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Q8NX96

- ATL_STAAW

UniProt

Q8NX96 - ATL_STAAW

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Protein
Bifunctional autolysin
Gene
atl, nag, MW0936
Organism
Staphylococcus aureus (strain MW2)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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 activityi

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.

GO - Molecular functioni

  1. N-acetylmuramoyl-L-alanine amidase activity Source: UniProtKB-EC
  2. amidase activity Source: InterPro
  3. mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall macromolecule metabolic process Source: InterPro
  2. peptidoglycan catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciSAUR196620:GJ9Z-960-MONOMER.

Protein family/group databases

CAZyiGH73. Glycoside Hydrolase Family 73.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional autolysin
Including the following 2 domains:
N-acetylmuramoyl-L-alanine amidase (EC:3.5.1.28)
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase (EC:3.2.1.96)
Gene namesi
Name:atl
Synonyms:nag
Ordered Locus Names:MW0936
OrganismiStaphylococcus aureus (strain MW2)
Taxonomic identifieri196620 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000418: Chromosome

Subcellular locationi

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.

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929 Reviewed prediction
Add
BLAST
Chaini30 – 12561227Bifunctional autolysin
PRO_0000045478Add
BLAST

Post-translational modificationi

Undergoes proteolytic processing to generate the two extracellular lytic enzymes, probably at the septal region on the cell surface By similarity.

Interactioni

Subunit structurei

Oligomer; forms a ring structure at the cell surface which is important for efficient partitioning of daughter cells after cell division By similarity.

Protein-protein interaction databases

STRINGi196620.MW0936.

Structurei

3D structure databases

ProteinModelPortaliQ8NX96.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati425 – 5891651
Add
BLAST
Repeati596 – 7581632
Add
BLAST
Repeati770 – 9321633
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni199 – 775577N-acetylmuramoyl-L-alanine amidase
Add
BLAST
Regioni776 – 1256481Endo-beta-N-acetylglucosaminidase
Add
BLAST

Domaini

The repeat domains R1, R2 and R3 are responsible for directing the proteins to the septal region By similarity.

Sequence similaritiesi

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.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG4193.
HOGENOMiHOG000279968.
KOiK13714.
OMAiKSGWISK.
OrthoDBiEOG6GXTN7.

Family and domain databases

Gene3Di3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR013338. Lysozyme_subfam2_dom.
IPR002901. MGlyc_endo_b_GlcNAc_like_dom.
[Graphical view]
PfamiPF01510. Amidase_2. 1 hit.
PF01832. Glucosaminidase. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
SM00047. LYZ2. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8NX96-1 [UniParc]FASTAAdd to Basket

