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Protein

Bifunctional autolysin

Gene

atl

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 5 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.1 Publication

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

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
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 36Sequence analysisAdd BLAST36
ChainiPRO_000001211437 – 1255Bifunctional autolysinAdd BLAST1219

Post-translational modificationi

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

Interactioni

Subunit structurei

Oligomer; forms a ring structure at the cell surface which is important for efficient partitioning of daughter cells after cell division.1 Publication

Protein-protein interaction databases

STRINGi93062.SACOL1062.

Structurei

3D structure databases

ProteinModelPortaliP0C5Z8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini442 – 516GW 1PROSITE-ProRule annotationAdd BLAST75
Domaini518 – 592GW 2PROSITE-ProRule annotationAdd BLAST75
Domaini611 – 685GW 3PROSITE-ProRule annotationAdd BLAST75
Domaini687 – 761GW 4PROSITE-ProRule annotationAdd BLAST75
Domaini783 – 858GW 5PROSITE-ProRule annotationAdd BLAST76
Domaini860 – 935GW 6PROSITE-ProRule annotationAdd BLAST76
Domaini942 – 1016GW 7PROSITE-ProRule annotationAdd BLAST75

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni199 – 775N-acetylmuramoyl-L-alanine amidaseAdd BLAST577
Regioni776 – 1255Endo-beta-N-acetylglucosaminidaseAdd BLAST480

Domaini

The GW domains are responsible for directing the proteins to the septal region.1 Publication

Sequence similaritiesi

In the N-terminal section; belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.Curated
In the C-terminal section; belongs to the glycosyl hydrolase 73 family.Curated
Contains 7 GW domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4108FQ0. Bacteria.
COG4193. LUCA.
COG5632. LUCA.

Family and domain databases

CDDicd06583. PGRP. 1 hit.
Gene3Di3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR002901. MGlyc_endo_b_GlcNAc-like_dom.
IPR025987. SH3-like_dom.
[Graphical view]
PfamiPF01832. Glucosaminidase. 1 hit.
PF13457. SH3_8. 6 hits.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
SM00047. LYZ2. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.
PROSITEiPS51780. GW. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0C5Z8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGVINRMAK KFNYKLPSMV ALTLVGSAVT AHQVQAAETT QDQTTNKNVL
60 70 80 90 100
DSNKVKATTE QAKAEVKNPT QNISGTQVYQ DPAIVQPKTA NNKTGNAQVS
110 120 130 140 150
QKVDTAQVNG DTRANQSATT NNTQPVAKST STTAPKTNTN VTNAGYSLVD
160 170 180 190 200
DEDDNSEHQI NPELIKSAAK PAALETQYKA AAPKAKTEAT PKVTTFSASA
210 220 230 240 250
QPRSVAATPK TSLPKYKPQV NSSINDYIRK NNLKAPKIEE DYTSYFPKYA
260 270 280 290 300
YRNGVGRPEG IVVHDTANDR STINGEISYM KNNYQNAFVH AFVDGDRIIE
310 320 330 340 350
TAPTDYLSWG VGAVGNPRFI NVEIVHTHDY ASFARSMNNY ADYAATQLQY
360 370 380 390 400
YGLKPDSAEY DGNGTVWTHY AVSKYLGGTD HADPHGYLRS HNYSYDQLYD
410 420 430 440 450
LINEKYLIKM GKVAPWGTQF TTTPTTPSKP TTPSKPSTGK LTVAANNGVA
460 470 480 490 500
QIKPTNSGLY TTVYDKTGKA TNEVQKTFAV SKTATLGNQK FYLVQDYNSG
510 520 530 540 550
NKFGWVKEGD VVYNTAKSPV NVNQSYSIKS GTKLYTVPWG TSKQVAGSVS
560 570 580 590 600
GSGNQTFKAS KQQQIDKSIY LYGSVNGKSG WVSKAYLVDT AKPTPTPIPK
610 620 630 640 650
PSTPTTNNKL TVSSLNGVAQ INAKNNGLFT TVYDKTGKPT KEVQKTFAVT
660 670 680 690 700
KEASLGGNKF YLVKDYNSPT LIGWVKQGDV IYNNAKSPVN VMQTYTVKPG
710 720 730 740 750
TKLYSVPWGT YKQEAGAVSG TGNQTFKATK QQQIDKSIYL FGTVNGKSGW
760 770 780 790 800
VSKAYLAVPA APKKAVAQPK TAVKAYTVTK PQTTQTVSKI AQVKPNNTGI
810 820 830 840 850
RASVYEKTAK NGAKYADRTF YVTKERAHGN ETYVLLNNTS HNIPLGWFNV
860 870 880 890 900
KDLNVQNLGK EVKTTQKYTV NKSNNGLSMV PWGTKNQVIL TGNNIAQGTF
910 920 930 940 950
NATKQVSVGK DVYLYGTINN RTGWVNAKDL TAPTAVKPTT SAAKDYNYTY
960 970 980 990 1000
VIKNGNGYYY VTPNSDTAKY SLKAFNEQPF AVVKEQVING QTWYYGKLSN
1010 1020 1030 1040 1050
GKLAWIKSTD LAKELIKYNQ TGMTLNQVAQ IQAGLQYKPQ VQRVPGKWTD
1060 1070 1080 1090 1100
ANFNDVKHAM DTKRLAQDPA LKYQFLRLDQ PQNISIDKIN QFLKGKGVLE
1110 1120 1130 1140 1150
NQGAAFNKAA QMYGINEVYL ISHALLETGN GTSQLAKGAD VVNNKVVTNS
1160 1170 1180 1190 1200
NTKYHNVFGI AAYDNDPLRE GIKYAKQAGW DTVSKAIVGG AKFIGNSYVK
1210 1220 1230 1240 1250
AGQNTLYKMR WNPAHPGTHQ YATDVDWANI NAKIIKGYYD KIGEVGKYFD

IPQYK
Length:1,255
Mass (Da):137,535
Last modified:January 15, 2008 - v1
Checksum:i7257DD87168AAE7D
GO

Sequence cautioni

The sequence AAP44166 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti932A → R in BAA22600 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF537210 Genomic DNA. Translation: AAP44166.1. Different initiation.
D42078 Genomic DNA. Translation: BAA22600.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF537210 Genomic DNA. Translation: AAP44166.1. Different initiation.
D42078 Genomic DNA. Translation: BAA22600.1.

3D structure databases

ProteinModelPortaliP0C5Z8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL1062.

Protein family/group databases

CAZyiGH73. Glycoside Hydrolase Family 73.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108FQ0. Bacteria.
COG4193. LUCA.
COG5632. LUCA.

Family and domain databases

CDDicd06583. PGRP. 1 hit.
Gene3Di3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR002901. MGlyc_endo_b_GlcNAc-like_dom.
IPR025987. SH3-like_dom.
[Graphical view]
PfamiPF01832. Glucosaminidase. 1 hit.
PF13457. SH3_8. 6 hits.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
SM00047. LYZ2. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.
PROSITEiPS51780. GW. 7 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATL_STAAU
AccessioniPrimary (citable) accession number: P0C5Z8
Secondary accession number(s): O32391
, P0C1R4, P52081, Q7WTC6, Q7WY94, Q7WY95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: October 5, 2016
This is version 48 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

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.