SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q99V41

- ATL_STAAN

UniProt

Q99V41 - ATL_STAAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Bifunctional autolysin

Gene
atl, nag, SA0905
Organism
Staphylococcus aureus (strain N315)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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

BioCyciSAUR158879:GJCB-957-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:SA0905
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000751: 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 predictionAdd
BLAST
Chaini30 – 12481219Bifunctional autolysinPRO_0000045475Add
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

STRINGi158879.SA0905.

Structurei

3D structure databases

ProteinModelPortaliQ99V41.
SMRiQ99V41. Positions 204-410, 433-576, 600-745, 935-1006, 1097-1231.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati417 – 5811651Add
BLAST
Repeati588 – 7501632Add
BLAST
Repeati762 – 9241633Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 767577N-acetylmuramoyl-L-alanine amidaseAdd
BLAST
Regioni768 – 1248481Endo-beta-N-acetylglucosaminidaseAdd
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.

Q99V41-1 [UniParc]FASTAAdd to Basket

« Hide

MAKKFNYKLP SMVALTLVGS AVTAHQVQAA ETTQDQTTNK NVLDSNKVKA     50
TTEQAKAEVK NPTQNISGTQ VYQDPAIVQP KTANNKTGNA QVSQKVDTAQ 100
VNGDTRANQS ATTNNTQPVA KSTSTTAPKT NTNVTNAGYS LVDDEDDNSE 150
HQINPELIKS AAKPAALETQ YKAAAPKAKT EATPKVTTFS ASAQPRSVAA 200
TPKTSLPKYK PQVNSSINDY IRKNNLKAPK IEEDYTSYFP KYAYRNGVGR 250
PEGIVVHDTA NDRSTINGEI SYMKNNYQNA FVHAFVDGDR IIETAPTDYL 300
SWGVGAVGNP RFINVEIVHT HDYASFARSM NNYADYAATQ LQYYGLKPDS 350
AEYDGNGTVW THYAVSKYLG GTDHADPHGY LRSHNYSYDQ LYDLINEKYL 400
IKMGKVAPWG TQFTTTPTTP SKPTTPSKPS TGKLTVAANN GVAQIKPTNS 450
GLYTTVYDKT GKATNEVQKT FAVSKTATLG NQKFYLVQDY NSGNKFGWVK 500
EGDVVYNTAK SPVNVNQSYS IKSGTKLYTV PWGTSKQVAG SVSGSGNQTF 550
KASKQQQIDK SIYLYGSVNG KSGWVSKAYL VDTAKPTPTP IPKPSTPTTN 600
NKLTVSSLNG VAQINAKNNG LFTTVYDKTG KPTKEVQKTF AVTKEASLGG 650
NKFYLVKDYN SPTLIGWVKQ GDVIYNNAKS PVNVMQTYTV KPGTKLYSVP 700
WGTYKQEAGA VSGTGNQTFK ATKQQQIDKS IYLFGTVNGK SGWVSKAYLA 750
VPAAPKKAVA QPKTAVKAYT VTKPQTTQTV SKIAQVKPNN TGIRASVYEK 800
TAKNGAKYAD RTFYVTKERA HGNETYVLLN NTSHNIPLGW FNVKDLNVQN 850
LGKEVKTTQK YTVNKSNNGL SMVPWGTKNQ VILTGNNIAQ GTFNATKQVS 900
VGKDVYLYGT INNRTGWVNA KDLTAPTAVK PTTSAAKDYN YTYVIKNGNG 950
YYYVTPNSDT AKYSLKAFNE QPFAVVKEQV INGQTWYYGK LSNGKLAWIK 1000
STDLAKELIK YNQTGMTLNQ VAQIQAGLQY KPQVQRVPGK WTDANFNDVK 1050
HAMDTKRLAQ DPALKYQFLR LDQPQNISID KINQFLKGKG VLENQGAAFN 1100
KAAQMYGINE VYLISHALLE TGNGTSQLAK GADVVNNKVV TNSNTKYHNV 1150
FGIAAYDNDP LREGIKYAKQ AGWDTVSKAI VGGAKFIGNS YVKAGQNTLY 1200
KMRWNPAHPG THQYATDVDW ANINAKIIKG YYDKIGEVGK YFDIPQYK 1248
Length:1,248
Mass (Da):136,751
Last modified:June 1, 2001 - v1
Checksum:i701B54EE6152275E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000018 Genomic DNA. Translation: BAB42150.1.
PIRiC89874.
RefSeqiNP_374172.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB42150; BAB42150; BAB42150.
GeneIDi1123728.
KEGGisau:SA0905.
PATRICi19573994. VBIStaAur116463_0967.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000018 Genomic DNA. Translation: BAB42150.1 .
PIRi C89874.
RefSeqi NP_374172.1. NC_002745.2.

3D structure databases

ProteinModelPortali Q99V41.
SMRi Q99V41. Positions 204-410, 433-576, 600-745, 935-1006, 1097-1231.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 158879.SA0905.

Protein family/group databases

CAZyi GH73. Glycoside Hydrolase Family 73.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB42150 ; BAB42150 ; BAB42150 .
GeneIDi 1123728.
KEGGi sau:SA0905.
PATRICi 19573994. VBIStaAur116463_0967.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SAUR158879:GJCB-957-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: N315.
  2. "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
    Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
    Submitted (OCT-2007) to UniProtKB
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: N315.

Entry informationi

Entry nameiATL_STAAN
AccessioniPrimary (citable) accession number: Q99V41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 79 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

Similar proteinsi