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Protein

Bifunctional autolysin

Gene

atl

Organism
Staphylococcus aureus (strain COL)
Status
Reviewed-Annotation score: 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).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

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
Ordered Locus Names:SACOL1062
OrganismiStaphylococcus aureus (strain COL)
Taxonomic identifieri93062 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000530 Componenti: 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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Sequence analysisAdd BLAST29
ChainiPRO_000004547330 – 1256Bifunctional autolysinAdd BLAST1227

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

STRINGi93062.SACOL1062.

Structurei

3D structure databases

ProteinModelPortaliQ5HH31.
SMRiQ5HH31.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini443 – 517GW 1PROSITE-ProRule annotationAdd BLAST75
Domaini519 – 593GW 2PROSITE-ProRule annotationAdd BLAST75
Domaini612 – 686GW 3PROSITE-ProRule annotationAdd BLAST75
Domaini688 – 762GW 4PROSITE-ProRule annotationAdd BLAST75
Domaini784 – 859GW 5PROSITE-ProRule annotationAdd BLAST76
Domaini861 – 936GW 6PROSITE-ProRule annotationAdd BLAST76
Domaini943 – 1017GW 7PROSITE-ProRule annotationAdd BLAST75

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni199 – 775N-acetylmuramoyl-L-alanine amidaseAdd BLAST577
Regioni776 – 1256Endo-beta-N-acetylglucosaminidaseAdd BLAST481

Domaini

The GW domains 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.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.
HOGENOMiHOG000279968.
KOiK13714.
OMAiAYAVTKP.

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.

Q5HH31-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKKFNYKLP SMVALTLVGS AVTAHQVQAA ETTQDQTTNK NVLDSNKVKA
60 70 80 90 100
TTEQAKAEVK NPTQNISGTQ VYQDPAIVQP KTANNKTGNA QVSQKVDTAQ
110 120 130 140 150
VNGDTRANQS ATTNNTQPVA KSTSTTAPKT NTNVTNAGYS LVDDEDDNSE
160 170 180 190 200
NQINPELIKS AAKPAALETQ YKTAAPKAAT TSAPKAKTEA TPKVTTFSAS
210 220 230 240 250
AQPRSVAATP KTSLPKYKPQ VNSSINDYIR KNNLKAPKIE EDYTSYFPKY
260 270 280 290 300
AYRNGVGRPE GIVVHDTAND RSTINGEISY MKNNYQNAFV HAFVDGDRII
310 320 330 340 350
ETAPTDYLSW GVGAVGNPRF INVEIVHTHD YASFARSMNN YADYAATQLQ
360 370 380 390 400
YYGLKPDSAE YDGNGTVWTH YAVSKYLGGT DHADPHGYLR SHNYSYDQLY
410 420 430 440 450
DLINEKYLIK MGKVAPWGTQ STTTPTTPSK PTTPSKPSTG KLTVAANNGV
460 470 480 490 500
AQIKPTNSGL YTTVYDKTGK ATNEVQKTFA VSKTATLGNQ KFYLVQDYNS
510 520 530 540 550
GNKFGWVKEG DVVYNTAKSP VNVNQSYSIK PGTKLYTVPW GTSKQVAGSV
560 570 580 590 600
SGSGNQTFKA SKQQQIDKSI YLYGSVNGKS GWVSKAYLVD TAKPTPTPTP
610 620 630 640 650
KPSTPTTNNK LTVSSLNGVA QINAKNNGLF TTVYDKTGKP TKEVQKTFAV
660 670 680 690 700
TKEASLGGNK FYLVKDYNSP TLIGWVKQGD VIYNNAKSPV NVMQTYTVKP
710 720 730 740 750
GTKLYSVPWG TYKQEAGAVS GTGNQTFKAT KQQQIDKSIY LFGTVNGKSG
760 770 780 790 800
WVSKAYLAVP AAPKKAVAQP KTAVKAYTVT KPQTTQTVSK IAQVKPNNTG
810 820 830 840 850
IRASVYEKTA KNGAKYADRT FYVTKERAHG NETYVLLNNT SHNIPLGWFN
860 870 880 890 900
VKDLNVQNLG KEVKTTQKYT VNKSNNGLSM VPWGTKNQVI LTGNNIAQGT
910 920 930 940 950
FNATKQVSVG KDVYLYGTIN NRTGWVNAKD LTAPTAVKPT TSAAKDYNYT
960 970 980 990 1000
YVIKNGNGYY YVTPNSDTAK YSLKAFNEQP FAVVKEQVIN GQTWYYGKLS
1010 1020 1030 1040 1050
NGKLAWIKST DLAKELIKYN QTGMALNQVA QIQAGLQYKP QVQRVPGKWT
1060 1070 1080 1090 1100
GANFNDVKHA MDTKRLAQDP ALKYQFLRLD QPQNISIDKI NQFLKGKGVL
1110 1120 1130 1140 1150
ENQGAAFNKA AQMYGINEVY LISHALLETG NGTSQLAKGA DVVNNKVVTN
1160 1170 1180 1190 1200
SNTKYHNVFG IAAYDNDPLR EGIKYAKQAG WDTVSKAIVG GAKFIGNSYV
1210 1220 1230 1240 1250
KAGQNTLYKM RWNPAHPGTH QYATDVDWAN INAKIIKGYY DKIGEVGKYF

DIPQYK
Length:1,256
Mass (Da):137,335
Last modified:February 15, 2005 - v1
Checksum:i5167A617EFBB7D67
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000046 Genomic DNA. Translation: AAW36526.1.
RefSeqiWP_001074555.1. NC_002951.2.

Genome annotation databases

EnsemblBacteriaiAAW36526; AAW36526; SACOL1062.
KEGGisac:SACOL1062.
PATRICi19528358. VBIStaAur112458_1032.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000046 Genomic DNA. Translation: AAW36526.1.
RefSeqiWP_001074555.1. NC_002951.2.

3D structure databases

ProteinModelPortaliQ5HH31.
SMRiQ5HH31.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL1062.

Protein family/group databases

CAZyiGH73. Glycoside Hydrolase Family 73.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW36526; AAW36526; SACOL1062.
KEGGisac:SACOL1062.
PATRICi19528358. VBIStaAur112458_1032.

Phylogenomic databases

eggNOGiENOG4108FQ0. Bacteria.
COG4193. LUCA.
COG5632. LUCA.
HOGENOMiHOG000279968.
KOiK13714.
OMAiAYAVTKP.

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_STAAC
AccessioniPrimary (citable) accession number: Q5HH31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: February 15, 2005
Last modified: November 2, 2016
This is version 80 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

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.