Reviewed, UniProtKB/Swiss-Prot O33635 (ATL_STAEP)

Names and origin

Protein names

Recommended name:
    Bifunctional autolysin
Alternative name(s):
    AtlE
Including the following 2 domains:
    1- Recommended name:
            N-acetylmuramoyl-L-alanine amidase
              EC=3.5.1.28
    2- Recommended name:
            Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
              EC=3.2.1.96

Gene names

Name:	atl
Synonyms:	atlE

Organism

Staphylococcus epidermidis

Taxonomic identifier

1282 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	1335 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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. As a bacterial surface-associated protein, mediates attachment to polystyrene surfaces, contributing to biofilm formation. Has also vitronectin-binding activity.
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. 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. Ref.1
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.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Secreted
Domain	Repeat Signal
Molecular function	Hydrolase
Technical term	Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	cellular cell wall macromolecule metabolic process Inferred from electronic annotation. Source: InterPro cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N-acetylmuramoyl-L-alanine amidase activity Inferred from electronic annotation. Source: EC amidase activity Inferred from electronic annotation. Source: InterPro mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 29	29	Potential
	Chain	30 – 1335	1306	Bifunctional autolysin		PRO_0000045479
Regions
	Repeat	516 – 681	166	1
	Repeat	682 – 845	164	2
	Repeat	846 – 1015	170	3
	Region	303 – 863	561	N-acetylmuramoyl-L-alanine amidase
	Region	864 – 1335	472	Endo-beta-N-acetylglucosaminidase

Sequences

	Sequence		Length	Mass (Da)
	O33635-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 0D8986BCB3DFF0A2	FASTA	1,335	148,273
	10 20 30 40 50 60 MAKKFNYKLP SMVALTLFGT AFTAHQANAA EQPQNQSNHK NVLDDQTALK QAEKAKSEVT 70 80 90 100 110 120 QSTTNVSGTQ TYQDPTQVQP KQDTQSTTYD ASLDEMSTYN EISSNQKQQS LSTDDANQNQ 130 140 150 160 170 180 TNSVTKNQQE ETNDLTQEDK TSTDTNQLQE TQSVAKENEK DLGANANNEQ QDKKMTASQP 190 200 210 220 230 240 SENQAIETQT ASNDNESQQK SQQVTSEQNE TATPKVSNTN ASGYNFDYDD EDDDSSTDHL 250 260 270 280 290 300 EPISLNNVNA TSKQTTSYKY KEPAQRVTTN TVKKETASNQ ATIDTKQFTP FSATAQPRTV 310 320 330 340 350 360 YSVSSQKTSS LPKYTPKVNS SINNYIRKKN MKAPRIEEDY TSYFPKYGYR NGVGRPEGIV 370 380 390 400 410 420 VHDTANDNST IDGEIAFMKR NYTNAFVHAF VDGNRIIETA PTDYLSWGAG PYGNQRFINV 430 440 450 460 470 480 EIVHTHDYDS FARSMNNYAD YAATQLQYYN LKPDSAENDG RGTVWTHAAI SNFLGGTDHA 490 500 510 520 530 540 DPHQYLRSHN YSYAELYDLI YEKYLIKTKQ VAPWGTTSTK PSQPSKPSGG TNNKLTVSAN 550 560 570 580 590 600 RGVAQIKPTN NGLYTTVYDS KGHKTDQVQK TLSVTKTATL GNNKFYLVED YNSGKKYGWV 610 620 630 640 650 660 KQGDVVYNTA KAPVKVNQTY NVKAGSTLYT VPWGTPKQVA SKVSGTGNQT FKATKQQQID 670 680 690 700 710 720 KATYLYGTVN GKSGWISKYY LTTASKPSNP TKPSTNNQLT VTNNSGVAQI NAKNSGLYTT 730 740 750 760 770 780 VYDTKGKTTN QIQRTLSVTK AATLGDKKFY LVGDYNTGTN YGWVKQDEVI YNTAKSPVKI 790 800 810 820 830 840 NQTYNVKPGV KLHTVPWGTY NQVAGTVSGK GDQTFKATKQ QQIDKATYLY GTVNGKSGWI 850 860 870 880 890 900 SKYYLTAPSK VQALSTQSTP APKQVKPSTQ TVNQIAQVKA NNSGIRASVY DKTAKSGTKY 910 920 930 940 950 960 ANRTFLINKQ RTQGNNTYVL LQDGTSNTPL GWVNINDVTT QNIGKQTQSI GKYSVKPTNN 970 980 990 1000 1010 1020 GLYSIAWGTK NQQLLAPNTL ANQAFNASKA VYVGKDLYLY GTVNNRTGWI AAKDLIQNST 1030 1040 1050 1060 1070 1080 DAQSTPYNYT FVINNSKSYF YMDPTKANRY SLKPYYEQTF TVIKQKNING VKWYYGQLLD 1090 1100 1110 1120 1130 1140 GKYVWIKSTD LVKEKIKYAY TGMTLNNAIN IQSRLKYKPQ VQNEPLKWSN ANYSQIKNAM 1150 1160 1170 1180 1190 1200 DTKRLANDSS LKYQFLRLDQ PQYLSAQALN KLLKGKGVLE NQGAAFSQAA RKYGLNEIYL 1210 1220 1230 1240 1250 1260 ISHALVETGN GTSQLAKGGD VSKGKFTTKT GHKYHNVFGI GAFDNNALVD GIKYAKNAGW 1270 1280 1290 1300 1310 1320 TSVSKAIIGG AKFIGNSYVK AGQNTLYKMR WNPANPGTHQ YATDINWANV NAQVLKQFYD 1330 KIGEVGKYFE IPTYK

References

[1]

"Evidence for autolysin-mediated primary attachment of Staphylococcus epidermidis to a polystyrene surface." Heilmann C., Hussain M., Peters G., Goetz F. Mol. Microbiol. 24:1013-1024(1997) [PubMed: 9220008] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 303-312, SUBCELLULAR LOCATION, INVOLVEMENT IN BIOFILM FORMATION. Strain: O47.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U71377 Genomic DNA. Translation: AAB63571.1.
PIR	T30211.
3D structure databases
SMR	O33635. Positions 347-488.
ModBase	Search...
Protein family/group databases
CAZy	GH73. Glycoside Hydrolase Family 73.
Enzyme and pathway databases
BRENDA	3.2.1.96. 874. 3.5.1.28. 874.
Family and domain databases
InterPro	IPR002502. Amidase_2. IPR013338. Lysozyme_dom_subfam2. IPR002901. Mano_Glyc_endo_b_GlcNAc. [Graphical view]
Pfam	PF01510. Amidase_2. 1 hit. PF01832. Glucosaminidase. 1 hit. [Graphical view]
SMART	SM00644. Ami_2. 1 hit. SM00047. LYZ2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATL_STAEP

Accession

Primary (citable) accession number: O33635

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	January 1, 1998
Last modified:	January 19, 2010
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)