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

Q931U5 (ATL_STAAM) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 72. 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:SAV1052
OrganismStaphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]
Taxonomic identifier158878 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length1248 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 – 12481219Bifunctional autolysin
PRO_0000045474

Regions

Repeat417 – 5811651
Repeat588 – 7501632
Repeat762 – 9241633
Region191 – 767577N-acetylmuramoyl-L-alanine amidase By similarity
Region768 – 1248481Endo-beta-N-acetylglucosaminidase By similarity

Sequences

Sequence LengthMass (Da)Tools
Q931U5 [UniParc].

Last modified July 5, 2004. Version 2.
Checksum: 701B54EE6152275E

FASTA1,248136,751
        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 HQINPELIKS AAKPAALETQ YKAAAPKAKT 

       190        200        210        220        230        240 
EATPKVTTFS ASAQPRSVAA TPKTSLPKYK PQVNSSINDY IRKNNLKAPK IEEDYTSYFP 

       250        260        270        280        290        300 
KYAYRNGVGR PEGIVVHDTA NDRSTINGEI SYMKNNYQNA FVHAFVDGDR IIETAPTDYL 

       310        320        330        340        350        360 
SWGVGAVGNP RFINVEIVHT HDYASFARSM NNYADYAATQ LQYYGLKPDS AEYDGNGTVW 

       370        380        390        400        410        420 
THYAVSKYLG GTDHADPHGY LRSHNYSYDQ LYDLINEKYL IKMGKVAPWG TQFTTTPTTP 

       430        440        450        460        470        480 
SKPTTPSKPS TGKLTVAANN GVAQIKPTNS GLYTTVYDKT GKATNEVQKT FAVSKTATLG 

       490        500        510        520        530        540 
NQKFYLVQDY NSGNKFGWVK EGDVVYNTAK SPVNVNQSYS IKSGTKLYTV PWGTSKQVAG 

       550        560        570        580        590        600 
SVSGSGNQTF KASKQQQIDK SIYLYGSVNG KSGWVSKAYL VDTAKPTPTP IPKPSTPTTN 

       610        620        630        640        650        660 
NKLTVSSLNG VAQINAKNNG LFTTVYDKTG KPTKEVQKTF AVTKEASLGG NKFYLVKDYN 

       670        680        690        700        710        720 
SPTLIGWVKQ GDVIYNNAKS PVNVMQTYTV KPGTKLYSVP WGTYKQEAGA VSGTGNQTFK 

       730        740        750        760        770        780 
ATKQQQIDKS IYLFGTVNGK SGWVSKAYLA VPAAPKKAVA QPKTAVKAYT VTKPQTTQTV 

       790        800        810        820        830        840 
SKIAQVKPNN TGIRASVYEK TAKNGAKYAD RTFYVTKERA HGNETYVLLN NTSHNIPLGW 

       850        860        870        880        890        900 
FNVKDLNVQN LGKEVKTTQK YTVNKSNNGL SMVPWGTKNQ VILTGNNIAQ GTFNATKQVS 

       910        920        930        940        950        960 
VGKDVYLYGT INNRTGWVNA KDLTAPTAVK PTTSAAKDYN YTYVIKNGNG YYYVTPNSDT 

       970        980        990       1000       1010       1020 
AKYSLKAFNE QPFAVVKEQV INGQTWYYGK LSNGKLAWIK STDLAKELIK YNQTGMTLNQ 

      1030       1040       1050       1060       1070       1080 
VAQIQAGLQY KPQVQRVPGK WTDANFNDVK HAMDTKRLAQ DPALKYQFLR LDQPQNISID 

      1090       1100       1110       1120       1130       1140 
KINQFLKGKG VLENQGAAFN KAAQMYGINE VYLISHALLE TGNGTSQLAK GADVVNNKVV 

      1150       1160       1170       1180       1190       1200 
TNSNTKYHNV FGIAAYDNDP LREGIKYAKQ AGWDTVSKAI VGGAKFIGNS YVKAGQNTLY 

      1210       1220       1230       1240 
KMRWNPAHPG THQYATDVDW ANINAKIIKG YYDKIGEVGK YFDIPQYK 

« Hide

References

« Hide 'large scale' references
[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Mu50 / ATCC 700699.
[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 785-1248.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000017 Genomic DNA. Translation: BAB57214.2.
AJ567416 Genomic DNA. Translation: CAD98826.1.
RefSeqNP_371576.2. NC_002758.2.

3D structure databases

ProteinModelPortalQ931U5.
SMRQ931U5. Positions 204-410, 433-576, 600-745, 935-1006, 1097-1231.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING158878.SAV1052.

Protein family/group databases

CAZyGH73. Glycoside Hydrolase Family 73.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB57214; BAB57214; SAV1052.
GeneID1121029.
KEGGsav:SAV1052.
PATRIC19562801. VBIStaAur52173_1079.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSAUR158878:GJJ5-1072-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_STAAM
AccessionPrimary (citable) accession number: Q931U5
Secondary accession number(s): Q7WY94, Q7WY95
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: July 5, 2004
Last modified: November 13, 2013
This is version 72 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