY 

       970        980        990       1000       1010       1020 
YYVTPNSDTA KYSLKAFNEQ PFAVVKEQVI NGQTWYYGKL SNGKLAWIKS TDLAKELIKY 

      1030       1040       1050       1060       1070       1080 
NQIGMTLNQV AQIQAGLQYK PQVQRVPGKW TDANFNDVKH AMDTKRLAQD PALKYQFLRL 

      1090       1100       1110       1120       1130       1140 
DQPQNISIDK INQFLKGKGV LENQGAAFNK AAQMYGINEV YLISHALLET GNGTSQLAKG 

      1150       1160       1170       1180       1190       1200 
ADVVNNKVVT NSNTKYHNVF GIAAYDNDPL REGIKYAKQA GWDTVSKAIV GGAKFIGNSY 

      1210       1220       1230       1240       1250 
VKAGQNTLYK MRWNPAHPGT HQYATDVDWA NINAKIIKGY YDKIGEVGKY FDIPQYK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571856 Genomic DNA. Translation: CAG40030.1.
RefSeqYP_040441.1. NC_002952.2.

3D structure databases

ProteinModelPortalQ6GI31.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING282458.SAR1026.

Protein family/group databases

CAZyGH73. Glycoside Hydrolase Family 73.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG40030; CAG40030; SAR1026.
GeneID2859873.
KEGGsar:SAR1026.
PATRIC19545587. VBIStaAur71814_1024.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4193.
HOGENOMHOG000279968.
KOK13714.
OMAKSGWISK.
OrthoDBEOG6GXTN7.
ProtClustDBCLSK886177.

Enzyme and pathway databases

BioCycSAUR282458:GJA5-1027-MONOMER.

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_STAAR
AccessionPrimary (citable) accession number: Q6GI31
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: July 19, 2004
Last modified: November 13, 2013
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