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Q2FZK7 (ATL_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 56. 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:SAOUHSC_00994
OrganismStaphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP]
Taxonomic identifier93061 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length1256 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 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 – 12561227Bifunctional autolysin
PRO_0000247668

Regions

Repeat425 – 5891651
Repeat596 – 7581632
Repeat770 – 9321633
Region199 – 775577N-acetylmuramoyl-L-alanine amidase
Region776 – 1256481Endo-beta-N-acetylglucosaminidase

Sequences

Sequence LengthMass (Da)Tools
Q2FZK7 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 2BB76CAA292FDD20

FASTA1,256137,384
        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 YKTAAPKAAT 

       190        200        210        220        230        240 
TSAPKAKTEA TPKVTTFSAS AQPRSVAATP KTSLPKYKPQ VNSSINDYIC 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 PTTPSKPSTG KLTVAANNGV AQIKPTNSGL YTTVYDKTGK ATNEVQKTFA 

       490        500        510        520        530        540 
VSKTATLGNQ KFYLVQDYNS GNKFGWVKEG DVVYNTAKSP VNVNQSYSIK PGTKLYTVPW 

       550        560        570        580        590        600 
GTSKQVAGSV SGSGNQTFKA SKQQQIDKSI YLYGSVNGKS GWVSKAYLVD TAKPTPTPTP 

       610        620        630        640        650        660 
KPSTPTTNNK LTVSSLNGVA QINAKNNGLF TTVYDKTGKP TKEVQKTFAV TKEASLGGNK 

       670        680        690        700        710        720 
FYLVKDYNSP TLIGWVKQGD VIYNNAKSPV NVMQTYTVKP GTKLYSVPWG TYKQEAGAVS 

       730        740        750        760        770        780 
GTGNQTFKAT KQQQIDKSIY LFGTVNGKSG WVSKAYLAVP AAPKKAVAQP KTAVKAYTVT 

       790        800        810        820        830        840 
KPQTTQTVSK IAQVKPNNTG IRASVYEKTA KNGAKYADRT FYVTKERAHG NETYVLLNNT 

       850        860        870        880        890        900 
SHNIPLGWFN VKDLNVQNLG KEVKTTQKYT VNKSNNGLSM VPWGTKNQVI LTGNNIAQGT 

       910        920        930        940        950        960 
FNATKQVSVG KDVYLYGTIN NRTGWVNAKD LTAPTAVKPT TSAAKDYNYT YVIKNGNGYY 

       970        980        990       1000       1010       1020 
YVTPNSDTAK YSLKAFNEQP FAVVKEQVIN GQTWYYGKLS NGKLAWIKST DLAKELIKYN 

      1030       1040       1050       1060       1070       1080 
QTGMTLNQVA QIQAGLQYKP QVQRVPGKWT DAKFNDVKHA MDTKRLAQDP ALKYQFLRLD 

      1090       1100       1110       1120       1130       1140 
QPQNISIDKI NQFLKGKGVL ENQGAAFNKA AQMYGINEVY LISHALLETG NGTSQLAKGA 

      1150       1160       1170       1180       1190       1200 
DVVNNKVVTN SNTKYHNVFG IAAYDNDPLR EGIKYAKQAG WDTVSKAIVG GAKFIGNSYV 

      1210       1220       1230       1240       1250 
KAGQNTLYKM RWNPAHPGTH QYATDVDWAN INAKIIKGYY DKIGEVGKYF DIPQYK 

« Hide

References

« Hide 'large scale' references
[1]"A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-beta-N-acetylglucosaminidase domain: cloning, sequence analysis, and characterization."
Oshida T., Sugai M., Komatsuzawa H., Hong Y.-M., Suginaka H., Tomasz A.
Proc. Natl. Acad. Sci. U.S.A. 92:285-289(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 205-214 AND 776-792.
[2]Foster S.J.
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The Staphylococcus aureus NCTC8325 genome."
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 8325.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D17366 Genomic DNA. Translation: BAA04185.1.
L41499 Genomic DNA. Translation: AAA99982.1.
CP000253 Genomic DNA. Translation: ABD30118.1.
RefSeqYP_499546.1. NC_007795.1.

3D structure databases

ProteinModelPortalQ2FZK7.
SMRQ2FZK7. Positions 212-418, 441-584, 608-753.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93061.SAOUHSC_00994.

Protein family/group databases

CAZyGH73. Glycoside Hydrolase Family 73.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD30118; ABD30118; SAOUHSC_00994.
GeneID3920394.
KEGGsao:SAOUHSC_00994.
PATRIC19579507. VBIStaAur99865_0912.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSAUR93061:GIWJ-959-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_STAA8
AccessionPrimary (citable) accession number: Q2FZK7
Secondary accession number(s): O32391 expand/collapse secondary AC list , P52081, Q7WTC6, Q7WY94, Q7WY95
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 21, 2006
Last modified: November 13, 2013
This is version 56 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