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A7X0T9 (ATL_STAA1) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 41. 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:SAHV_1045
OrganismStaphylococcus aureus (strain Mu3 / ATCC 700698) [Complete proteome] [HAMAP]
Taxonomic identifier418127 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length1255 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. 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.

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 caution

The sequence BAF77928.1 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_0000313013

Regions

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

Sequences

Sequence LengthMass (Da)Tools
A7X0T9 [UniParc].

Last modified January 15, 2008. Version 2.
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

« Hide 'large scale' references
[1]"Mutated response regulator graR is responsible for phenotypic conversion of Staphylococcus aureus from heterogeneous vancomycin-intermediate resistance to vancomycin-intermediate resistance."
Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.
Antimicrob. Agents Chemother. 52:45-53(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Mu3 / ATCC 700698.
[2]"Genetic analysis of seventeen genes in Staphylococcus aureus with reduced susceptibility to vancomycin (VRSA) and heteroVRSA (hVRSA)."
Wootton M., Avison M.B., Bennett P.M., Howe R.A., MacGowan A.P., Walsh T.R.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 784-1255.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009324 Genomic DNA. Translation: BAF77928.1. Different initiation.
AJ567417 Genomic DNA. Translation: CAD98827.1.
RefSeqYP_001441635.1. NC_009782.1.

3D structure databases

ProteinModelPortalA7X0T9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING418127.SAHV_1045.

Protein family/group databases

CAZyGH73. Glycoside Hydrolase Family 73.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF77928; BAF77928; SAHV_1045.
GeneID5559758.
KEGGsaw:SAHV_1045.
PATRIC19557087. VBIStaAur127830_1062.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4193.
KOK13714.
OrthoDBEOG6GXTN7.
ProtClustDBCLSK886177.

Enzyme and pathway databases

BioCycSAUR418127:GJP9-1063-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_STAA1
AccessionPrimary (citable) accession number: A7X0T9
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: November 13, 2013
This is version 41 of the entry and version 2 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