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MAKKFNYKLP SMVALTLVGS AVTAHQVQAA ETTQDQTTNK NVLDSNKVKA     50
TTEQAKAEVK NPTQNISGTQ VYQDPAIVQP KTANNKTGNA QVSQKVDTAQ 100
VNGDTRANQS ATTNNTQPVA KSTSTTAPKT NTNVTNAGYS LVDDEDDNSE 150
NQINPELIKS AAKPAALETQ YKAAAPKAAT TSAPKAKTEA TPKVTTFSAS 200
AQPRSVAATP KTSLPKYKPQ VNSSINDYIR KNNLKAPKIE EDYTSYFPKY 250
AYRNGVGRPE GIVVHDTAND RSTINGEISY MKNNYQNAFV HAFVDGDRII 300
ETAPTDYLSW GVGAVGNPRF INVEIVHTHD YASFARSMNN YADYAATQLQ 350
YYGLKPDSAE YDGNGTVWTH YAVSKYLGGT DHADPHGYLR SHNYSYDQLY 400
DLINEKYLIK MGKVAPWGTQ STTTPTTPSK PTTPSKPSTG KLTVAANNGV 450
AQIKPTNSGL YTTVYDKTGK ATNEVQKTFA VSKTATLGNQ KFYLVQDYNS 500
GNKFGWVKEG DVVYNTAKSP VNVNQSYSIK PGTKLYTVPW GTSKQVAGSV 550
SGSGNQTFKA SKQQQIDKSI YLYGSVNGKS GWVSKAYLVD TAKPTPTPTP 600
KPSTPTTNNK LTVSSLNGVA QINAKNNGLF TTVYDKTGKP TKEVQKTFAV 650
TKEASLGGNK FYLVKDYNSP TLIGWVKQGD VIYNNAKSPV NVMQTYTVKP 700
GTKLYSVPWG TYKQEAGAVS GTGNQTFKAT KQQQIDKSIY LFGTVNGKSG 750
WVSKAYLAVP AAPKKAVAQP KTAVKAYTVT KPQTTQTVSK IAQVKPNNTG 800
IRASVYEKTA KNGAKYADRT FYVTKERAHG NETYVLLNNT SHNIPLGWFN 850
VKDLNVQNLG KEVKTTQKYT VNKSNNGLSM VPWGTKNQVI LTGNNIAQGT 900
FNATKQVSVG KDVYLYGTIN NRTGWVNAKD LTAPTAVKPT TSAAKDYNYT 950
YVIKNGNGYY YVTPNSDTAK YSLKAFNEQP FAVVKEQVIN GQTWYYGKLS 1000
NGKLAWIKST DLAKELIKYN QTGMTLNQVA QIQAGLQYKP QVQRVPGKWT 1050
DANFNDVKHA MDTKRLAQDP ALKYQFLRLD QPQNISIDKI NQFLKGKGVL 1100
ENQGAAFNKA AQMYGINEVY LISHALLETG NGTSQLAKGA DVVNNKVVTN 1150
SNTKYHNVFG IAAYDNDPLR EGIKYAKQAG WDTVSKAIVG GAKFIGNSYV 1200
KAGQNTLYKM RWNPAHPGTH QYATDIDWAN INAKIIKGYY DKIGEVGKYF 1250
DIPQYK 1256
Length:1,256
Mass (Da):137,407
Last modified:October 1, 2002 - v1
Checksum:iD4C2016EB269FD61
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000033 Genomic DNA. Translation: BAB94801.1.
RefSeqiNP_645753.1. NC_003923.1.

Genome annotation databases

EnsemblBacteriaiBAB94801; BAB94801; BAB94801.
GeneIDi1003048.
KEGGisam:MW0936.
PATRICi19568444. VBIStaAur44266_0981.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000033 Genomic DNA. Translation: BAB94801.1 .
RefSeqi NP_645753.1. NC_003923.1.

3D structure databases

ProteinModelPortali Q8NX96.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196620.MW0936.

Protein family/group databases

CAZyi GH73. Glycoside Hydrolase Family 73.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB94801 ; BAB94801 ; BAB94801 .
GeneIDi 1003048.
KEGGi sam:MW0936.
PATRICi 19568444. VBIStaAur44266_0981.

Phylogenomic databases

eggNOGi COG4193.
HOGENOMi HOG000279968.
KOi K13714.
OMAi KSGWISK.
OrthoDBi EOG6GXTN7.

Enzyme and pathway databases

BioCyci SAUR196620:GJ9Z-960-MONOMER.

Family and domain databases

Gene3Di 3.40.80.10. 1 hit.
InterProi IPR002502. Amidase_domain.
IPR013338. Lysozyme_subfam2_dom.
IPR002901. MGlyc_endo_b_GlcNAc_like_dom.
[Graphical view ]
Pfami PF01510. Amidase_2. 1 hit.
PF01832. Glucosaminidase. 1 hit.
[Graphical view ]
SMARTi SM00644. Ami_2. 1 hit.
SM00047. LYZ2. 1 hit.
[Graphical view ]
SUPFAMi SSF55846. SSF55846. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MW2.

Entry informationi

Entry nameiATL_STAAW
AccessioniPrimary (citable) accession number: Q8NX96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: October 1, 2002
Last modified: September 3, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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